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Conserved domains on  [gi|204138|gb|AAA41157|]
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fibroblast growth factor receptor subtype 4 [Rattus sp.]

Protein Classification

protein kinase family protein( domain architecture ID 229507)

protein kinase family protein containing immunoglobulin (Ig) domains, may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
302-615 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05099:

Pssm-ID: 451246 [Multi-domain]  Cd Length: 314  Bit Score: 688.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05099   1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05099  81 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05099 161 AARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPN 615
Cdd:cd05099 241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVLAAVSEEYLDLSMPFEQYSPS 314
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
95-197 2.35e-58

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05858:

Pssm-ID: 448366  Cd Length: 105  Bit Score: 191.33  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    95 PILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKHIVINGSSLGADGFPYVQVLKTTDINSS--EVEVLYLRNVSAE 172
Cdd:cd05858   1 PILQAGLPANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVEVLKTAGVNTTdkEIEVLYLRNVTFE 80
                        90       100
                ....*....|....*....|....*
gi 204138   173 DAGEYTCLAGNSIGLSYQSAWLTVL 197
Cdd:cd05858  81 DAGEYTCLAGNSIGISHHSAWLTVL 105
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
1-87 1.22e-50

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05857:

Pssm-ID: 448366 [Multi-domain]  Cd Length: 95  Bit Score: 170.42  E-value: 1.22e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     1 MEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIR 80
Cdd:cd05857   9 MEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSIN 88

                ....*..
gi 204138    81 YSYLLDV 87
Cdd:cd05857  89 HTYHLDV 95
 
Name Accession Description Interval E-value
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
302-615 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 688.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05099   1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05099  81 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05099 161 AARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPN 615
Cdd:cd05099 241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVLAAVSEEYLDLSMPFEQYSPS 314
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
315-591 2.09e-142

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 414.59  E-value: 2.09e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     315 LVLGKPLGEGCFGQVVCAEALGMDSsrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGE---NTKIKVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     395 YVIVEYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRK---------------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     475 KIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:pfam07714 142 KISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLEDGY 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 204138     555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:pfam07714 222 RLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
315-591 1.28e-138

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 405.01  E-value: 1.28e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      315 LVLGKPLGEGCFGQVVCAEALGMDSSRPDQtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVE---VAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      395 YVIVEYAAKGNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKE--------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      475 KIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:smart00221 143 KISDFGLSRDLYDDDYYKV-KGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGY 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 204138      555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:smart00221 222 RLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
95-197 2.35e-58

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 191.33  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    95 PILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKHIVINGSSLGADGFPYVQVLKTTDINSS--EVEVLYLRNVSAE 172
Cdd:cd05858   1 PILQAGLPANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVEVLKTAGVNTTdkEIEVLYLRNVTFE 80
                        90       100
                ....*....|....*....|....*
gi 204138   173 DAGEYTCLAGNSIGLSYQSAWLTVL 197
Cdd:cd05858  81 DAGEYTCLAGNSIGISHHSAWLTVL 105
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
1-87 1.22e-50

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 170.42  E-value: 1.22e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     1 MEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIR 80
Cdd:cd05857   9 MEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSIN 88

                ....*..
gi 204138    81 YSYLLDV 87
Cdd:cd05857  89 HTYHLDV 95
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
317-567 1.03e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 121.39  E-value: 1.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdssrpdQTSIVAVKMLKDNASDKDLAD--LISEMEMMKLIGRHKNIINLLGVCTQEGPL 394
Cdd:COG0515   4 ILRKLGEGSFGEVYLAR----------DRKLVALKVLAKKLESKSKEVerFLREIQILASLNHPPNIVKLYDFFQDEGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRarrppgpdlspdgPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:COG0515  74 YLVMEYVDGGSLEDLLK-------------KIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 -KIADFGLARGV------HHIDYYKKTSNGRLPvkWMAPEAL---FDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVE 544
Cdd:COG0515 141 vKLIDFGLAKLLpdpgstSSIPALPSTSVGTPG--YMAPEVLlglSLAYASSSSDIWSLGITLYELLT-GLPPFEGEKNS 217
                       250       260
                ....*....|....*....|...
gi 204138   545 ELFSLLREGHRMERPPNCPSELY 567
Cdd:COG0515 218 SATSQTLKIILELPTPSLASPLS 240
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
317-540 2.70e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 86.35  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    317 LGKPLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLAD-------------LISEMEMMKLIgRHKNIIN 383
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGK-------IVAIKKVKIIEISNDVTKdrqlvgmcgihftTLRELKIMNEI-KHENIMG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    384 LLGVCTQEGPLYVIVEYAAkGNLREFLRARrppgpdlspdgPRSSEgplsfpALVSC-AYQVARGMQYLESRKCIHRDLA 462
Cdd:PTZ00024  85 LVDVYVEGDFINLVMDIMA-SDLKKVVDRK-----------IRLTE------SQVKCiLLQILNGLNVLHKWYFMHRDLS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    463 ARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVK-----------WM-APEALF-DRVYTHQSDVWSFGILLWE 529
Cdd:PTZ00024 147 PANIFINSKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYrAPELLMgAEKYHFAVDMWSVGCIFAE 226
                        250
                 ....*....|..
gi 204138    530 IftLGGSP-YPG 540
Cdd:PTZ00024 227 L--LTGKPlFPG 236
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8-87 3.99e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.69  E-value: 3.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138        8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:smart00410   6 VKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
102-196 4.30e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 4.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKHiviNGSSLGADGfpyvqvlKTTDINSSEVEVLYLRNVSAEDAGEYTCLA 181
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQ---GGKLLAESG-------RFSVSRSGSTSTLTISNVTPEDSGTYTCAA 70
                           90
                   ....*....|....*
gi 204138      182 GNSIGLSYQSAWLTV 196
Cdd:smart00410  71 TNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
7-78 2.72e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 65.74  E-value: 2.72e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138       7 AVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIgGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGS 78
Cdd:pfam07679  11 EVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRF-KVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
348-540 4.24e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 69.05  E-value: 4.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    348 VAVKMLKDN-ASDKDL-----------ADLIsememmkligrHKNIINLLGVcTQEGPLYVIV-EYAAKGNLREFLRarr 414
Cdd:NF033483  35 VAVKVLRPDlARDPEFvarfrreaqsaASLS-----------HPNIVSVYDV-GEDGGIPYIVmEYVDGRTLKDYIR--- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    415 ppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLAR----------- 483
Cdd:NF033483 100 -------------EHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARalssttmtqtn 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138    484 ---G-VHhidYykktsngrlpvkwMAPE-ALFDRVyTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:NF033483 167 svlGtVH---Y-------------LSPEqARGGTV-DARSDIYSLGIVLYEMLT-GRPPFDG 210
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
102-183 1.03e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 57.98  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSslgadgfpyvQVLKTTDINSSEVEVLYLRNVSAEDAGEYTCLA 181
Cdd:pfam13927   8 PSSVVVVEGETVTLTCEASGSPPPTITWYK----NGG----------KLSSGRTSLVGGNGTLTISNVTREDSGTYTCTA 73

                  ..
gi 204138     182 GN 183
Cdd:pfam13927  74 SN 75
 
Name Accession Description Interval E-value
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
302-615 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 688.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05099   1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05099  81 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05099 161 AARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPN 615
Cdd:cd05099 241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVLAAVSEEYLDLSMPFEQYSPS 314
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
302-596 0e+00

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 627.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSsRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05053   1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDN-KPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05053  80 INLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05053 160 AARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLL 596
Cdd:cd05053 240 PVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRILT 294
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
292-601 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 554.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   292 PLLTGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEM 371
Cdd:cd05101   3 PMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   372 MKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYL 451
Cdd:cd05101  83 MKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   452 ESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIF 531
Cdd:cd05101 163 ASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIF 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   532 TLGGSPYPGIPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL-LAVSEE 601
Cdd:cd05101 243 TLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILtLTTNEE 313
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
302-633 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 553.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05100   1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05100  81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05100 161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVS-EEYLDLRLTFGPYSPNNGDAS 620
Cdd:cd05100 241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTStDEYLDLSVPFEQYSPGCPDSP 320
                       330
                ....*....|....
gi 204138   621 STCSS-SDSVFSHD 633
Cdd:cd05100 321 SSCSSgDDSVFAHD 334
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
301-601 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 542.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   301 DLPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKN 380
Cdd:cd05098   1 ELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   381 IINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRD 460
Cdd:cd05098  81 IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   461 LAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPG 540
Cdd:cd05098 161 LAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPG 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   541 IPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEE 601
Cdd:cd05098 241 VPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQ 301
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
319-592 1.89e-144

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 420.02  E-value: 1.89e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDSsrpdQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDG----KTVDVAVKTLKEDASESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRPPGPDLSPDgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd00192  76 EYMEGGDLLDFLRKSRPVFPSPEPS-------TLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMER 558
Cdd:cd00192 149 FGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPK 228
                       250       260       270
                ....*....|....*....|....*....|....
gi 204138   559 PPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd00192 229 PENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
315-591 2.09e-142

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 414.59  E-value: 2.09e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     315 LVLGKPLGEGCFGQVVCAEALGMDSsrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGE---NTKIKVAVKTLKEGADEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     395 YVIVEYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRK---------------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     475 KIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:pfam07714 142 KISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLEDGY 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 204138     555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:pfam07714 222 RLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
315-591 1.28e-138

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 405.01  E-value: 1.28e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      315 LVLGKPLGEGCFGQVVCAEALGMDSSRPDQtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVE---VAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      395 YVIVEYAAKGNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKE--------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      475 KIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:smart00221 143 KISDFGLSRDLYDDDYYKV-KGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGY 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 204138      555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:smart00221 222 RLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
315-591 1.57e-136

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 399.60  E-value: 1.57e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      315 LVLGKPLGEGCFGQVVCAEALGMDSSRPDQtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVE---VAVKTLKEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      395 YVIVEYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:smart00219  77 YIVMEYMEGGDLLSYLRKNRPK---------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      475 KIADFGLARGVHHIDYYKKTSnGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:smart00219 142 KISDFGLSRDLYDDDYYRKRG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGY 220
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 204138      555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:smart00219 221 RLPQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
308-591 1.27e-121

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 362.96  E-value: 1.27e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGV 387
Cdd:cd05054   2 WEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKS--ATCRTVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CT-QEGPLYVIVEYAAKGNLREFLRARRP---PGPDLSP-------DGPRSSEGPLSFPALVSCAYQVARGMQYLESRKC 456
Cdd:cd05054  80 CTkPGGPLMVIVEFCKFGNLSNYLRSKREefvPYRDKGArdveeeeDDDELYKEPLTLEDLICYSFQVARGMEFLASRKC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   457 IHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGS 536
Cdd:cd05054 160 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGAS 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   537 PYPGIPVEELF-SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05054 240 PYPGVQMDEEFcRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
302-595 9.89e-116

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 348.32  E-value: 9.89e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMdsSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05055  24 LPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGL--SKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLGNHENI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05055 102 VNLLGACTIGGPILVITEYCCYGDLLNFLR--------------RKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05055 168 AARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGM 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   542 PVEELF-SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05055 248 PVDSKFyKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
314-595 6.81e-115

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 345.41  E-value: 6.81e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEALGMdSSRPDQTSiVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGP 393
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKATAFRL-KGRAGYTT-VAVKMLKENASSSELRDLLSEFNLLKQVN-HPHVIKLYGACSQDGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRPPGPD-LSPDGPRSS-------EGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARN 465
Cdd:cd05045  78 LLLIVEYAKYGSLRSFLRESRKVGPSyLGSDGNRNSsyldnpdERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEE 545
Cdd:cd05045 158 VLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPER 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 204138   546 LFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05045 238 LFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
308-597 1.17e-111

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 339.26  E-value: 1.17e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTsiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGV 387
Cdd:cd05103   2 WEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRT--VAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEG-PLYVIVEYAAKGNLREFLRARRPP-----------------GPDLSPD-----------GPRSSEG-------- 430
Cdd:cd05103  80 CTKPGgPLMVIVEFCKFGNLSAYLRSKRSEfvpyktkgarfrqgkdyVGDISVDlkrrldsitssQSSASSGfveeksls 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   431 ---------------PLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTS 495
Cdd:cd05103 160 dveeeeagqedlykdFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   496 NGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSL-LREGHRMERPPNCPSELYGLMRECW 574
Cdd:cd05103 240 DARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRrLKEGTRMRAPDYTTPEMYQTMLDCW 319
                       330       340
                ....*....|....*....|...
gi 204138   575 HAAPSQRPTFKQLVEALDKVLLA 597
Cdd:cd05103 320 HGEPSQRPTFSELVEHLGNLLQA 342
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
308-595 1.25e-109

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 333.87  E-value: 1.25e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQTsiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGV 387
Cdd:cd05102   2 WEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCET--VAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQ-EGPLYVIVEYAAKGNLREFLRARRP---PGPDLSP------------------------DGPRSSEG--------- 430
Cdd:cd05102  80 CTKpNGPLMVIVEFCKYGNLSNFLRAKREgfsPYRERSPrtrsqvrsmveavradrrsrqgsdRVASFTEStsstnqprq 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   431 --------PLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVK 502
Cdd:cd05102 160 evddlwqsPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARLPLK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   503 WMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF-SLLREGHRMERPPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd05102 240 WMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFcQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKER 319
                       330
                ....*....|....
gi 204138   582 PTFKQLVEALDKVL 595
Cdd:cd05102 320 PTFSDLVEILGDLL 333
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
308-591 8.94e-105

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 321.57  E-value: 8.94e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGV 387
Cdd:cd14207   2 WEFARERLKLGKSLGRGAFGKVVQASAFGIKKS--PTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEG-PLYVIVEYAAKGNLREFLRARRP---PGPDLS-------------PDGPR--------SSEG------------ 430
Cdd:cd14207  80 CTKSGgPLMVIVEYCKYGNLSNYLKSKRDffvTNKDTSlqeelikekkeaePTGGKkkrlesvtSSESfassgfqedksl 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   431 ----------------PLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKT 494
Cdd:cd14207 160 sdveeeeedsgdfykrPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   495 SNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV-EELFSLLREGHRMERPPNCPSELYGLMREC 573
Cdd:cd14207 240 GDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIdEDFCSKLKEGIRMRAPEFATSEIYQIMLDC 319
                       330
                ....*....|....*...
gi 204138   574 WHAAPSQRPTFKQLVEAL 591
Cdd:cd14207 320 WQGDPNERPRFSELVERL 337
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
302-595 3.20e-103

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 318.77  E-value: 3.20e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05104  24 LPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKA--DSAMTVAVKMLKPSAHSTEREALMSELKVLSYLGNHINI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARR-------------------------------------PPGP------ 418
Cdd:cd05104 102 VNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRdsficpkfedlaeaalyrnllhqremacdslneymdmKPSVsyvvpt 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   419 ----------------DLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLA 482
Cdd:cd05104 182 kadkrrgvrsgsyvdqDVTSEILEEDELALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLA 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   483 RGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF-SLLREGHRMERPPN 561
Cdd:cd05104 262 RDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVDSKFyKMIKEGYRMDSPEF 341
                       330       340       350
                ....*....|....*....|....*....|....
gi 204138   562 CPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05104 342 APSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQL 375
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
308-592 2.57e-101

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 310.04  E-value: 2.57e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVcaEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHkNIINLLGV 387
Cdd:cd05032   1 WELPREKITLIRELGQGSFGMVY--EGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCH-HVVRLLGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEgplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05032  78 VSTGQPTLVVMELMAKGDLKSYLRSRRPEAENNPGLGPPTLQ------KFIQMAAEIADGMAYLAAKKFVHRDLAARNCM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05032 152 VAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05032 232 KFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
302-595 8.58e-101

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 312.16  E-value: 8.58e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   302 LPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMdsSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNI 381
Cdd:cd05106  27 LPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGL--GKEDNVLRVAVKMLKASAHTDEREALMSELKILSHLGQHKNI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRP---------------------------------------------- 415
Cdd:cd05106 105 VNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAEtflnfvmalpeisetssdyknitlekkyirsdsgfssqgsdtyvem 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   416 -PGPDLSPDGPRSSEG-------PLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHH 487
Cdd:cd05106 185 rPVSSSSSQSSDSKDEedtedswPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMN 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   488 IDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF-SLLREGHRMERPPNCPSEL 566
Cdd:cd05106 265 DSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILVNSKFyKMVKRGYQMSRPDFAPPEI 344
                       330       340
                ....*....|....*....|....*....
gi 204138   567 YGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05106 345 YSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
300-595 4.02e-95

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 298.46  E-value: 4.02e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   300 LDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSrpdQTSI-VAVKMLKDNASDKDLADLISEMEMMKLIGRH 378
Cdd:cd05107  24 MQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHS---QSTMkVAVKMLKSTARSSEKQALMSELKIMSHLGPH 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   379 KNIINLLGVCTQEGPLYVIVEYAAKGNLREFLR------------ARRPPGP---------------------------D 419
Cdd:cd05107 101 LNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHrnkhtflqyyldKNRDDGSlisggstplsqrkshvslgsesdggymD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   420 LSPDGPRS------------------------------------------SEGP-LSFPALVSCAYQVARGMQYLESRKC 456
Cdd:cd05107 181 MSKDESADyvpmqdmkgtvkyadiessnyespydqylpsapertrrdtliNESPaLSYMDLVGFSYQVANGMEFLASKNC 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   457 IHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGS 536
Cdd:cd05107 261 VHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGT 340
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   537 PYPGIPVEELF-SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05107 341 PYPELPMNEQFyNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
300-595 1.24e-93

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 294.62  E-value: 1.24e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   300 LDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPdqTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHK 379
Cdd:cd05105  24 MQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQP--VMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   380 NIINLLGVCTQEGPLYVIVEYAAKGNL-------REFLRARRPPGPD-------LSP----------------------- 422
Cdd:cd05105 102 NIVNLLGACTKSGPIYIITEYCFYGDLvnylhknRDNFLSRHPEKPKkdldifgINPadestrsyvilsfenkgdymdmk 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   423 ---------------------------DGPRS-----------------SEGpLSFPALVSCAYQVARGMQYLESRKCIH 458
Cdd:cd05105 182 qadttqyvpmleikeaskysdiqrsnyDRPASykgsndsevknllsddgSEG-LTTLDLLSFTYQVARGMEFLASKNCVH 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   459 RDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPY 538
Cdd:cd05105 261 RDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPY 340
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   539 PGIPVEELF-SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05105 341 PGMIVDSTFyNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
308-591 4.39e-91

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 282.70  E-value: 4.39e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGmdssrpdQTsiVAVKMLKDNASDKDlaDLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05039   1 WAINKKDLKLGELIGKGEFGDVMLGDYRG-------QK--VAVKCLKDDSTAAQ--AFLAEASVMTTL-RHPNLVQLLGV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgpRSSegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05039  69 VLEGNGLYIVTEYMAKGSLVDYLRSRG-----------RAV---ITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARgvhhiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05039 135 VSEDNVAKVSDFGLAK-----EASSNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVV 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05039 210 PHVEKGYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKL 253
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
319-592 4.70e-91

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 282.25  E-value: 4.70e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGmdssrpdqTSIVAVKMLKDNASDKDlaDLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNG--------TTKVAVKTLKPGTMSPE--AFLQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlSPDGprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05034  70 ELMSKGSLLDYLR---------TGEG-----RALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVAD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMER 558
Cdd:cd05034 136 FGLARLIED-DEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPK 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 204138   559 PPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05034 215 PPGCPDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
309-593 4.73e-89

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 278.50  E-value: 4.73e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEALGMDS-SRPDQtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05036   2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPGdPSPLQ---VAVKTLPELCSEQDEMDFLMEALIMSKF-NHPNIVRCIGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRPpgpdlSPDGPrsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05036  78 CFQRLPRFILLELMAGGDLKSFLRENRP-----RPEQP----SSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VT---EDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVE 544
Cdd:cd05036 149 LTckgPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQ 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 204138   545 ELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDK 593
Cdd:cd05036 229 EVMEFVTSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
308-592 5.82e-89

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 277.39  E-value: 5.82e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVcaEALGMDSSRpdqtsiVAVKMLKDNASDKdLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05148   1 WERPREEFTLERKLGSGYFGEVW--EGLWKNRVR------VAIKILKSDDLLK-QQDFQKEVQALKRL-RHKHLISLFAV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRarrppgpdlSPDGpRSsegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05148  71 CSVGEPVYIITELMEKGSLLAFLR---------SPEG-QV----LPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNIL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHiDYYKkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05148 137 VGEDLVCKVADFGLARLIKE-DVYL-SSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVY 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05148 215 DQITAGYRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREELD 259
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
309-593 1.08e-88

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 277.87  E-value: 1.08e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDqtSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVC 388
Cdd:cd05050   1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYEPF--TMVAVKMLKEEASADMQADFQREAALMAEFD-HPNIVKLLGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   389 TQEGPLYVIVEYAAKGNLREFLRARRP---------PGPDLSPDGPRSsegPLSFPALVSCAYQVARGMQYLESRKCIHR 459
Cdd:cd05050  78 AVGKPMCLLFEYMAYGDLNEFLRHRSPraqcslshsTSSARKCGLNPL---PLSCTEQLCIAKQVAAGMAYLSERKFVHR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   460 DLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYP 539
Cdd:cd05050 155 DLATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYY 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 204138   540 GIPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDK 593
Cdd:cd05050 235 GMAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
321-591 2.67e-88

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 276.22  E-value: 2.67e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSSRPDQTSiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05044   3 LGSGAFGEVFEGTAKDILGDGSGETK-VAVKTLRKGATDQEKAEFLKEAHLMSNF-KHPNILKLLGVCLDNDPQYIILEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPgpdlSPDGPRssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD----VMKI 476
Cdd:cd05044  81 MEGGDLLSYLRAARPT----AFTPPL-----LTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDyrerVVKI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRM 556
Cdd:cd05044 152 GDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRL 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   557 ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05044 232 DQPDNCPDDLYELMLRCWSTDPEERPSFARILEQL 266
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
309-587 4.47e-87

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 273.48  E-value: 4.47e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEALGMdsSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVC 388
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGELLGP--SSEESAISVAIKTLKENASPKTQQDFRREAELMSDL-QHPNIVCLLGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   389 TQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd05048  78 TKEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS 548
Cdd:cd05048 158 GDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIE 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   549 LLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05048 238 MIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
321-595 1.76e-85

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 268.83  E-value: 1.76e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEaLGMDSSRPDqtsiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05047   3 IGEGNFGQVLKAR-IKKDGLRMD----AAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05047  78 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVhhiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERPP 560
Cdd:cd05047 158 LSRGQ---EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   561 NCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05047 235 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 269
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
309-587 3.53e-85

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 268.82  E-value: 3.53e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEALGMD---------SSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHK 379
Cdd:cd05051   1 EFPREKLEFVEKLGEGQFGEVHLCEANGLSdltsddfigNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQL-KDP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   380 NIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRssegPLSFPALVSCAYQVARGMQYLESRKCIHR 459
Cdd:cd05051  80 NIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNSK----TLSYGTLLYMATQIASGMKYLESLNFVHR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   460 DLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGG-SPY 538
Cdd:cd05051 156 DLATRNCLVGPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKeQPY 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   539 PGIPVEELFSLLREGHR-------MERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05051 236 EHLTDEQVIENAGEFFRddgmevyLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
308-587 4.35e-84

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 265.04  E-value: 4.35e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVcaEALGmdssrpDQTSIVAVKMLKDNASDKDlaDLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05068   3 WEIDRKSLKLLRKLGSGQFGEVW--EGLW------NNTTPVAVKTLKPGTMDPE--DFLREAQIMKKL-RHPKLIQLYAV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05068  72 CTLEEPIYIITELMKHGSLLEYLQGKG---------------RSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05068 137 VGENNICKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVL 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05068 217 QQVERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETL 256
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
321-607 3.66e-82

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 261.09  E-value: 3.66e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdsSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05089  10 IGEGNFGQVIKAMI-----KKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAIEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05089  85 APYGNLLDFLRKSRVLETDPAFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVhhiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERPP 560
Cdd:cd05089 165 LSRGE---EVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKPR 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   561 NCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAvSEEYLDLRL 607
Cdd:cd05089 242 NCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEA-RKAYVNMAL 287
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
309-593 6.21e-81

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 257.39  E-value: 6.21e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEalgMDSSRPDQT-SIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGE---CYNLEPEQDkMLVAVKTLKDASSPDARKDFEREAELLTNL-QHENIVKFYGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARrppGPDL-SPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd05049  77 CTEGDPLLMVFEYMEHGDLNKFLRSH---GPDAaFLASEDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEEL 546
Cdd:cd05049 154 LVGTNLVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEV 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   547 FSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDK 593
Cdd:cd05049 234 IECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
308-592 3.58e-80

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 254.65  E-value: 3.58e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVcaEALGmdsSRPDQTsiVAVKMLKDNASDkdLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05052   1 WEIERTDITMKHKLGGGQYGEVY--EGVW---KKYNLT--VAVKTLKEDTME--VEEFLKEAAVMKEI-KHPNLVQLLGV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05052  71 CTREPPFYIITEFMPYGNLLDYLR--------------ECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05052 137 VGENHLVKVADFGLSRLMTG-DTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVY 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05052 216 ELLEKGYRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
308-595 2.05e-78

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 250.42  E-value: 2.05e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVvcaeALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05056   1 YEIQREDITLGRCIGEGQFGDV----YQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQF-DHPHIVKLIGV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTqEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05056  76 IT-ENPVWIVMELAPLGELRSYLQVNK---------------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05056 140 VSSPDCVKLGDFGLSRYMEDESYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05056 219 GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLSDIL 266
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
308-591 6.29e-78

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 249.89  E-value: 6.29e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVcaEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHkNIINLLGV 387
Cdd:cd05061   1 WEVSREKITLLRELGQGSFGMVY--EGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCH-HVVRLLGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRPPGPDlSPDGPrssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05061  78 VSKGQPTLVVMELMAHGDLKSYLRSLRPEAEN-NPGRP-----PPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05061 152 VAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05061 232 KFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
310-595 1.80e-77

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 248.45  E-value: 1.80e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   310 FPRDRLVLGKPLGEGCFGQVvcaEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd05038   1 FEERHLKFIKQLGEGHFGSV---ELCRYDPLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTL-DHEYIVKYKGVCE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGP--LYVIVEYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05038  77 SPGRrsLRLIMEYLPSGSLRDYLQRHRDQ---------------IDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNIL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGV-HHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIP---- 542
Cdd:cd05038 142 VESEDLVKISDFGLAKVLpEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPAlflr 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   543 ----------VEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05038 222 migiaqgqmiVTRLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
315-595 6.27e-77

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 246.68  E-value: 6.27e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVVCAEAlgmdsSRPDQTSI-VAVKMLK-DNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEG 392
Cdd:cd05035   1 LKLGKILGEGEFGSVMEAQL-----KQDDGSQLkVAVKTMKvDIHTYSEIEEFLSEAACMKDFD-HPNVMRLIGVCFTAS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PL------YVIVEYAAKGNLREFLRARRppgpdlspdgprSSEGPLSFP--ALVSCAYQVARGMQYLESRKCIHRDLAAR 464
Cdd:cd05035  75 DLnkppspMVILPFMKHGDLHSYLLYSR------------LGGLPEKLPlqTLLKFMVDIAKGMEYLSNRNFIHRDLAAR 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVE 544
Cdd:cd05035 143 NCMLDENMTVCVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENH 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   545 ELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05035 223 EIYDYLRNGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
321-591 7.88e-77

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 245.14  E-value: 7.88e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdssrpdqtSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd13999   1 IGSGSFGEVYKGKWRG---------TDVAIKKLKvEDDNDELLKEFRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd13999  71 YMPGGSLYDLLHKKKIP---------------LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLARGVHHIDYYKKTSNGRlpVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLREGHRMER 558
Cdd:cd13999 136 GLSRIKNSTTEKMTGVVGT--PRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELsPIQIAAAVVQKGLRPPI 212
                       250       260       270
                ....*....|....*....|....*....|...
gi 204138   559 PPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd13999 213 PPDCPPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
321-595 8.40e-77

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 247.22  E-value: 8.40e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEaLGMDSSRPDqtsiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05088  15 IGEGNFGQVLKAR-IKKDGLRMD----AAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05088  90 APHGNLLDFLRKSRVLETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVhhiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERPP 560
Cdd:cd05088 170 LSRGQ---EVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPL 246
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   561 NCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05088 247 NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 281
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
321-592 5.16e-76

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 243.51  E-value: 5.16e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdssRPDQTSiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05041   3 IGRGNFGDVYRGVL------KPDNTE-VAVKTCRETLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPIMIVMEL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05041  75 VPGGSLLTFLR---------------KKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERPP 560
Cdd:cd05041 140 MSREEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPE 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 204138   561 NCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05041 220 LCPEAVYRLMLQCWAYDPENRPSFSEIYNELQ 251
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
308-593 1.92e-75

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 242.09  E-value: 1.92e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDssrpdqtsiVAVKMLKDNASDKDLADLISEMEMMkligRHKNIINLLGV 387
Cdd:cd05083   1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQK---------VAVKNIKCDVTAQAFLEETAVMTKL----QHKNLVRLLGV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGpLYVIVEYAAKGNLREFLRARrppGPDLSPdgprssegplsFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05083  68 ILHNG-LYIVMELMSKGNLVNFLRSR---GRALVP-----------VIQLLQFSLDVAEGMEYLESKKLVHRDLAARNIL 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGvhhidYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05083 133 VSEDGVAKISDFGLAKV-----GSMGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVK 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDK 593
Cdd:cd05083 208 EAVEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLEK 253
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
315-591 1.51e-74

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 239.66  E-value: 1.51e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVVCAEALGMDSsrpdqtsiVAVKMLKDNASDKDlaDLISEME-MMKLigRHKNIINLLGVCTQEGP 393
Cdd:cd05059   6 LTFLKELGSGQFGVVHLGKWRGKID--------VAIKMIKEGSMSED--DFIEEAKvMMKL--SHPKLVQLYGVCTKQRP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05059  74 IFIVTEYMANGCLLNYLRERR---------------GKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREG 553
Cdd:cd05059 139 VKVSDFGLARYVLD-DEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQG 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   554 HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05059 218 YRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
319-591 3.97e-74

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 238.79  E-value: 3.97e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVcaeaLGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEME-MMKLigRHKNIINLLGVCtQEGPLYVI 397
Cdd:cd05060   1 KELGHGNFGSVR----KGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASvMAQL--DHPCIVRLIGVC-KGEPLMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRppgpdlspdgprssegplSFPA--LVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd05060  74 MELAPLGPLLKYLKKRR------------------EIPVsdLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAK 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVH-HIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:cd05060 136 ISDFGMSRALGaGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGE 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05060 216 RLPRPEECPQEIYSIMLSCWKYRPEDRPTFSELESTF 252
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
312-595 1.59e-73

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 238.30  E-value: 1.59e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEAlgmdsSRPDQTSI-VAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd14204   6 RNLLSLGKVLGEGEFGSVMEGEL-----QQPDGTNHkVAVKTMKlDNFSQREIEEFLSEAACMKDF-NHPNVIRLLGVCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLY-----VIVEYAAKGNLREFL-RARRPPGPDLSPdgprssegplsFPALVSCAYQVARGMQYLESRKCIHRDLAA 463
Cdd:cd14204  80 EVGSQRipkpmVILPFMKYGDLHSFLlRSRLGSGPQHVP-----------LQTLLKFMIDIALGMEYLSSRNFLHRDLAA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   464 RNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd14204 149 RNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQN 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   544 EELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd14204 229 HEIYDYLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLL 280
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
319-595 3.65e-73

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 236.50  E-value: 3.65e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCaealGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMkliGR--HKNIINLLGVCTQEGPLYV 396
Cdd:cd05033  10 KVIGGGEFGEVCS----GSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIM---GQfdHPNVIRLEGVVTKSRPVMI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05033  83 VTEYMENGSLDKFLR---------------ENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRM 556
Cdd:cd05033 148 SDFGLSRRLEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRL 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   557 ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05033 228 PPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKMI 266
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
312-587 3.65e-73

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 237.17  E-value: 3.65e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEALGMdssRPDQ-TSIVAVKMLKDnASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd05092   4 RRDIVLKWELGEGAFGKVFLAECHNL---LPEQdKMLVAVKALKE-ATESARQDFQREAELLTVL-QHQHIVRFYGVCTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARrppGPD--LSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd05092  79 GEPLIMVFEYMRHGDLNRFLRSH---GPDakILDGGEGQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS 548
Cdd:cd05092 156 GQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIE 235
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   549 LLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05092 236 CITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
308-594 5.33e-73

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 235.65  E-value: 5.33e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDssrpdqtsiVAVKMLKDNASDKDLadlISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05082   1 WALNMKELKLLQTIGKGEFGDVMLGDYRGNK---------VAVKCIKNDATAQAF---LAEASVMTQL-RHSNLVQLLGV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQE-GPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd05082  68 IVEEkGGLYIVTEYMAKGSLVDYLRSR--------------GRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNV 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFGLARGVHHIDyykktSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEEL 546
Cdd:cd05082 134 LVSEDNVAKVSDFGLTKEASSTQ-----DTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDV 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   547 FSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd05082 209 VPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
310-593 1.81e-72

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 235.05  E-value: 1.81e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   310 FPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDQtsIVAVKMLKDNASDKDLADLISEMEM-MKLigRHKNIINLLGVC 388
Cdd:cd05046   2 FPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGET--LVLVKALQKTKDENLQSEFRRELDMfRKL--SHKNVVRLLGLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   389 TQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd05046  78 REAEPHYMILEYTDLGDLKQFLRATKSKDEKLKPP-------PLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHHIDYYKkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS 548
Cdd:cd05046 151 SSQREVKVSLLSLSKDVYNSEYYK-LRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLN 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 204138   549 LLREGH-RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDK 593
Cdd:cd05046 230 RLQAGKlELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVSALGE 275
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
308-602 3.57e-72

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 234.16  E-value: 3.57e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEAlgmdssrpDQTSIVAVKMLKDNAsdKDLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05072   2 WEIPRESIKLVKKLGAGQFGEVWMGYY--------NNSTKVAVKTLKPGT--MSVQAFLEEANLMKTL-QHDKLVRLYAV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRarrppgpdlSPDGprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05072  71 VTKEEPIYIITEYMAKGSLLDFLK---------SDEG-----GKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05072 137 VSESLMCKIADFGLARVIED-NEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVM 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEY 602
Cdd:cd05072 216 SALQRGYRMPRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTATEGQY 270
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
308-591 1.65e-70

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 229.92  E-value: 1.65e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDqtSIVAVKMLKDNASDKDLADLISEMEMMKLIGRHkNIINLLGV 387
Cdd:cd05062   1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPE--TRVAIKTVNEAASMRERIEFLNEASVMKEFNCH-HVVRLLGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRPPGPDlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05062  78 VSQGQPTLVIMELMTRGDLKSYLRSLRPEMEN------NPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05062 152 VAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05062 232 RFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSI 275
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
312-591 4.67e-70

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 228.87  E-value: 4.67e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEALGMDSSRPDqtsiVAVKMLKDNASDKDLADLISEMemMKLIG-RHKNIINLLGVCTQ 390
Cdd:cd05043   5 RERVTLSDLLQEGTFGRIFHGILRDEKGKEEE----VLVKTVKDHASEIQVTMLLQES--SLLYGlSHQNLLPILHVCIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 E-GPLYVIVEYAAKGNLREFLRARRppgpDLSPDGPRSsegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd05043  79 DgEKPMVLYPYMNWGNLKLFLQQCR----LSEANNPQA----LSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVID 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSL 549
Cdd:cd05043 151 DELQVKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAY 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   550 LREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05043 231 LKDGYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCL 272
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
307-595 1.61e-69

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 227.30  E-value: 1.61e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   307 LWEFPRDRLVLGKPLGEGCFGQVVCAealgmdSSRPDQTSI---VAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIIN 383
Cdd:cd05057   1 LRIVKETELEKGKVLGSGAFGTVYKG------VWIPEGEKVkipVAIKVLREETGPKANEEILDEAYVMASVD-HPHLVR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   384 LLGVCTQEgPLYVIVEYAAKGNLREFLRArrppgpdlspdgPRSSEGPLSfpaLVSCAYQVARGMQYLESRKCIHRDLAA 463
Cdd:cd05057  74 LLGICLSS-QVQLITQLMPLGCLLDYVRN------------HRDNIGSQL---LLNWCVQIAKGMSYLEEKRLVHRDLAA 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   464 RNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd05057 138 RNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPA 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   544 EELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05057 218 VEIPDLLEKGERLPQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMA 269
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
318-591 3.21e-69

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 225.58  E-value: 3.21e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVCAEAlgmdssRPDQTsIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05084   1 GERIGRGNFGEVFSGRL------RADNT-PVAVKSCRETLPPDLKAKFLQEARILKQYS-HPNIVRLIGVCTQKQPIYIV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRarrppgpdlspdgprsSEGP-LSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05084  73 MELVQGGDFLTFLR----------------TEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRM 556
Cdd:cd05084 137 SDFGMSREEEDGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRL 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   557 ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05084 217 PCPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
314-595 8.14e-69

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 225.66  E-value: 8.14e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEAlgmdsSRPDQTSIVAVKMLKDN-ASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQ-- 390
Cdd:cd05075   1 KLALGKTLGEGEFGSVMEGQL-----NQDDSVLKVAVKTMKIAiCTRSEMEDFLSEAVCMKEFD-HPNVMRLIGVCLQnt 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 --EG---PLyVIVEYAAKGNLREFLRARRppgpdlspdgprSSEGPLSFPA--LVSCAYQVARGMQYLESRKCIHRDLAA 463
Cdd:cd05075  75 esEGypsPV-VILPFMKHGDLHSFLLYSR------------LGDCPVYLPTqmLVKFMTDIASGMEYLSSKNFIHRDLAA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   464 RNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd05075 142 RNCMLNENMNVCVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVEN 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   544 EELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05075 222 SEIYDYLRQGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKIL 273
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
311-595 9.89e-69

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 225.57  E-value: 9.89e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAEaLGMDSsrpDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd05074   7 QEQQFTLGRMLGKGEFGSVREAQ-LKSED---GSFQKVAVKMLKaDIFSSSDIEEFLREAACMKEF-DHPNVIKLIGVSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPL------YVIVEYAAKGNLREFLRARRppgpdlspdgprSSEGPLSFP--ALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd05074  82 RSRAKgrlpipMVILPFMKHGDLHTFLLMSR------------IGEEPFTLPlqTLVRFMIDIASGMEYLSSKNFIHRDL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05074 150 AARNCMLNENMTVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGV 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05074 230 ENSEIYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
319-591 6.39e-68

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 222.22  E-value: 6.39e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEAlgmdsSRPDQTSI-VAVKMLK-DNASDKD-LADLISEMEMMKLIgRHKNIINLLGVCTQEgPLY 395
Cdd:cd05040   1 EKLGDGSFGVVRRGEW-----TTPSGKVIqVAVKCLKsDVLSQPNaMDDFLKEVNAMHSL-DHPNLIRLYGVVLSS-PLM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRARRPpgpdlspdgprssegplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05040  74 MVTELAPLGSLLDRLRKDQG-----------------HFLISTLCDYavQIANGMAYLESKRFIHRDLAARNILLASKDK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLAR--GVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLL- 550
Cdd:cd05040 137 VKIGDFGLMRalPQNE-DHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKId 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   551 REGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05040 216 KEGERLERPDDCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
308-597 2.65e-67

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 220.91  E-value: 2.65e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVvcaeALGMDSSrpdqTSIVAVKMLKDNASDKDLadLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05067   2 WEVPRETLKLVERLGAGQFGEV----WMGYYNG----HTKVAIKSLKQGSMSPDA--FLAEANLMKQL-QHQRLVRLYAV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEgPLYVIVEYAAKGNLREFLRarrppgpdlSPDGPRssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05067  71 VTQE-PIYIITEYMENGSLVDFLK---------TPSGIK-----LTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANIL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05067 136 VSDTLSCKIADFGLARLIEDNEYTAR-EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVI 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLA 597
Cdd:cd05067 215 QNLERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLEDFFTA 264
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
321-587 8.63e-66

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 217.58  E-value: 8.63e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdSSRPDQTSIVAVKMLKDNAsDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05091  14 LGEDRFGKVYKGHLFG--TAPGEQTQAVAIKTLKDKA-EGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05091  91 CSHGDLHEFLVMRSPHSDVGSTDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERPP 560
Cdd:cd05091 171 LFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRQVLPCPD 250
                       250       260
                ....*....|....*....|....*..
gi 204138   561 NCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05091 251 DCPAWVYTLMLECWNEFPSRRPRFKDI 277
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
318-591 1.37e-65

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 216.03  E-value: 1.37e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVvcaealgMDSSRPDQTSiVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05085   1 GELLGKGNFGEV-------YKGTLKDKTP-VAVKTCKEDLPQELKIKFLSEARILKQYD-HPNIVKLIGVCTQRQPIYIV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05085  72 MELVPGGDFLSFLRKKK---------------DELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKIS 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLAR----GVhhidyYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREG 553
Cdd:cd05085 137 DFGMSRqeddGV-----YSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKG 211
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   554 HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05085 212 YRMSAPQRCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
309-591 3.45e-65

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 216.78  E-value: 3.45e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEALGMDS---------SRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHK 379
Cdd:cd05095   1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMEKfmdkdfaleVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   380 NIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHR 459
Cdd:cd05095  80 NIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALP----SNALTVSYSDLRFMAAQIASGMKYLSSLNFVHR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   460 DLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTL-GGSPY 538
Cdd:cd05095 156 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFcREQPY 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   539 PGIPVEELF----SLLREGHR---MERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05095 236 SQLSDEQVIentgEFFRDQGRqtyLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLL 295
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
312-604 1.25e-64

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 214.90  E-value: 1.25e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEALGMDssrPDQTSI-VAVKMLKDnASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd05093   4 RHNIVLKRELGEGAFGKVFLAECYNLC---PEQDKIlVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARrppGPD--LSPDGPRSSEgpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd05093  79 GDPLIMVFEYMKHGDLNKFLRAH---GPDavLMAEGNRPAE--LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS 548
Cdd:cd05093 154 GENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIE 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   549 LLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQlVEALDKVLLAVSEEYLD 604
Cdd:cd05093 234 CITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKE-IHSLLQNLAKASPVYLD 288
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
321-597 8.56e-64

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 211.56  E-value: 8.56e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALgmdssRPDQTSI-VAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVC-TQEGPLYVIV 398
Cdd:cd05058   3 IGKGHFGCVYHGTLI-----DSDGQKIhCAVKSLNRITDIEEVEQFLKEGIIMKDF-SHPNVLSLLGIClPSEGSPLVVL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLR--ARRPPGPDLspdgprssegplsfpalVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05058  77 PYMKHGDLRNFIRseTHNPTVKDL-----------------IGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYK--KTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:cd05058 140 ADFGLARDIYDKEYYSvhNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGR 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLA 597
Cdd:cd05058 220 RLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQIFST 262
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
308-592 8.07e-63

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 209.11  E-value: 8.07e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEAlgmdssrpDQTSIVAVKMLKDNAsdKDLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05073   6 WEIPRESLKLEKKLGAGQFGEVWMATY--------NKHTKVAVKTMKPGS--MSVEAFLAEANVMKTL-QHDKLVKLHAV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEgPLYVIVEYAAKGNLREFLRarrppgpdlSPDGPRssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05073  75 VTKE-PIYIITEFMAKGSLLDFLK---------SDEGSK-----QPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANIL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05073 140 VSASLVCKIADFGLARVIEDNEYTAR-EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05073 219 RALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
309-591 8.97e-63

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 210.22  E-value: 8.97e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQV-VC-----AEALGMDSSR-PDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNI 381
Cdd:cd05097   1 EFPRQQLRLKEKLGEGQFGEVhLCeaeglAEFLGEGAPEfDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRL-KNPNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpDLSPDGPRSSEGP-LSFPALVSCAYQVARGMQYLESRKCIHRD 460
Cdd:cd05097  80 IRLLGVCVSDDPLCMITEYMENGDLNQFLSQR-----EIESTFTHANNIPsVSIANLLYMAVQIASGMKYLASLNFVHRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   461 LAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTL-GGSPYP 539
Cdd:cd05097 155 LATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLcKEQPYS 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   540 GIPVEELFSLLREGHR-------MERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05097 235 LLSDEQVIENTGEFFRnqgrqiyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
317-589 1.50e-62

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 208.15  E-value: 1.50e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      317 LGKPLGEGCFGQVVCAEALgmDSSRpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:smart00220   3 ILEKLGEGSFGKVYLARDK--KTGK-----LVAIKVIKKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      397 IVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:smart00220  75 VMEYCEGGDLFDLLKKR----------------GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      477 ADFGLARGVHHIDYYKK---TSNgrlpvkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLRE 552
Cdd:smart00220 139 ADFGLARQLDPGEKLTTfvgTPE------YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDdQLLELFKKIGK 211
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 204138      553 GHR--MERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:smart00220 212 PKPpfPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
309-587 1.58e-62

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 209.10  E-value: 1.58e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEAL--GMDssrpdQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLG 386
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIYKGHLYlpGMD-----HAQLVAIKTLKDYNNPQQWNEFQQEASLMTEL-HHPNIVCLLG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQEGPLYVIVEYAAKGNLREFLRARRPPGP-DLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARN 465
Cdd:cd05090  75 VVTQEQPVCMLFEFMNQGDLHEFLIMRSPHSDvGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEE 545
Cdd:cd05090 155 ILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQE 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   546 LFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05090 235 VIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
309-587 2.42e-62

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 209.41  E-value: 2.42e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAEA------------LGMDSSRPdqtSIVAVKMLKDNASDKDLADLISEMEMMKLIg 376
Cdd:cd05096   1 KFPRGHLLFKEKLGEGQFGEVHLCEVvnpqdlptlqfpFNVRKGRP---LLVAVKILRPDANKNARNDFLKEVKILSRL- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   377 RHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARR------PPGPDLSPDGPrsseGP-LSFPALVSCAYQVARGMQ 449
Cdd:cd05096  77 KDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHlddkeeNGNDAVPPAHC----LPaISYSSLLHVALQIASGMK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   450 YLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWE 529
Cdd:cd05096 153 YLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWE 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   530 IFTL-GGSPYPGIPVEELF----SLLREGHR---MERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05096 233 ILMLcKEQPYGELTDEQVIenagEFFRDQGRqvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
312-591 2.54e-62

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 208.71  E-value: 2.54e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEALGMDSSRpdQTSIVAVKMLKDN--ASDKDL---ADLISEMEmmkligrHKNIINLLG 386
Cdd:cd05094   4 RRDIVLKRELGEGAFGKVFLAECYNLSPTK--DKMLVAVKTLKDPtlAARKDFqreAELLTNLQ-------HDHIVKFYG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd05094  75 VCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEEL 546
Cdd:cd05094 155 LVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEV 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   547 FSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05094 235 IECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKIL 279
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
319-592 1.11e-61

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 205.54  E-value: 1.11e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGmdssrpdqTSIVAVKMLKDNASDKDlaDLISEMEMMKLIgRHKNIINLLGVCTQEgPLYVIV 398
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNG--------TTKVAIKTLKPGTMSPE--AFLEEAQIMKKL-RHDKLVQLYAVVSEE-PIYIVT 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlSPDGPRssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd14203  69 EFMSKGSLLDFLK---------DGEGKY-----LKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIAD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHiDYYKKTSNGRLPVKWMAPEA-LFDRvYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd14203 135 FGLARLIED-NEYTARQGAKFPIKWTAPEAaLYGR-FTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMP 212
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14203 213 CPPGCPESLHELMCQCWRKDPEERPTFEYLQSFLE 247
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
311-588 3.46e-60

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 202.03  E-value: 3.46e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDrLVLGKPLGEGCFGQVvcaeALGMDSSRPDqtsiVAVKMLKDNASDKDlaDLISEME-MMKLigRHKNIINLLGVCT 389
Cdd:cd05113   3 PKD-LTFLKELGTGQFGVV----KYGKWRGQYD----VAIKMIKEGSMSED--EFIEEAKvMMNL--SHEKLVQLYGVCT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRARRppgpdlspDGPRSSEgplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd05113  70 KQRPIFIITEYMANGCLLNYLREMR--------KRFQTQQ-------LLEMCKDVCEAMEYLESKQFLHRDLAARNCLVN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSL 549
Cdd:cd05113 135 DQGVVKVSDFGLSRYVLD-DEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEH 213
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   550 LREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd05113 214 VSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
308-602 1.74e-59

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 200.68  E-value: 1.74e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGmdssrpdqTSIVAVKMLKDNASDKDLadLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05069   7 WEIPRESLRLDVKLGQGCFGEVWMGTWNG--------TTKVAIKTLKPGTMMPEA--FLQEAQIMKKL-RHDKLVPLYAV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEgPLYVIVEYAAKGNLREFLRarrppgpdlSPDGPRssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05069  76 VSEE-PIYIVTEFMGKGSLLDFLK---------EGDGKY-----LKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANIL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05069 141 VGDNLVCKIADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVL 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEY 602
Cdd:cd05069 220 EQVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTATEPQY 274
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
313-591 4.36e-59

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 199.02  E-value: 4.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGQVVCAEALGMDSsrpdqtsiVAVKMLKDNASDKDlaDLISEME-MMKLigRHKNIINLLGVCTQE 391
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYWLNKDK--------VAIKTIREGAMSEE--DFIEEAEvMMKL--SHPKLVQLYGVCLEQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd05112  72 APICLVFEFMEHGCLSDYLRTQR---------------GLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGEN 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLR 551
Cdd:cd05112 137 QVVKVSDFGMTRFVLD-DQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDIN 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   552 EGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05112 216 AGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
95-197 2.35e-58

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 191.33  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    95 PILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKHIVINGSSLGADGFPYVQVLKTTDINSS--EVEVLYLRNVSAE 172
Cdd:cd05858   1 PILQAGLPANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVEVLKTAGVNTTdkEIEVLYLRNVTFE 80
                        90       100
                ....*....|....*....|....*
gi 204138   173 DAGEYTCLAGNSIGLSYQSAWLTVL 197
Cdd:cd05858  81 DAGEYTCLAGNSIGISHHSAWLTVL 105
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
308-602 3.25e-58

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 197.22  E-value: 3.25e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGmdssrpdqTSIVAVKMLKDNASDKDLadLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05071   4 WEIPRESLRLEVKLGQGCFGEVWMGTWNG--------TTRVAIKTLKPGTMSPEA--FLQEAQVMKKL-RHEKLVQLYAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEgPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05071  73 VSEE-PIYIVTEYMSKGSLLDFLKGE--------------MGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANIL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd05071 138 VGENLVCKVADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVL 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   548 SLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEY 602
Cdd:cd05071 217 DQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQY 271
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
321-589 4.24e-58

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 194.80  E-value: 4.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaEALGMDSSRPdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd00180   1 LGKGSFGKVY--KARDKETGKK-----VAVKVIPKEKLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd00180  73 CEGGSLKDLLKENK---------------GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIftlggspypgipveelfsllreghrmerpp 560
Cdd:cd00180 138 LAKDLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL------------------------------ 187
                       250       260
                ....*....|....*....|....*....
gi 204138   561 ncpSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd00180 188 ---EELKDLIRRMLQYDPKKRPSAKELLE 213
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
319-595 9.05e-58

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 195.96  E-value: 9.05e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVcaeaLGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05063  11 KVIGAGEFGEVF----RGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFS-HHNIIRLEGVVTKFKPAMIIT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05063  86 EYMENGALDKYLR---------------DHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHI-DYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd05063 151 FGLSRVLEDDpEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLP 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05063 231 APMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
314-595 1.05e-57

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 195.47  E-value: 1.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVvCAEALGMDSSRpdqTSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGP 393
Cdd:cd05066   5 CIKIEKVIGAGEFGEV-CSGRLKLPGKR---EIPVAIKTLKAGYTEKQRRDFLSEASIMGQFD-HPNIIHLEGVVTRSKP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05066  80 VMIVTEYMENGSLDAFLR---------------KHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHH-IDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLRE 552
Cdd:cd05066 145 CKVSDFGLSRVLEDdPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEE 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   553 GHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05066 225 GYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
315-595 3.76e-57

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 193.92  E-value: 3.76e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVvcaeALGMDSSrpdqTSIVAVKMLKDNASDKDlaDLISEME-MMKLigRHKNIINLLGVCTQEGP 393
Cdd:cd05114   6 LTFMKELGSGLFGVV----RLGKWRA----QYKVAIKAIREGAMSEE--DFIEEAKvMMKL--THPKLVQLYGVCTQQKP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05114  74 IYIVTEFMENGCLLNYLRQRR---------------GKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREG 553
Cdd:cd05114 139 VKVSDFGMTRYVLD-DQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRG 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   554 HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05114 218 HRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTITEIA 259
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
308-602 6.82e-57

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 193.75  E-value: 6.82e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGmdssrpdqTSIVAVKMLKDNASDKDlaDLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd05070   4 WEIPRESLQLIKRLGNGQFGEVWMGTWNG--------NTKVAIKTLKPGTMSPE--SFLEEAQIMKKL-KHDKLVQLYAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEgPLYVIVEYAAKGNLREFLRarrppgpdlspDGprssEG-PLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd05070  73 VSEE-PIYIVTEYMSKGSLLDFLK-----------DG----EGrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFGLARGVHHIDYYKKtSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEEL 546
Cdd:cd05070 137 LVGNGLICKIADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREV 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   547 FSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEY 602
Cdd:cd05070 216 LEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQY 271
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
309-594 2.78e-56

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 193.32  E-value: 2.78e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLvlgkpLGEGCFGQVVcaEALGMdssrPDQTSI---VAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLL 385
Cdd:cd05108   8 EFKKIKV-----LGSGAFGTVY--KGLWI----PEGEKVkipVAIKELREATSPKANKEILDEAYVMASV-DNPHVCRLL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   386 GVCTQEGpLYVIVEYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARN 465
Cdd:cd05108  76 GICLTST-VQLITQLMPFGCLLDYVREHKDN---------------IGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLAR--GVHHIDYYkkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd05108 140 VLVKTPQHVKITDFGLAKllGAEEKEYH--AEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPA 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   544 EELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd05108 218 SEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKM 268
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
319-595 5.27e-56

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 191.68  E-value: 5.27e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVvcaEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEG--PLYV 396
Cdd:cd05079  10 RDLGEGHFGKV---ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDGgnGIKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLrarrppgpdlspdgPRSsEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05079  86 IMEFLPSGSLKEYL--------------PRN-KNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVH-HIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGS-------------PYPG-I 541
Cdd:cd05079 151 GDFGLTKAIEtDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSesspmtlflkmigPTHGqM 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05079 231 TVTRLVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
319-594 1.06e-55

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 190.62  E-value: 1.06e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALgmdssrPDQTSI---VAVKMLKDNASDKDLADLISEMEMMKLIGRhKNIINLLGVCTQEgPLY 395
Cdd:cd05109  13 KVLGSGAFGTVYKGIWI------PDGENVkipVAIKVLRENTSPKANKEILDEAYVMAGVGS-PYVCRLLGICLTS-TVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd05109  85 LVTQLMPYGCLLDYVRENK---------------DRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLAR--GVHHIDYYkkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREG 553
Cdd:cd05109 150 ITDFGLARllDIDETEYH--ADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKG 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   554 HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd05109 228 ERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRM 268
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
312-584 1.53e-55

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 189.77  E-value: 1.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGK-PLGEGCFGQVvcaeALGMDSSRPDQTSiVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQ 390
Cdd:cd05115   2 RDNLLIDEvELGSGNFGCV----KKGVYKMRKKQID-VAIKVLKQGNEKAVRDEMMREAQIMHQLD-NPYIVRMIGVCEA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGpLYVIVEYAAKGNLREFLRARRppgpdlspdgprsSEGPLSfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd05115  76 EA-LMLVMEMASGGPLNKFLSGKK-------------DEITVS--NVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHID-YYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSL 549
Cdd:cd05115 140 QHYAKISDFGLSKALGADDsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSF 219
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   550 LREGHRMERPPNCPSELYGLMRECWHAAPSQRPTF 584
Cdd:cd05115 220 IEQGKRMDCPAECPPEMYALMSDCWIYKWEDRPNF 254
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
319-584 2.23e-55

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 189.02  E-value: 2.23e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVvcaeALGMDSSRPDQtSIVAVKMLKDNASDKDLAD-LISEMEMMKLIGrHKNIINLLGVCTQEGpLYVI 397
Cdd:cd05116   1 GELGSGNFGTV----KKGYYQMKKVV-KTVAVKILKNEANDPALKDeLLREANVMQQLD-NPYIVRMIGICEAES-WMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05116  74 MEMAELGPLNKFLQKNRH----------------VTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKIS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHID-YYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRM 556
Cdd:cd05116 138 DFGLSKALRADEnYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERM 217
                       250       260
                ....*....|....*....|....*...
gi 204138   557 ERPPNCPSELYGLMRECWHAAPSQRPTF 584
Cdd:cd05116 218 ECPAGCPPEMYDLMKLCWTYDVDERPGF 245
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
321-595 1.08e-54

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 187.77  E-value: 1.08e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVvCAEALGMDSSRpdqTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05065  12 IGAGEFGEV-CRGRLKLPGKR---EIFVAIKTLKSGYTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRPVMIITEF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05065  87 MENGALDSFLR---------------QNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHID---YYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd05065 152 LSRFLEDDTsdpTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLP 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05065 232 PPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
321-594 1.73e-54

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 187.41  E-value: 1.73e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCaeaLGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGP--LYVIV 398
Cdd:cd05080  12 LGEGHFGKVSL---YCYDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTL-YHENIVKYKGCCSEQGGksLQLIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLrarrppgpdlspdgPRSSegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05080  88 EYVPLGSLRDYL--------------PKHS---IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGV---HhiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFT--------------LGGSPYPGI 541
Cdd:cd05080 151 FGLAKAVpegH--EYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLThcdssqspptkfleMIGIAQGQM 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 204138   542 PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd05080 229 TVVRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
Pkinase pfam00069
Protein kinase domain;
315-589 4.04e-54

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 185.50  E-value: 4.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     315 LVLGKPLGEGCFGQVVcaEALGMDSSRpdqtsIVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:pfam00069   1 YEVLEKLGSGSFGTVY--KAKHRDTGK-----IVAIKKIkKEKIKKKKDKNILREIKILKKL-NHPNIVRLYDAFEDKDN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     394 LYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:pfam00069  73 LYLVLEYVEGGSLFDLLSEK----------------GAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     474 MKIADFGLARGVHHiDYYKKTSNGRLPvkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREG 553
Cdd:pfam00069 137 LKITDFGLARQLNS-GSSLTTFVGTPW--YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELIIDQ 212
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 204138     554 HRM--ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:pfam00069 213 PYAfpELPSNLSEEAKDLLKKLLKKDPSKRLTATEALQ 250
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
321-591 1.59e-53

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 185.10  E-value: 1.59e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVvcaEALGMDSSRPDQTSIVAVKMLKDNASDKdLADLISEMEMMKLIgRHKNIINLLGVCTQEG--PLYVIV 398
Cdd:cd05081  12 LGKGNFGSV---ELCRYDPLGDNTGALVAVKQLQHSGPDQ-QRDFQREIQILKAL-HSDFIVKYRGVSYGPGrrSLRLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05081  87 EYLPSGCLRDFLQRHR---------------ARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIAD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGV-HHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFT--------------LGGSPYPGIPV 543
Cdd:cd05081 152 FGLAKLLpLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTycdkscspsaeflrMMGCERDVPAL 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   544 EELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL---VEAL 591
Cdd:cd05081 232 CRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALgpqLDML 282
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
310-594 1.37e-52

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 182.52  E-value: 1.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   310 FPRDRLVLGKPLGEGCFGQVvcaEALGMDSSRPDQTSIVAVKMLKdNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd14205   1 FEERHLKFLQQLGKGNFGSV---EMCRYDPLQDNTGEVVAVKKLQ-HSTEEHLRDFEREIEILKSL-QHDNIVKYKGVCY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEG--PLYVIVEYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd14205  76 SAGrrNLRLIMEYLPYGSLRDYLQKHKER---------------IDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNIL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGV-HHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFT-------------- 532
Cdd:cd14205 141 VENENRVKIGDFGLTKVLpQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefmr 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   533 -LGGSPYPGIPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14205 221 mIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
1-87 1.22e-50

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 170.42  E-value: 1.22e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     1 MEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIR 80
Cdd:cd05857   9 MEKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSIN 88

                ....*..
gi 204138    81 YSYLLDV 87
Cdd:cd05857  89 HTYHLDV 95
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
310-587 5.38e-50

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 175.14  E-value: 5.38e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   310 FPRDRLVLGKPLGEGCFGQVVCAEALgmdssrPDQTSI---VAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLG 386
Cdd:cd05111   4 FKETELRKLKVLGSGVFGTVHKGIWI------PEGDSIkipVAIKVIQDRSGRQSFQAVTDHMLAIGSLD-HAYIVRLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTqeGP-LYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARN 465
Cdd:cd05111  77 ICP--GAsLQLVTQLLPLGSLLDHVRQHR---------------GSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEE 545
Cdd:cd05111 140 VLLKSPSQVQVADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAE 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   546 LFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05111 220 VPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKEL 261
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
95-195 1.11e-49

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409363  Cd Length: 102  Bit Score: 167.98  E-value: 1.11e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    95 PILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKHIVINGSSLGADGFPYVQVLKTTDIN-SSEVEVLYLRNVSAED 173
Cdd:cd04974   1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGLPYVTVLKVAGVNtTGEENTLTISNVTFDD 80
                        90       100
                ....*....|....*....|..
gi 204138   174 AGEYTCLAGNSIGLSYQSAWLT 195
Cdd:cd04974  81 AGEYICLAGNSIGLSFHSAWLT 102
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
319-594 7.97e-49

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 172.94  E-value: 7.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVcaeaLGMDSSRPDQTSI-VAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEgPLYVI 397
Cdd:cd05110  13 KVLGSGAFGTVY----KGIWVPEGETVKIpVAIKILNETTGPKANVEFMDEALIMASMD-HPHLVRLLGVCLSP-TIQLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05110  87 TQLMPHGCLLDYVHEHK---------------DNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKIT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd05110 152 DFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLP 231
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd05110 232 QPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRM 268
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
321-595 1.05e-47

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 168.56  E-value: 1.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVvCAEALGMDSSRpdqTSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05064  13 LGTGRFGEL-CRGCLKLPSKR---ELPVAIHTLRAGCSDKQRRGFLAEALTLGQFD-HSNIVRLEGVITRGNTMMIVTEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05064  88 MSNGALDSFLRKH---------------EGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 laRGVH-HIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERP 559
Cdd:cd05064 153 --RLQEdKSEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAP 230
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 204138   560 PNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd05064 231 RNCPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
348-592 1.26e-47

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 167.29  E-value: 1.26e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLKDNaSDKDLADLisememMKLigRHKNIINLLGVCTQeGPLY-VIVEYAAKGNLREFLRARRPPGPDLspdgpr 426
Cdd:cd14059  19 VAVKKVRDE-KETDIKHL------RKL--NHPNIIKFKGVCTQ-APCYcILMEYCPYGQLYEVLRAGREITPSL------ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   427 ssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDyYKKTSNGrlPVKWMAP 506
Cdd:cd14059  83 ----------LVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKS-TKMSFAG--TVAWMAP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   507 EALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEE-LFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFK 585
Cdd:cd14059 150 EVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAiIWGVGSNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFR 228

                ....*..
gi 204138   586 QLVEALD 592
Cdd:cd14059 229 QILMHLD 235
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
348-594 9.83e-45

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 160.25  E-value: 9.83e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLK---DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPgPDLspdg 424
Cdd:cd14061  20 VAVKAARqdpDEDISVTLENVRQEARLFWML-RHPNIIALRGVCLQPPNLCLVMEYARGGALNRVLAGRKIP-PHV---- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   425 prssegplsfpaLVSCAYQVARGMQYLESRK---CIHRDLAARNVLVTE--------DDVMKIADFGLARGVHHIDyyKK 493
Cdd:cd14061  94 ------------LVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLAREWHKTT--RM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   494 TSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPveelFSLLREGHRMER-----PPNCPSELYG 568
Cdd:cd14061 160 SAAGTY--AWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGID----GLAVAYGVAVNKltlpiPSTCPEPFAQ 232
                       250       260
                ....*....|....*....|....*.
gi 204138   569 LMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14061 233 LMKDCWQPDPHDRPSFADILKQLENI 258
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
314-589 2.09e-44

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 159.22  E-value: 2.09e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVcaeaLGMDSsrpDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd06606   1 RWKKGELLGKGSFGSVY----LALNL---DTGELMAVKEVElSGDSEEELEALEREIRILSSL-KHPNIVRYLGTERTEN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd06606  73 TLNIFLEYVPGGSLASLLK----------------KFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVHHIDyykkTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI--PVEEL 546
Cdd:cd06606 137 VVKLADFGCAKRLAEIA----TGEGTKSLRgtpyWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELgnPVAAL 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   547 FSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06606 212 FKIGSSGEPPPIPEHLSEEAKDFLRKCLQRDPKKRPTADELLQ 254
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
321-587 1.62e-43

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 157.42  E-value: 1.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmDSSrPDQtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14206   5 IGNGWFGKVILGEIFS-DYT-PAQ---VVVKELRVSAGPLEQRKFISEAQPYRSL-QHPNILQCLGLCTETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPgPDLSPDGPrssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd14206  79 CQLGDLKRYLRAQRKA-DGMTPDLP-----TRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRLPVKWMAPEaLFDRVY--------THQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS-LLR 551
Cdd:cd14206 153 LSHNNYKEDYYLTPDRLWIPLRWVAPE-LLDELHgnlivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTfVVR 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   552 EGH-RMERP----PNCpSELYGLMRECWhAAPSQRPTFKQL 587
Cdd:cd14206 232 EQQmKLAKPrlklPYA-DYWYEIMQSCW-LPPSQRPSVEEL 270
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
321-594 3.57e-41

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 150.96  E-value: 3.57e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDssrpdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIG--RHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14146   2 IGVGGFGKVYRATWKGQE---------VAVKAARQDPDEDIKATAESVRQEAKLFSmlRHPNIIKLEGVCLEEPNLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRArrppgpdlSPDGPRSSEGPLSFP-ALVSCAYQVARGMQYLESRK---CIHRDLAARNVLVTE---- 470
Cdd:cd14146  73 EFARGGTLNRALAA--------ANAAPGPRRARRIPPhILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEkieh 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDV----MKIADFGLARGVHHIDyyKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIP-VEE 545
Cdd:cd14146 145 DDIcnktLKITDFGLAREWHRTT--KMSAAGTY--AWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDgLAV 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 204138   546 LFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14146 220 AYGVAVNKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
322-592 4.69e-41

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 149.72  E-value: 4.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   322 GEGCFGQVVCAEALGMDSSrpdqtsiVAVKMLkdNASDKDlADLISEMEmmkligrHKNIINLLGVCTqEGPLYVIV-EY 400
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKE-------VAVKKL--LKIEKE-AEILSVLS-------HRNIIQFYGAIL-EAPNYGIVtEY 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRppgpdlspdgprsSEgPLSFPALVSCAYQVARGMQYLESR---KCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd14060  64 ASYGSLFDYLNSNE-------------SE-EMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKIC 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTsnGRLPvkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGgSPYPGIPVEELFSLLREGH-RM 556
Cdd:cd14060 130 DFGASRFHSHTTHMSLV--GTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTRE-VPFKGLEGLQVAWLVVEKNeRP 204
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 204138   557 ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14060 205 TIPSSCPRSFAELMRRCWEADVKERPSFKQIIGILE 240
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
321-591 6.78e-41

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 149.51  E-value: 6.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGqVVCAEALgmdssrpdQTSIVAVKMLKDNASDKDLADLISEMEMMKligrHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14058   1 VGRGSFG-VVCKARW--------RNQIVAVKIIESESEKKAFEVEVRQLSRVD----HPNIIKLYGACSNQKPVCLVMEY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRarrppGPDLSPDgprssegpLSFPALVSCAYQVARGMQYLES---RKCIHRDLAARNVLVTED-DVMKI 476
Cdd:cd14058  68 AEGGSLYNVLH-----GKEPKPI--------YTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGgTVLKI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHidyYKKTSNGRLPvkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPvEELFSLLREGHRM 556
Cdd:cd14058 135 CDFGTACDIST---HMTNNKGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIG-GPAFRIMWAVHNG 207
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   557 ERPP---NCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd14058 208 ERPPlikNCPKPIESLMTRCWSKDPEKRPSMKEIVKIM 245
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
315-594 1.37e-39

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 146.34  E-value: 1.37e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVVCAEALGmdssrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14145   8 LVLEEIIGIGGFGKVYRAIWIG------DEVAVKAARHDPDEDISQTIENVRQEAKLFAML-KHPNIIALRGVCLKEPNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRPPgPDLspdgprssegplsfpaLVSCAYQVARGMQYLESRK---CIHRDLAARNVLVTE- 470
Cdd:cd14145  81 CLVMEFARGGPLNRVLSGKRIP-PDI----------------LVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILILEk 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 -------DDVMKIADFGLARGVHHIDyyKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIP- 542
Cdd:cd14145 144 vengdlsNKILKITDFGLAREWHRTT--KMSAAG--TYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDg 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   543 VEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14145 219 LAVAYGVAMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
321-591 7.37e-39

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 143.79  E-value: 7.37e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdssrpDQTSIVAVkmLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14065   1 LGKGFFGEVYKVTH--------RETGKVMV--MKELKRFDEQRSFLKEVKLMRRL-SHPNILRFIGVCVKDNKLNFITEY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK---IA 477
Cdd:cd14065  70 VNGGTLEELLK---------------SMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVhhIDYYKKTSNGRLPVK------WMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLR 551
Cdd:cd14065 135 DFGLAREM--PDEKTKKPDRKKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDYLPRTMDFGLDV 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   552 EGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd14065 213 RAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
321-584 1.42e-38

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 143.36  E-value: 1.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCA--EALGMDssrpdqtsiVAVKMLK-DNASDKDLADLISEMEMMKLiGRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd13978   1 LGSGGFGTVSKArhVSWFGM---------VAIKCLHsSPNCIEERKALLKEAEKMER-ARHSYVLPLLGVCVERRSLGLV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRPPGPdlspdgprsseGPLSFPALvscaYQVARGMQYLE--SRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd13978  71 MEYMENGSLKSLLEREIQDVP-----------WSLRFRII----HEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVK 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVH----HIDYYKKTSNGRLPVkWMAPEAL--FDRVYTHQSDVWSFGILLWEIFTlGGSPYPG-IPVEELFS 548
Cdd:cd13978 136 ISDFGLSKLGMksisANRRRGTENLGGTPI-YMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT-RKEPFENaINPLLIMQ 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   549 LLREGHRMERPPNC-------PSELYGLMRECWHAAPSQRPTF 584
Cdd:cd13978 214 IVSKGDRPSLDDIGrlkqienVQELISLMIRCWDGNPDARPTF 256
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
319-587 3.33e-38

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 142.43  E-value: 3.33e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEA-LGMDSSRpdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05087   3 KEIGHGWFGKVFLGEVnSGLSSTQ------VVVKELKASASVQDQMQFLEEAQPYRAL-QHTNLLQCLAQCAEVTPYLLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRPpGPDLSPDgprssegPLSfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05087  76 MEFCPLGDLKGYLRSCRA-AESMAPD-------PLT---LQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTSNGRLPVKWMAPEaLFDRVY--------THQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSL 549
Cdd:cd05087 145 DYGLSHCKYKEDYFVTADQLWVPLRWIAPE-LVDEVHgnllvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTY 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   550 LREGHRMERP-PNCPSEL----YGLMRECWhAAPSQRPTFKQL 587
Cdd:cd05087 224 TVREQQLKLPkPQLKLSLaerwYEVMQFCW-LQPEQRPTAEEV 265
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
315-592 1.06e-37

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 140.93  E-value: 1.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVVCAEALGmdssrpdqtSIVAVKMLKDNAsDKDLA----DLISEMEMMKLIGrHKNIINLLGVCTQ 390
Cdd:cd14147   5 LRLEEVIGIGGFGKVYRGSWRG---------ELVAVKAARQDP-DEDISvtaeSVRQEARLFAMLA-HPNIIALKAVCLE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRPPgPDLspdgprssegplsfpaLVSCAYQVARGMQYLESRK---CIHRDLAARNVL 467
Cdd:cd14147  74 EPNLCLVMEYAAGGPLSRALAGRRVP-PHV----------------LVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNIL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VT--------EDDVMKIADFGLARGVHHIDyyKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYP 539
Cdd:cd14147 137 LLqpienddmEHKTLKITDFGLAREWHKTT--QMSAAGTY--AWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYR 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 204138   540 GIP-VEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14147 212 GIDcLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLE 265
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
321-594 1.89e-37

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 140.12  E-value: 1.89e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaEALGMDSSrpdqtsiVAVKMLKDNAsDKDLA----DLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd14148   2 IGVGGFGKVY--KGLWRGEE-------VAVKAARQDP-DEDIAvtaeNVRQEARLFWML-QHPNIIALRGVCLNPPHLCL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRPPgpdlspdgPRssegplsfpALVSCAYQVARGMQYLESRK---CIHRDLAARNVLVTE--- 470
Cdd:cd14148  71 VMEYARGGALNRALAGKKVP--------PH---------VLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpie 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 -----DDVMKIADFGLARGVHHIDyyKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYpgipvEE 545
Cdd:cd14148 134 nddlsGKTLKITDFGLAREWHKTT--KMSAAGTY--AWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPY-----RE 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   546 LFSL-LREGHRMER-----PPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14148 204 IDALaVAYGVAMNKltlpiPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
319-587 5.67e-37

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 139.26  E-value: 5.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEAL-GMDSSRpdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05042   1 QEIGNGWFGKVLLGEIYsGTSVAQ------VVVKELKASANPKEQDTFLKEGQPYRIL-QHPNILQCLGQCVEAIPYLLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRPPgpDLSPDGPRSsegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05042  74 MEFCDLGDLKAYLRSEREH--ERGDSDTRT---------LQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTSNGRLPVKWMAPEaLFDRVY--------THQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS- 548
Cdd:cd05042 143 DYGLAHSRYKEDYIETDDKLWFPLRWTAPE-LVTEFHdrllvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAq 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   549 LLREGH------RMERPpnCPSELYGLMRECWhAAPSQRPTFKQL 587
Cdd:cd05042 222 VVREQDtklpkpQLELP--YSDRWYEVLQFCW-LSPEQRPAAEDV 263
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
1-87 7.41e-37

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 132.73  E-value: 7.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     1 MEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIR 80
Cdd:cd05729   9 MEEREHALPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSIN 88

                ....*..
gi 204138    81 YSYLLDV 87
Cdd:cd05729  89 HTYDVDV 95
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
317-593 1.00e-36

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 138.10  E-value: 1.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALgmDSSRPdqtsiVAVKMLK-DNASDKDL-ADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14014   4 LVRLLGRGGMGEVYRARDT--LLGRP-----VAIKVLRpELAEDEEFrERFLREARALARL-SHPNIVRVYDVGEDDGRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd14014  76 YIVMEYVEGGSLADLLRER----------------GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHHIdyyKKTSNGRLP--VKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLR 551
Cdd:cd14014 140 KLTDFGIARALGDS---GLTQTGSVLgtPAYMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDsPAAVLAKHLQ 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   552 EGHRMER--PPNCPSELYGLMRECWHAAPSQRP-TFKQLVEALDK 593
Cdd:cd14014 216 EAPPPPSplNPDVPPALDAIILRALAKDPEERPqSAAELLAALRA 260
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
321-593 1.40e-36

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 138.17  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14066   1 IGSGGFGTVYKGV-------LENGT-VVAVKRLNEMNCAASKKEFLTELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYL---ESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd14066  72 MPNGSLEDRLHCHK-------------GSPPLPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPKLT 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd14066 139 DFGLARLIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVDENRENASRKDLVEWVESK 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 204138   558 RPPNC-------PSELYGLMRE-----------CWHAAPSQRPTFKQLVEALDK 593
Cdd:cd14066 218 GKEELedildkrLVDDDGVEEEeveallrlallCTRSDPSLRPSMKEVVQMLEK 271
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
321-596 1.10e-35

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 135.71  E-value: 1.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV--VCAEALGmdssrpdqtsivAVKMLKD--NASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd14154   1 LGKGFFGQAikVTHRETG------------EVMVMKEliRFDEEAQRNFLKEVKVMRSL-DHPNVLKFIGVLYKDKKLNL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd14154  68 ITEYIPGGTLKDVLK---------------DMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVV 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLAR---------GVHHIDYYKKTSNGRLPVK---------WMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPY 538
Cdd:cd14154 133 ADFGLARliveerlpsGNMSPSETLRHLKSPDRKKrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADP 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   539 PGIPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLL 596
Cdd:cd14154 213 DYLPRTKDFGLNVDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYL 270
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
350-595 2.86e-35

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 133.75  E-value: 2.86e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   350 VKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLrarrppgpdlspdgprSSE 429
Cdd:cd14155  20 VMALKMNTLSSNRANMLREVQLMNRL-SHPNILRFMGVCVHQGQLHALTEYINGGNLEQLL----------------DSN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   430 GPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD---VMKIADFGLARGVHHIDYYKKtsngRLPV----K 502
Cdd:cd14155  83 EPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPDYSDGKE----KLAVvgspY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   503 WMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRmERPPNCPSELYGLMRECWHAAPSQRP 582
Cdd:cd14155 159 WMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLDYDAFQ-HMVGDCPPDFLQLAFNCCNMDPKSRP 237
                       250
                ....*....|...
gi 204138   583 TFKQLVEALDKVL 595
Cdd:cd14155 238 SFHDIVKTLEEIL 250
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
317-587 3.62e-35

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 133.48  E-value: 3.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdsSRPDQtSIVAVKMLKDNaSDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05122   4 ILEKIGKGGFGVVYKAR------HKKTG-QIVAIKKINLE-SKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDELWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARrppgpdlspdgprssegPLSFPaLVSCAY---QVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05122  75 VMEFCSGGSLKDLLKNT-----------------NKTLT-EQQIAYvckEVLKGLEYLHSHGIIHRDIKAANILLTSDGE 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLArgvhhidyyKKTSNGRLPVK------WMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEEL 546
Cdd:cd05122 137 VKLIDFGLS---------AQLSDGKTRNTfvgtpyWMAPEVIQGKPYGFKADIWSLGITAIEMAE-GKPPYSELpPMKAL 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   547 FSLLREGH-RMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd05122 207 FLIATNGPpGLRNPKKWSKEFKDFLKKCLQKDPEKRPTAEQL 248
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
317-587 5.94e-35

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 132.73  E-value: 5.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVcaEALGMDSSRpdqtsIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd06627   4 LGDLIGRGAFGSVY--KGLNLNTGE-----FVAIKQISlEKIPKSDLKSVMGEIDLLKKL-NHPNIVKYIGSVKTKDSLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRarrppgpdlsPDGPrssegplsFP-ALVSC-AYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd06627  76 IILEYVENGSLASIIK----------KFGK--------FPeSLVAVyIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLRE 552
Cdd:cd06627 138 VKLADFGVATKLNEVEKDENSVVG--TPYWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLqPMAALFRIVQD 214
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   553 GHrMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd06627 215 DH-PPLPENISPELRDFLLQCFQKDPTLRPSAKEL 248
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
317-589 3.84e-34

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 130.67  E-value: 3.84e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAealgmdssRPDQTS-IVAVKML-KDNASDKDLAD-LISEME-MMKLigRHKNIINLLGVCTQEG 392
Cdd:cd14007   4 IGKPLGKGKFGNVYLA--------REKKSGfIVALKVIsKSQLQKSGLEHqLRREIEiQSHL--RHPNILRLYGYFEDKK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRARRPpgpdlspdgprssegplsFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd14007  74 RIYLILEYAPNGELYKELKKQKR------------------FDEKEAAKYiyQLALALDYLHSKNIIHRDIKPENILLGS 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLArgVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLL 550
Cdd:cd14007 136 NGELKLADFGWS--VHAPSNRRKTFCGTL--DYLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQETYKRI 210
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   551 REGHrMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14007 211 QNVD-IKFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
316-587 1.68e-33

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 128.79  E-value: 1.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVvcaeALGMDSsrpdQT-SIVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:cd14003   3 ELGKTLGEGSFGKV----KLARHK----LTgEKVAIKIIdKSKLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRPpgpdLSPDgprssEGPLSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14003  74 IYLVMEYASGGELFDYIVNNGR----LSED-----EARRFFQQLIS-------AVDYCHSNGIVHRDLKLENILLDKNGN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARgvhHIDYYK--KTSNGRLPvkWMAPEALFDRVY-THQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLL 550
Cdd:cd14003 138 LKIIDFGLSN---EFRGGSllKTFCGTPA--YAAPEVLLGRKYdGPKADVWSLGVILYAMLT-GYLPFDDDNDSKLFRKI 211
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   551 REGHrMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14003 212 LKGK-YPIPSHLSPDARDLIRRMLVVDPSKRITIEEI 247
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
363-589 1.46e-31

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 123.76  E-value: 1.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   363 ADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRArrppgpdlspdgprsSEGPLSFPALVscAY 442
Cdd:cd14027  36 EALLEEGKMMNRL-RHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKK---------------VSVPLSVKGRI--IL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   443 QVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVK-----------WMAPEALFD 511
Cdd:cd14027  98 EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDgtakknagtlyYMAPEHLND 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   512 --RVYTHQSDVWSFGILLWEIFTlGGSPYP-GIPVEELFSLLREGHR---MERPPNCPSELYGLMRECWHAAPSQRPTFK 585
Cdd:cd14027 178 vnAKPTEKSDVYSFAIVLWAIFA-NKEPYEnAINEDQIIMCIKSGNRpdvDDITEYCPREIIDLMKLCWEANPEARPTFP 256

                ....
gi 204138   586 QLVE 589
Cdd:cd14027 257 GIEE 260
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
318-589 3.61e-31

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 122.51  E-value: 3.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVcaEALGMDSSrpdqtSIVAVKMLKDNASDKDLADLISEMEM-MKLIG--RHKNIINLLGVCTQEGPL 394
Cdd:cd06632   5 GQLLGSGSFGSVY--EGFNGDTG-----DFFAVKEVSLVDDDKKSRESVKQLEQeIALLSklRHPNIVQYYGTEREEDNL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd06632  78 YIFLEYVPGGSIHKLLQ----------------RYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARgvhHIDYYKKTSNGRLPVKWMAPEAL--FDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLR 551
Cdd:cd06632 142 KLADFGMAK---HVEAFSFAKSFKGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYeGVAAIFKIGN 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   552 EGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06632 218 SGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
321-591 1.73e-30

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 120.80  E-value: 1.73e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMD-----------SSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd14000   2 LGDGGFGSVYRASYKGEPvavkifnkhtsSNFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHL-HHPSIVYLLGIGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QegPLYVIVEYAAKGNLREFLRARRPPGPDLspdgprsseGPLSFPALvscAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd14000  81 H--PLMLVLELAPLGSLDHLLQQDSRSFASL---------GRTLQQRI---ALQVADGLRYLHSAMIIYRDLKSHNVLVW 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDV-----MKIADFGLARGVHHIDyyKKTSNGrlPVKWMAPE-ALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd14000 147 TLYPnsaiiIKIADYGISRQCCRMG--AKGSEG--TPGFRAPEiARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKF 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 204138   544 EELFSLLREGHRMERPPNC--PSELYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd14000 223 PNEFDIHGGLRPPLKQYECapWPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
313-589 5.25e-30

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 118.89  E-value: 5.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQE 391
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGR-------RKYTGQVVALKFIpKRGKSEKELRNLRQEIEILRKL-NHPNIIEMLDSFETK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAkGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd14002  73 KEFVVVTEYAQ-GELFQIL----------------EDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLARGVhHIDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlgGSPypgiP--VEELFSL 549
Cdd:cd14002 136 GVVKLCDFGFARAM-SCNTLVLTSIKGTPL-YMAPELVQEQPYDHTADLWSLGCILYELFV--GQP----PfyTNSIYQL 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   550 LRegHRMERP--------PNCPSELYGLMREcwhaAPSQRPTFKQLVE 589
Cdd:cd14002 208 VQ--MIVKDPvkwpsnmsPEFKSFLQGLLNK----DPSKRLSWPDLLE 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
317-567 1.03e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 121.39  E-value: 1.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdssrpdQTSIVAVKMLKDNASDKDLAD--LISEMEMMKLIGRHKNIINLLGVCTQEGPL 394
Cdd:COG0515   4 ILRKLGEGSFGEVYLAR----------DRKLVALKVLAKKLESKSKEVerFLREIQILASLNHPPNIVKLYDFFQDEGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRarrppgpdlspdgPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:COG0515  74 YLVMEYVDGGSLEDLLK-------------KIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 -KIADFGLARGV------HHIDYYKKTSNGRLPvkWMAPEAL---FDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVE 544
Cdd:COG0515 141 vKLIDFGLAKLLpdpgstSSIPALPSTSVGTPG--YMAPEVLlglSLAYASSSSDIWSLGITLYELLT-GLPPFEGEKNS 217
                       250       260
                ....*....|....*....|...
gi 204138   545 ELFSLLREGHRMERPPNCPSELY 567
Cdd:COG0515 218 SATSQTLKIILELPTPSLASPLS 240
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
321-592 1.33e-29

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 117.49  E-value: 1.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdssrpdqtsIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGpLYVIVE 399
Cdd:cd14062   1 IGSGSFGTVYKGRWHG----------DVAVKKLNvTDPTPSQLQAFKNEVAVLRKT-RHVNILLFMGYMTKPQ-LAIVTQ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRArrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd14062  69 WCEGSSLYKHLHV---------------LETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDF 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLARgvhhidyYKKTSNGRLPVK-------WMAPEALF---DRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFsL 549
Cdd:cd14062 134 GLAT-------VKTRWSGSQQFEqptgsilWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQI-L 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 204138   550 LREGHRMERP------PNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14062 205 FMVGRGYLRPdlskvrSDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
316-587 1.72e-29

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 118.19  E-value: 1.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKpLGEGCFGQVvcaealgMDSSRPDQTSIVAVKMLKDNASDKDLADLI-SEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd07833   5 VLGV-VGEGAYGVV-------LKCRNKATGEIVAIKKFKESEDDEDVKKTAlREVKVLRQL-RHENIVNLKEAFRRKGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKgNLREFLRARrPPGpdLSPDGPRSsegplsfpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd07833  76 YLVFEYVER-TLLELLEAS-PGG--LPPDAVRS------------YIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVH-----HIDYYKKTsngrlpvKWM-APEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPG------ 540
Cdd:cd07833 140 KLCDFGFARALTarpasPLTDYVAT-------RWYrAPELLVgDTNYGKPVDVWAIGCIMAELLD--GEPlFPGdsdidq 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   541 ------------------------------IPVEELFSLLReghrmeRPPN-CPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd07833 211 lyliqkclgplppshqelfssnprfagvafPEPSQPESLER------RYPGkVSSPALDFLKACLRMDPKERLTCDEL 282
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
321-596 3.61e-29

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 116.98  E-value: 3.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdSSRPDQTSIVAVKMLK-DNASDKDLadlISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd14221   1 LGKGCFGQAIKV------THRETGEVMVMKELIRfDEETQRTF---LKEVKVMRCL-EHPNVLKFIGVLYKDKRLNFITE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARrppgpdlspdgprSSEGPLSfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd14221  71 YIKGGTLRGIIKSM-------------DSHYPWS--QRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLAR--------GVHHIDYYKKTSNGRLPV----KWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd14221 136 GLARlmvdektqPEGLRSLKKPDRKKRYTVvgnpYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDF 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   548 SLLREGHrMER--PPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLL 596
Cdd:cd14221 216 GLNVRGF-LDRycPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLRM 265
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
308-594 1.98e-28

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 114.77  E-value: 1.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMdssrpdqtsiVAVKMLKDNA-SDKDLADLISEMEMMKLIgRHKNIINLLG 386
Cdd:cd14151   3 WEIPDGQITVGQRIGSGSFGTVYKGKWHGD----------VAVKMLNVTApTPQQLQAFKNEVGVLRKT-RHVNILLFMG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQEgPLYVIVEYAAKGNLREFLRArrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd14151  72 YSTKP-QLAIVTQWCEGSSLYHHLHI---------------IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFGLA------RGVHHIDYYKKTsngrlpVKWMAPEALF---DRVYTHQSDVWSFGILLWEIFTlGGSP 537
Cdd:cd14151 136 FLHEDLTVKIGDFGLAtvksrwSGSHQFEQLSGS------ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLP 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   538 YPGI-PVEELFSLLREGH----RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14151 209 YSNInNRDQIIFMVGRGYlspdLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 270
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
321-480 4.97e-28

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 109.45  E-value: 4.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdssrpdQTSIVAVKMLKDNASDkDLADLISEMEMMKLIGRH-KNIINLLGVCTQEGPLYVIVE 399
Cdd:cd13968   1 MGEGASAKVFWAEGEC-------TTIGVAVKIGDDVNNE-EGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd13968  73 LVKGGTLIAYT-----------------QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDF 135

                .
gi 204138   480 G 480
Cdd:cd13968 136 G 136
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
318-589 5.97e-28

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 113.03  E-value: 5.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQvvCAEALGMDSSRPDQTSIVAVKMLKdnaSDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14099   6 GKFLGKGGFAK--CYEVTDMSTGKVYAGKVVPKSSLT---KPKQREKLKSEIKIHRSL-KHPNIVKFHDCFEDEENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd14099  80 LELCSNGSLMELLKRRKA----------------LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTSNGRlPvKWMAPEALFDRV-YTHQSDVWSFGILLweiFTL--GGSPYPGIPVEELFSLLREGH 554
Cdd:cd14099 144 DFGLAARLEYDGERKKTLCGT-P-NYIAPEVLEKKKgHSFEVDIWSLGVIL---YTLlvGKPPFETSDVKETYKRIKKNE 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 204138   555 -RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14099 219 ySFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILS 254
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
339-591 8.35e-28

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 112.57  E-value: 8.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   339 SSRPDQTSIVaVKMLKDNASDKDLA--DLISemeMMKLIgRHKNIINLLGVCTQEGplYVIV-EYAAKGNLREFLRaRRP 415
Cdd:cd05037  25 DGRVQEVEVL-LKVLDSDHRDISESffETAS---LMSQI-SHKHLVKLYGVCVADE--NIMVqEYVRYGPLDKYLR-RMG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   416 PGPDLSpdgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV------MKIADFGLARGVHHID 489
Cdd:cd05037  97 NNVPLS--------------WKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGVPITVLSRE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   490 YYKktsngrLPVKWMAPEALFD--RVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERpPNCPsELY 567
Cdd:cd05037 163 ERV------DRIPWIAPECLRNlqANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPA-PDCA-ELA 234
                       250       260
                ....*....|....*....|....
gi 204138   568 GLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd05037 235 ELIMQCWTYEPTKRPSFRAILRDL 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
318-588 1.98e-27

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 111.86  E-value: 1.98e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVcaeaLGMDSSRPDQTSIVAVKMLKDNASDKD-----LADLISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd06628   5 GALIGSGSFGSVY----LGMNASSGELMAVKQVELPSVSAENKDrkksmLDALQREIALLREL-QHENIVQYLGSSSDAN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd06628  80 HLNIFLEYVPGGSVATLL----------------NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVhHIDYYKKTSNGRLP-----VKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIpvEELF 547
Cdd:cd06628 144 GIKISDFGISKKL-EANSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDC--TQMQ 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   548 SLLREGH--RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd06628 220 AIFKIGEnaSPTIPSNISSEARDFLEKTFEIDHNKRPTADELL 262
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
321-587 2.85e-27

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 111.02  E-value: 2.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdsSRPDQtSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd08215   8 IGKGSFGSAYLVR------RKSDG-KLYVLKEIDlSNMSEKEREEALNEVKLLSKL-KHPNIVKYYESFEENGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARRPPGpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd08215  80 YADGGDLAQKIKKQKKKG------------QPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLARGVHHID----------YYkktsngrlpvkwMAPEALFDRVYTHQSDVWSFGILLWEIFTL-----GGSpypgipVE 544
Cdd:cd08215 148 GISKVLESTTdlaktvvgtpYY------------LSPELCENKPYNYKSDIWALGCVLYELCTLkhpfeANN------LP 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   545 ELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd08215 210 ALVYKIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSANEI 252
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
319-589 4.04e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 110.76  E-value: 4.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAealgMDSSRPDQtsiVAVKMLKDNASDKDLadLISEMEMMKlIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd06614   6 EKIGEGASGEVYKA----TDRATGKE---VAIKKMRLRKQNKEL--IINEILIMK-ECKHPNIVDYYDSYLVGDELWVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd06614  76 EYMDGGSLTDIIT---------------QNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLAD 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPY---PgiPVEELFSLLREG-H 554
Cdd:cd06614 141 FGFAAQLTKEKSKRNSVVGT-PY-WMAPEVIKRKDYGPKVDIWSLGIMCIEM-AEGEPPYleeP--PLRALFLITTKGiP 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   555 RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06614 216 PLKNPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQ 250
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
319-587 4.64e-27

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 110.56  E-value: 4.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGmdssrpDQTSiVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd08530   6 KKLGKGSYGSVYKVKRLS------DNQV-YALKEVNlGSLSQKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd08530  78 MEYAPFGDLSKLISKRK------------KKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHhiDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFSLLREGhRME 557
Cdd:cd08530 146 DLGISKVLK--KNLAKTQIGT-PL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMATF-RPPFEARTMQELRYKVCRG-KFP 219
                       250       260       270
                ....*....|....*....|....*....|.
gi 204138   558 RPPNCPS-ELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd08530 220 PIPPVYSqDLQQIIRSLLQVNPKKRPSCDKL 250
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
367-586 6.13e-27

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 110.56  E-value: 6.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   367 SEMEMMKLIG--RHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpDLSPDGPRSSegplsfpalvSCAYQV 444
Cdd:cd13992  42 TILQELNQLKelVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNR-----EIKMDWMFKS----------SFIKDI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   445 ARGMQYL-ESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVH-HIDYYKKTSNGRLPVKWMAPEALFDRVYTH----QS 518
Cdd:cd13992 107 VKGMNYLhSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEeQTNHQLDEDAQHKKLLWTAPELLRGSLLEVrgtqKG 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   519 DVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERP------PNCPSELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd13992 187 DVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFRPelavllDEFPPRLVLLVKQCWAENPEKRPSFKQ 260
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
321-589 1.12e-26

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 109.83  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdssRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd06611  13 LGDGAFGKVYKA--------QHKETGLFAAAKIIQIESEEELEDFMVEIDILSEC-KHPNIVGLYEAYFYENKLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRArrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd06611  84 CDGGALDSIMLE---------------LERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGILLWEIfTLGGSPYPGI-PVEELFSLLR-EG 553
Cdd:cd06611 149 VSAKNKSTLQKRDTFIGT-PY-WMAPEVVAcetfkDNPYDYKADIWSLGITLIEL-AQMEPPHHELnPMRVLLKILKsEP 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 204138   554 HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06611 226 PTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLK 261
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
321-589 1.18e-26

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 109.28  E-value: 1.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaEALGMDSSRpdqtsIVAVKMLKdnaSDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd06612  11 LGEGSYGSVY--KAIHKETGQ-----VVAIKVVP---VEEDLQEIIKEISILKQC-DSPYIVKYYGSYFKNTDLWIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd06612  80 CGAGSVSDIMKIT---------------NKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLReghrmeRP 559
Cdd:cd06612 145 VSGQLTDTMAKRNTVIGT-PF-WMAPEVIQEIGYNNKADIWSLGITAIEMAE-GKPPYSDIhPMRAIFMIPN------KP 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   560 PNC---PS----ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06612 216 PPTlsdPEkwspEFNDFVKKCLVKDPEERPSAIQLLQ 252
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
313-583 1.79e-26

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 109.01  E-value: 1.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGQVVCAEALGmdssrpdQTsiVAVKMLKdnASDKDLADLIS---EMEMMKLigRHKNIINLLG--- 386
Cdd:cd13979   3 EPLRLQEPLGSGGFGSVYKATYKG-------ET--VAVKIVR--RRRKNRASRQSfwaELNAARL--RHENIVRVLAaet 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQEGPLYVIVEYAAKGNLREFLRARRPPGPdlspdgprssegpLSFPALVSCAyqVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd13979  70 GTDFASLGLIIMEYCGNGTLQQLIYEGSEPLP-------------LAHRILISLD--IARALRFCHSHGIVHLDVKPANI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFG---LARGVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPV 543
Cdd:cd13979 135 LISEQGVCKLCDFGcsvKLGEGNEVGTPRSHIGGTY--TYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQ 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   544 EELFSLLREGHRMERPPNCPSE----LYGLMRECWHAAPSQRPT 583
Cdd:cd13979 212 HVLYAVVAKDLRPDLSGLEDSEfgqrLRSLISRCWSAQPAERPN 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
321-587 2.73e-26

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 108.41  E-value: 2.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSrpDQTSiVAVKMLK------------DNASDKD-LADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd14008   1 LGRGSFGKVK----LALDTE--TGQL-YAIKIFNksrlrkrregknDRGKIKNaLDDVRREIAIMKKL-DHPNIVRLYEV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CT--QEGPLYVIVEYAakgnlreflrarrPPGPDLSPDGPRSSEgPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARN 465
Cdd:cd14008  73 IDdpESDKLYLVLEYC-------------EGGPVMELDSGDRVP-PLPEETARKYFRDLVLGLEYLHENGIVHRDIKPEN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEaLFDRVYTHQS----DVWSFGILLWeIFTLGGSPYPGI 541
Cdd:cd14008 139 LLLTADGTVKISDFGVSEMFEDGNDTLQKTAGT-PA-FLAPE-LCDGDSKTYSgkaaDIWALGVTLY-CLVFGRLPFNGD 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   542 PVEELFSLLREGHRM-ERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14008 215 NILELYEAIQNQNDEfPIPPELSPELKDLLRRMLEKDPEKRITLKEI 261
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
316-589 3.04e-26

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 107.71  E-value: 3.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKpLGEGCFGQVVCAEalgmdSSRPDQtsIVAVKMLKDNASDKDLAdlISEMEMMKLIG---RHKNIINLLGVCTQEG 392
Cdd:cd05118   3 VLRK-IGEGAFGTVWLAR-----DKVTGE--KVAIKKIKNDFRHPKAA--LREIKLLKHLNdveGHPNIVKLLDVFEHRG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 P--LYVIVEYAaKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd05118  73 GnhLCLVFELM-GMNLYELIKDYPRG---------------LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DD-VMKIADFGLARGVHHIDYYKKTSngrlPVKWMAPEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPGI-PVEEL 546
Cdd:cd05118 137 ELgQLKLADFGLARSFTSPPYTPYVA----TRWYRAPEVLLgAKPYGSSIDIWSLGCILAELLT--GRPlFPGDsEVDQL 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   547 FSLLRE-GhrmerppncPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd05118 211 AKIVRLlG---------TPEALDLLSKMLKYDPAKRITASQALA 245
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
321-584 3.61e-26

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 107.69  E-value: 3.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALgmdssrpDQTSIVAVK-MLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd14009   1 IGRGSFATVWKGRHK-------QTGEVVAIKeISRKKLNKKLQENLESEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD---VMKI 476
Cdd:cd14009  73 YCAGGDLSQYIRKR----------------GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDyYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLREGHR 555
Cdd:cd14009 137 ADFGFARSLQPAS-MAETLCGS-PL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRGSnHVQLLRNIERSDAV 212
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   556 MERP------PNCPSELYGLMRecwhAAPSQRPTF 584
Cdd:cd14009 213 IPFPiaaqlsPDCKDLLRRLLR----RDPAERISF 243
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
321-540 4.09e-26

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 108.34  E-value: 4.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssrpDQTS--IVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd07829   7 LGEGTYGVVYKAK---------DKKTgeIVALKKIRlDNEEEGIPSTALREISLLKEL-KHPNIVKLLDVIHTENKLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKgNLREFLRARRPPGPdlspdgprssegplsfPALVSC-AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd07829  77 FEYCDQ-DLKKYLDKRPGPLP----------------PNLIKSiMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKL 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   477 ADFGLARGVHHidyykktsngrlPVK---------WM-APEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPG 540
Cdd:cd07829 140 ADFGLARAFGI------------PLRtythevvtlWYrAPEILLgSKHYSTAVDIWSVGCIFAELIT--GKPlFPG 201
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
314-589 6.16e-26

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 107.47  E-value: 6.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVcaeaLGMDSSRPDqtsIVAVKMLKDNASDKDLAD---------LISEMEMMKLIgRHKNIINL 384
Cdd:cd06629   2 KWVKGELIGKGTYGRVY----LAMNATTGE---MLAVKQVELPKTSSDRADsrqktvvdaLKSEIDTLKDL-DHPNIVQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   385 LGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLspdgprssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAAR 464
Cdd:cd06629  74 LGFEETEDYFSIFLEYVPGGSIGSCLRKYGKFEEDL----------------VRFFTRQILDGLAYLHSKGILHRDLKAD 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEAL--FDRVYTHQSDVWSFGILLWEIFTlGGSPYPgiP 542
Cdd:cd06629 138 NILVDLEGICKISDFGISKKSDDIYGNNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLA-GRRPWS--D 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   543 VEELFSLLREGHRMERPP-----NCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06629 215 DEAIAAMFKLGNKRSAPPvpedvNLSPEALDFLNACFAIDPRDRPTAAELLS 266
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
321-583 6.49e-26

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 107.64  E-value: 6.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEaLGMDSSrpdqTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd05086   5 IGNGWFGKVLLGE-IYTGTS----VARVVVKELKASANPKEQDDFLQQGEPYYIL-QHPNILQCVGQCVEAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRppgpdlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd05086  79 CDLGDLKTYLANQQ-----------EKLRGDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRLPVKWMAPE---ALFDRVY----THQSDVWSFGILLWEIFTLGGSPYPGIPVEELFS-LLRE 552
Cdd:cd05086 148 IGFSRYKEDYIETDDKKYAPLRWTAPElvtSFQDGLLaaeqTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNhVIKE 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   553 ghRMERPPNCPSEL------YGLMRECWhAAPSQRPT 583
Cdd:cd05086 228 --RQVKLFKPHLEQpysdrwYEVLQFCW-LSPEKRPT 261
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
347-594 7.21e-26

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 107.22  E-value: 7.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   347 IVAVKMLKDnasDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLrARRppgpdlspdgpr 426
Cdd:cd14156  20 VMVVKIYKN---DVDQHKIVREISLLQKL-SHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL-ARE------------ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   427 ssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK---IADFGLARGVhhidyykktsnGRLPVK- 502
Cdd:cd14156  83 --ELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREV-----------GEMPANd 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   503 ------------WMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRmERPPNCPSELYGLM 570
Cdd:cd14156 150 perklslvgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFGLDVQAFK-EMVPGCPEPFLDLA 228
                       250       260
                ....*....|....*....|....
gi 204138   571 RECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14156 229 ASCCRMDAFKRPSFAELLDELEDI 252
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
304-589 8.09e-26

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 107.81  E-value: 8.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   304 LDP--LWEfprdrlVLGKpLGEGCFGQVVCAealgmdssRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNI 381
Cdd:cd06644   8 LDPneVWE------IIGE-LGDGAFGKVYKA--------KNKETGALAAAKVIETKSEEELEDYMVEIEILATCN-HPYI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   382 INLLGVCTQEGPLYVIVEYAAKGNLREFLrarrppgpdLSPDgprssEGpLSFPALVSCAYQVARGMQYLESRKCIHRDL 461
Cdd:cd06644  72 VKLLGAFYWDGKLWIMIEFCPGGAVDAIM---------LELD-----RG-LTEPQIQVICRQMLEALQYLHSMKIIHRDL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGL-ARGVHHIDyyKKTSNGRLPVkWMAPEALF-----DRVYTHQSDVWSFGILLWEIFTLGG 535
Cdd:cd06644 137 KAGNVLLTLDGDIKLADFGVsAKNVKTLQ--RRDSFIGTPY-WMAPEVVMcetmkDTPYDYKADIWSLGITLIEMAQIEP 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   536 SPYPGIPVEELFSLLReghrmERPP--NCPS----ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06644 214 PHHELNPMRVLLKIAK-----SEPPtlSQPSkwsmEFRDFLKTALDKHPETRPSAAQLLE 268
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
321-587 1.06e-25

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 106.57  E-value: 1.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVvcAEALgmdssrpDQTSI--VAVKMLKDNASDK---DLADLISEMEMMKLIgRHKNIINLLGVCTQE--GP 393
Cdd:cd14119   1 LGEGSYGKV--KEVL-------DTETLcrRAVKILKKRKLRRipnGEANVKREIQILRRL-NHRNVIKLVDVLYNEekQK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAkGNLREFLrarrppgpDLSPDGprssegplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd14119  71 LYMVMEYCV-GGLQEML--------DSAPDK--------RLPIWQAHGYfvQLIDGLEYLHSQGIIHKDIKPGNLLLTTD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLARGVHHI--DYYKKTSNGRlPvKWMAPE-ALFDRVYT-HQSDVWSFGILLWEIFTlGGSPYPGIPVEELF 547
Cdd:cd14119 134 GTLKISDFGVAEALDLFaeDDTCTTSQGS-P-AFQPPEiANGQDSFSgFKVDIWSAGVTLYNMTT-GKYPFEGDNIYKLF 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   548 SLLREGhRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14119 211 ENIGKG-EYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
319-589 2.40e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 105.43  E-value: 2.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEAlGMDSSRPDQTSIVAVKM-LKDNASDKDLADLISEMEmmkligrHKNIINLLGVCTQEGPLYVI 397
Cdd:cd08225   6 KKIGEGSFGKIYLAKA-KSDSEHCVIKEIDLTKMpVKEKEASKKEVILLAKMK-------HPNIVTFFASFQENGRLFIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREflRARRPPGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD-VMKI 476
Cdd:cd08225  78 MEYCDGGDLMK--RINRQRGVLFSED------------QILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGmVAKL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFSLLREGHRM 556
Cdd:cd08225 144 GDFGIARQLNDSMELAYTCVGT-PY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFA 220
                       250       260       270
                ....*....|....*....|....*....|...
gi 204138   557 ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd08225 221 PISPNFSRDLRSLISQLFKVSPRDRPSITSILK 253
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
308-589 2.60e-25

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 106.26  E-value: 2.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEfprdrlVLGKpLGEGCFGQVVCAEAlgmdssrpDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGrHKNIINLLGV 387
Cdd:cd06643   7 WE------IVGE-LGDGAFGKVYKAQN--------KETGILAAAKVIDTKSEEELEDYMVEIDILASCD-HPNIVKLLDA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd06643  71 FYYENNLWILIEFCAGGAVDAVML---------------ELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNIL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLA----RGVHHIDYYKKTSngrlpvKWMAPEALF-----DRVYTHQSDVWSFGILLWEIFTLGGSPY 538
Cdd:cd06643 136 FTLDGDIKLADFGVSakntRTLQRRDSFIGTP------YWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIEPPHH 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   539 PGIPVEELFSLLR-EGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06643 210 ELNPMRVLLKIAKsEPPTLAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQ 261
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
316-553 2.64e-25

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 105.25  E-value: 2.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVcaeaLGMDSSRPDQtsiVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd05117   3 ELGKVLGRGSFGVVR----LAVHKKTGEE---YAVKIIdKKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT---ED 471
Cdd:cd05117  75 YLVMELCTGGELFDRI----------------VKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPD 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLARGVHHiDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLweiFTL--GGSPYPGIPVEELFSL 549
Cdd:cd05117 139 SPIKIIDFGLAKIFEE-GEKLKTVCGTP--YYVAPEVLKGKGYGKKCDIWSLGVIL---YILlcGYPPFYGETEQELFEK 212

                ....
gi 204138   550 LREG 553
Cdd:cd05117 213 ILKG 216
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
315-589 3.36e-25

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 105.37  E-value: 3.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQV--VCaealgmdsSRPDQtSIVAVKMLKDNASDKDLADLISEMEMMkLIGRHKNIINLLGVCTQEG 392
Cdd:cd06623   3 LERVKVLGQGSSGVVykVR--------HKPTG-KIYALKKIHVDGDEEFRKQLLRELKTL-RSCESPYVVKCYGAFYKEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLES-RKCIHRDLAARNVLVTED 471
Cdd:cd06623  73 EISIVLEYMDGGSLADLLKKV----------------GKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELFSLLR 551
Cdd:cd06623 137 GEVKIADFGISKVLENTLDQCNTFVG--TVTYMSPERIQGESYSYAADIWSLGLTLLE-CALGKFPFLPPGQPSFFELMQ 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   552 E---GHRMERPPNCPS-ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06623 214 AicdGPPPSLPAEEFSpEFRDFISACLQKDPKKRPSAAELLQ 255
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
321-596 6.63e-25

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 104.64  E-value: 6.63e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdSSRPDQTSIVAVKMLK-DNASDKDLadlISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd14222   1 LGKGFFGQAIKV------THKATGKVMVMKELIRcDEETQKTF---LTEVKVMRSLD-HPNVLKFIGVLYKDKRLNLLTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd14222  71 FIEGGTLKDFLR----------------ADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADF 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLARGVhhIDYYKKTSNGRLPVK--------------------WMAPEALFDRVYTHQSDVWSFGILLWEIFtlgGSPYP 539
Cdd:cd14222 135 GLSRLI--VEEKKKPPPDKPTTKkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEII---GQVYA 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   540 G---IPVEELFSL-LREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVLL 596
Cdd:cd14222 210 DpdcLPRTLDFGLnVRLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALSL 270
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
320-589 1.01e-24

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 103.98  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   320 PLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd06610   8 VIGSGATAVVYAAYCLPKKE-------KVAIKRIDLEKCQTSMDELRKEIQAMSQC-NHPNVVSYYTSFVVGDELWLVMP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARRPpgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd06610  80 LLSGGSLLDIMKSSYP-------------RGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 G----LARGVHHIDYYKKTSNGRlPVkWMAPEALF-DRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGH 554
Cdd:cd06610 147 GvsasLATGGDRTRKVRKTFVGT-PC-WMAPEVMEqVRGYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLMLTLQND 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   555 rmerPPNCPSEL----YG-----LMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06610 224 ----PPSLETGAdykkYSksfrkMISLCLQKDPSKRPTAEELLK 263
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
315-593 2.76e-24

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 102.81  E-value: 2.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVVCAEALGMdssrpdqtsiVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEgP 393
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRGRWHGD----------VAIKLLNiDYLNEEQLEAFKEEVAAYKNT-RHDNLVLFMGACMDP-P 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGN-LREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14063  70 HLAIVTSLCKGRtLYSLIHERKEK---------------FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGR 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMkIADFGLArGVHHIDYYKKTSNG-RLPVKW---MAPEAL----FDRV------YTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd14063 135 VV-ITDFGLF-SLSGLLQPGRREDTlVIPNGWlcyLAPEIIralsPDLDfeeslpFTKASDVYAFGTVWYELLA-GRWPF 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   539 PGIPVEELFSLLREGHRMerPPN---CPSELYGLMRECWHAAPSQRPTFKQLVEALDK 593
Cdd:cd14063 212 KEQPAESIIWQVGCGKKQ--SLSqldIGREVKDILMQCWAYDPEKRPTFSDLLRMLER 267
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
318-587 2.79e-24

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 102.51  E-value: 2.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVCaealGMDSsrpdQTSIVAVKMLKDNASDKDLAD-----LISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd06631   6 GNVLGKGAYGTVYC----GLTS----TGQLIAVKQVELDTSDKEKAEkeyekLQEEVDLLKTL-KHVNIVGYLGTCLEDN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLrARRppgpdlspdgprsseGPLsfPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06631  77 VVSIFMEFVPGGSIASIL-ARF---------------GAL--EEPVFCRYtkQILEGVAYLHNNNVIHRDIKGNNIMLMP 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHIDYYKKTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFTlgGSPyPGIPVEEL 546
Cdd:cd06631 139 NGVIKLIDFGCAKRLCINLSSGSQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEMAT--GKP-PWADMNPM 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   547 FSLLREGHRMERPPNCPSELYGLMRE----CWHAAPSQRPTFKQL 587
Cdd:cd06631 216 AAIFAIGSGRKPVPRLPDKFSPEARDfvhaCLTRDQDERPSAEQL 260
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
343-586 3.49e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 101.98  E-value: 3.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   343 DQTSIVAVK-MLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdls 421
Cdd:cd14121  19 GAREVVAVKcVSKSSLNKASTENLLTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCSGGDLSRFIRSRR------- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   422 pdgpRSSEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD--VMKIADFGLARGVHHIDyyKKTSNGRL 499
Cdd:cd14121  91 ----TLPESTVR-----RFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKPND--EAHSLRGS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   500 PVkWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELFSLLREGHRMERPPN------CPSELYGLMREc 573
Cdd:cd14121 160 PL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKIRSSKPIEIPTRpelsadCRDLLLRLLQR- 236
                       250
                ....*....|...
gi 204138   574 whaAPSQRPTFKQ 586
Cdd:cd14121 237 ---DPDRRISFEE 246
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
316-587 5.96e-24

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 102.23  E-value: 5.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDNASDKDladlisemEMMKL--------IGRHKNIINLLGV 387
Cdd:cd07830   2 KVIKQLGDGTFGSVYLARNK-------ETGELVAIKKMKKKFYSWE--------ECMNLrevkslrkLNEHPNIVKLKEV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAaKGNLREFLRARRPpgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd07830  67 FRENDELYFVFEYM-EGNLYQLMKDRKG--------------KPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLL 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVH----HIDY-----YKktsngrlpvkwmAPEALF-DRVYTHQSDVWSFGILLWEIFTL---- 533
Cdd:cd07830 132 VSGPEVVKIADFGLAREIRsrppYTDYvstrwYR------------APEILLrSTSYSSPVDIWALGCIMAELYTLrplf 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   534 -G--------------GSP---------------------YPGIPVEELFsllreghrmerpPNCPSELYGLMRECWHAA 577
Cdd:cd07830 200 pGsseidqlykicsvlGTPtkqdwpegyklasklgfrfpqFAPTSLHQLI------------PNASPEAIDLIKDMLRWD 267
                       330
                ....*....|
gi 204138   578 PSQRPTFKQL 587
Cdd:cd07830 268 PKKRPTASQA 277
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
317-587 1.09e-23

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 100.56  E-value: 1.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd08529   4 ILNKLGKGSFGVVYKVV-------RKVDGRVYALKQIDiSRMSRKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKGKLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRARRppGPDLSPDGprssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd08529  76 IVMEYAENGDLHSLIKSQR--GRPLPEDQ------------IWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLggsPYPgIPVEELFSLLREGHR 555
Cdd:cd08529 142 IGDLGVAKILSDTTNFAQTIVGT-PY-YLSPELCEDKPYNEKSDVWALGCVLYELCTG---KHP-FEAQNQGALILKIVR 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 204138   556 MERPPNCPS---ELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd08529 216 GKYPPISASysqDLSQLIDSCLTKDYRQRPDTTEL 250
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
321-592 1.15e-23

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 100.68  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdssrpdqtSIVAVKMLKDNA----SDKDLadLISEMEMMKLIGrHKNIINLLGVCTQEGPLYV 396
Cdd:cd14064   1 IGSGSFGKVYKGRCRN---------KIVAIKRYRANTycskSDVDM--FCREVSILCRLN-HPCVIQFVGACLDDPSQFA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IV-EYAAKGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLE--SRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14064  69 IVtQYVSGGSLFSLLHEQKRV---------------IDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGH 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIDYYKKTSN-GRLpvKWMAPEaLFDRV--YTHQSDVWSFGILLWEIFTlGGSPY----PGIPVEEL 546
Cdd:cd14064 134 AVVADFGESRFLQSLDEDNMTKQpGNL--RWMAPE-VFTQCtrYSIKADVFSYALCLWELLT-GEIPFahlkPAAAAADM 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 204138   547 fsllreGHRMERPP---NCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14064 210 ------AYHHIRPPigySIPKPISSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
316-588 2.12e-23

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 100.10  E-value: 2.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGvCTQEGP- 393
Cdd:cd14069   4 DLVQTLGEGAFGEVFLAV-------NRNTEEAVAVKFVdMKRAPGDCPENIKKEVCIQKML-SHKNVVRFYG-HRREGEf 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLreFLRarrppgpdLSPD-GPRSSEGPLSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14069  75 QYLFLEYASGGEL--FDK--------IEPDvGMPEDVAQFYFQQLMA-------GLKYLHSCGITHRDIKPENLLLDEND 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVHHIDyYKKTSN---GRLPvkWMAPEALFDRVYTHQ-SDVWSFGILLWEIFTlGGSPY--PgIPVEEL 546
Cdd:cd14069 138 NLKISDFGLATVFRYKG-KERLLNkmcGTLP--YVAPELLAKKKYRAEpVDVWSCGIVLFAMLA-GELPWdqP-SDSCQE 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   547 FSLLREGHRMERPP--NCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd14069 213 YSDWKENKKTYLTPwkKIDTAALSLLRKILTENPNKRITIEDIK 256
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
317-527 2.13e-23

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 99.95  E-value: 2.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdSSRPDQTSIVAVKML-KDNASDKDLAD-LISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14080   4 LGKTIGEGSYSKVKLAE-----YTKSGLKEKVACKIIdKKKAPKDFLEKfLPRELEILRKL-RHPNIIQVYSIFERGSKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLS-------FpalvscaYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd14080  78 FIFMEYAEHGDLLEYIQKR----------------GALSesqariwF-------RQLALAVQYLHSLDIAHRDLKCENIL 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   468 VTEDDVMKIADFGLARgVHHIDYYKKTSN---GRLpvKWMAPEALFDRVYT-HQSDVWSFGILL 527
Cdd:cd14080 135 LDSNNNVKLSDFGFAR-LCPDDDGDVLSKtfcGSA--AYAAPEILQGIPYDpKKYDIWSLGVIL 195
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
311-589 2.37e-23

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 100.07  E-value: 2.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDNASDKDlaDLISEMEMMKLIGRHKNIINLLGVCTQ 390
Cdd:cd06608   4 PAGIFELVEVIGEGTYGKVYKARHK-------KTGQLAAIKIMDIIEDEEE--EIKLEINILRKFSNHPNIATFYGAFIK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGP------LYVIVEYAAKGNLREFLRARRPPGpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAAR 464
Cdd:cd06608  75 KDPpggddqLWLVMEYCGGGSVTDLVKGLRKKG------------KRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGILLWEIFTlGGSPYP 539
Cdd:cd06608 143 NILLTEEAEVKLVDFGVSAQLDSTLGRRNTFIGT-PY-WMAPEVIacdqqPDASYDARCDVWSLGITAIELAD-GKPPLC 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   540 GI-PVEELFSLLRE-GHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06608 220 DMhPMRALFKIPRNpPPTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELLE 271
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
347-587 2.88e-23

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 99.86  E-value: 2.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   347 IVAVKMLKDNASDKDLADLISEMEMMKLI--GRHKNIINLLGvCTQEGP-LYVIVEYAAKGNLREFLRArrppgpdlspd 423
Cdd:cd06917  28 VVALKVLNLDTDDDDVSDIQKEVALLSQLklGQPKNIIKYYG-SYLKGPsLWIIMDYCEGGSIRTLMRA----------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   424 gprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkW 503
Cdd:cd06917  96 ------GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTFVGT-PY-W 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   504 MAPEALFD-RVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREghrmERPPNCPSELYG-LMRE----CWHAA 577
Cdd:cd06917 168 MAPEVITEgKYYDTKADIWSLGITTYEMAT-GNPPYSDVDALRAVMLIPK----SKPPRLEGNGYSpLLKEfvaaCLDEE 242
                       250
                ....*....|
gi 204138   578 PSQRPTFKQL 587
Cdd:cd06917 243 PKDRLSADEL 252
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
346-587 3.81e-23

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 99.59  E-value: 3.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   346 SIVAVKMLKDNASDKDLADLIsEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRarrppGPDLSPDGP 425
Cdd:cd14042  31 NLVAIKKVNKKRIDLTREVLK-ELKHMRDL-QHDNLTRFIGACVDPPNICILTEYCPKGSLQDILE-----NEDIKLDWM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   426 -RSSegplsfpaLVscaYQVARGMQYL-ESRKCIHRDLAARNVLVTEDDVMKIADFGLA---RGVHHID----YYKKtsn 496
Cdd:cd14042 104 fRYS--------LI---HDIVKGMHYLhDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHsfrSGQEPPDdshaYYAK--- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   497 gRLpvkWMAPEALFDRVY----THQSDVWSFGILLWEIFTLGGsPYpGI------PVEELFSLLREGhrmERPP------ 560
Cdd:cd14042 170 -LL---WTAPELLRDPNPpppgTQKGDVYSFGIILQEIATRQG-PF-YEegpdlsPKEIIKKKVRNG---EKPPfrpsld 240
                       250       260
                ....*....|....*....|....*....
gi 204138   561 --NCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14042 241 elECPDEVLSLMQRCWAEDPEERPDFSTL 269
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
317-587 5.13e-23

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 98.97  E-value: 5.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQV-VCAEAlgmDSSRPdqtsiVAVKML----KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQE 391
Cdd:cd06625   4 QGKLLGQGAFGQVyLCYDA---DTGRE-----LAVKQVeidpINTEASKEVKALECEIQLLKNL-QHERIVQYYGCLQDE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPalVSCAY--QVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd06625  75 KSLSIFMEYMPGGSVKDEIKAY----------------GALTEN--VTRKYtrQILEGLAYLHSNMIVHRDIKGANILRD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVHHIdyykKTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEE 545
Cdd:cd06625 137 SNGNVKLGDFGASKRLQTI----CSSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAA 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   546 LFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd06625 213 IFKIATQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEEL 254
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
319-594 7.43e-23

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 98.55  E-value: 7.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVcaealgmdssRPDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGpLYVI 397
Cdd:cd14150   6 KRIGTGSFGTVF----------RGKWHGDVAVKILKvTEPTPEQLQAFKNEMQVLRKT-RHVNILLFMGFMTRPN-FAII 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRArrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd14150  74 TQWCEGSSLYRHLHV---------------TETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARgvhhidyYKKTSNGRLPVK-------WMAPEALF---DRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPV-EEL 546
Cdd:cd14150 139 DFGLAT-------VKTRWSGSQQVEqpsgsilWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNrDQI 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   547 FSLLREGHRM----ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14150 211 IFMVGRGYLSpdlsKLSSNCPKAMKRLLIDCLKFKREERPLFPQILVSIELL 262
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
319-529 1.99e-22

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 96.99  E-value: 1.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAealgmdssRPDQTS-IVAVKMLKDNASDkDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd06613   6 QRIGSGTYGDVYKA--------RNIATGeLAAVKVIKLEPGD-DFEIIQQEISMLKEC-RHPNIVAYFGSYLRRDKLWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRArrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd06613  76 MEYCGGGSLQDIYQV----------------TGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLA 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   478 DFGLARGVHHIDYYKKTSNGRLpvKWMAPEALFDR---VYTHQSDVWSFGILLWE 529
Cdd:cd06613 140 DFGVSAQLTATIAKRKSFIGTP--YWMAPEVAAVErkgGYDGKCDIWALGITAIE 192
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
331-594 2.11e-22

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 97.24  E-value: 2.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   331 CAEALGMDSSRPDQTSI-----VAVKMLKDNAS--DKDLADLISEMEMMKligrHKNIINLLGVCTQEGPLYVIVEYAAK 403
Cdd:cd14045  11 CTTAHNAQKKPFTQTGIydgrtVAIKKIAKKSFtlSKRIRKEVKQVRELD----HPNLCKFIGGCIEVPNVAIITEYCPK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   404 GNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLA- 482
Cdd:cd14045  87 GSLNDVLL---------------NEDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTt 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   483 ----RGVHHIDYYKKtsngRLPVKWMAPEA--LFDRVYTHQSDVWSFGILLWEIFTLGgSPYPG----------IPVEEL 546
Cdd:cd14045 152 yrkeDGSENASGYQQ----RLMQVYLPPENhsNTDTEPTQATDVYSYAIILLEIATRN-DPVPEddysldeawcPPLPEL 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   547 FSllreGHRMERPPnCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14045 227 IS----GKTENSCP-CPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
321-587 3.16e-22

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 96.93  E-value: 3.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSsRPDQtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd06609   9 IGKGSFGEVY----KGIDK-RTNQ--VVAIKVIDLEEAEDEIEDIQQEIQFLSQC-DSPYITKYYGSFLKGSKLWIIMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRarrpPGPDlspdgprsSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd06609  81 CGGGSVLDLLK----PGPL--------DETYIAF-----ILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSLLReghrmERP 559
Cdd:cd06609 144 VSGQLTSTMSKRNTFVGT-PF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLhPMRVLFLIPK-----NNP 215
                       250       260       270
                ....*....|....*....|....*....|...
gi 204138   560 PNCPSELY-----GLMRECWHAAPSQRPTFKQL 587
Cdd:cd06609 216 PSLEGNKFskpfkDFVELCLNKDPKERPSAKEL 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
321-594 4.96e-22

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 96.41  E-value: 4.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaealgmdSSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14664   1 IGRGGAGTVY--------KGVMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMI-RHRNIVRLRGYCSNPTTNLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARRPPGPdlspdgprssegPLSFPALVSCAYQVARGMQYLE---SRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd14664  72 MPNGSLGELLHSRPESQP------------PLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVA 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKKTSNgRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd14664 140 DFGLAKLMDDKDSHVMSSV-AGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIVDWVRGLL 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 204138   558 RPPNCPSEL------YGLMRE----------CWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14664 218 EEKKVEALVdpdlqgVYKLEEveqvfqvallCTQSSPMERPTMREVVRMLEGD 270
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
313-551 9.38e-22

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 96.92  E-value: 9.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQ 390
Cdd:cd05619   5 EDFVLHKMLGKGSFGKVFLAELKGTNQ-------FFAIKALKKDVvlMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRppgpdlSPDGPRSSegplSFPALVSCayqvarGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd05619  78 KENLFFVMEYLNGGDLMFHIQSCH------KFDLPRAT----FYAAEIIC------GLQFLHSKGIVYRDLKLDNILLDK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELFSLL 550
Cdd:cd05619 142 DGHIKIADFGMCK--ENMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQSI 218

                .
gi 204138   551 R 551
Cdd:cd05619 219 R 219
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
321-587 9.53e-22

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 95.02  E-value: 9.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVvcaealgmDSSRPDQTSIVAVKML-KDNASD-KDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14161  11 LGKGTYGRV--------KKARDSSGRLVAIKSIrKDRIKDeQDLLHIRREIEIMSSLN-HPHIISVYEVFENSSKIVIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRPpgpdLSpdgprSSEGPLSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd14161  82 EYASRGDLYDYISERQR----LS-----ELEARHFFRQIVS-------AVHYCHANGIVHRDLKLENILLDANGNIKIAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLArGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTH-QSDVWSFGILLWeIFTLGGSPYPGIPVEELFSLLREGHRme 557
Cdd:cd14161 146 FGLS-NLYNQDKFLQTYCGS-PL-YASPEIVNGRPYIGpEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGAY-- 219
                       250       260       270
                ....*....|....*....|....*....|
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14161 220 REPTKPSDACGLIRWLLMVNPERRATLEDV 249
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
308-592 1.87e-21

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 94.71  E-value: 1.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVLGKPLGEGCFGQVVCAEALGMdssrpdqtsiVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLG 386
Cdd:cd14149   7 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD----------VAVKILKvVDPTPEQFQAFRNEVAVLRKT-RHVNILLFMG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQeGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNV 466
Cdd:cd14149  76 YMTK-DNLAIVTQWCEGSSLYKHLHVQ---------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   467 LVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALF---DRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-P 542
Cdd:cd14149 140 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GELPYSHInN 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 204138   543 VEELFSLLREGHRM----ERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14149 219 RDQIIFMVGRGYASpdlsKLYKNCPKAMKRLVADCIKKVKEERPLFPQILSSIE 272
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
312-594 2.85e-21

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 94.49  E-value: 2.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVcaeaLGMDSSRpdqtsIVAVKMLKD--NASDKDLADLI-SEMEMMKLIgRHKNIINLLGvC 388
Cdd:cd14158  14 RPISVGGNKLGEGGFGVVF----KGYINDK-----NVAVKKLAAmvDISTEDLTKQFeQEIQVMAKC-QHENLVELLG-Y 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   389 TQEGPLYVIV-EYAAKGNLREFLRARrppgpDLSPdgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd14158  83 SCDGPQLCLVyTYMPNGSLLDRLACL-----NDTP--------PLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANIL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVyTHQSDVWSFGILLWEIFTlgGSPypgiPVEE-- 545
Cdd:cd14158 150 LDETFVPKISDFGLARASEKFSQTIMTERIVGTTAYMAPEALRGEI-TPKSDIFSFGVVLLEIIT--GLP----PVDEnr 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   546 ---LFSLLREGHRMER--------------PPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14158 223 dpqLLLDIKEEIEDEEktiedyvdkkmgdwDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
317-589 3.31e-21

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 93.48  E-value: 3.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAealgmdssRPDQTS-IVAVKMLKDNASDKDLAD--LISEMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:cd14116   9 IGRPLGKGKFGNVYLA--------REKQSKfILALKVLFKAQLEKAGVEhqLRREVEIQSHL-RHPNILRLYGYFHDATR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNL-REFLRARRppgpdlspdgprssegplsFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd14116  80 VYLILEYAPLGTVyRELQKLSK-------------------FDEQRTATYitELANALSYCHSKRVIHRDIKPENLLLGS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLArgVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELFsll 550
Cdd:cd14116 141 AGELKIADFGWS--VHAPSSRRTTLCGTL--DYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETY--- 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   551 REGHRME--RPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14116 213 KRISRVEftFPDFVTEGARDLISRLLKHNPSQRPMLREVLE 253
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
319-594 3.31e-21

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 94.26  E-value: 3.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGmdssrpdqtSIVAVKML--KDNASDKDLADlISEMEMMkligRHKNIINL-------LGVCT 389
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRG---------EKVAVKIFssRDEDSWFRETE-IYQTVML----RHENILGFiaadiksTGSWT 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QegpLYVIVEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYL------ESRK--CIHRDL 461
Cdd:cd14056  67 Q---LWLITEYHEHGSLYDYL-----------------QRNTLDTEEALRLAYSAASGLAHLhteivgTQGKpaIAHRDL 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   462 AARNVLVTEDDVMKIADFGLArgvhhIDYYKKTSNGRLP-------VKWMAPEALFDRVYTH------QSDVWSFGILLW 528
Cdd:cd14056 127 KSKNILVKRDGTCCIADLGLA-----VRYDSDTNTIDIPpnprvgtKRYMAPEVLDDSINPKsfesfkMADIYSFGLVLW 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   529 EIFTLGGS---------PYPGI----P-VEELFSLLREghRMERPP------NCP--SELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd14056 202 EIARRCEIggiaeeyqlPYFGMvpsdPsFEEMRKVVCV--EKLRPPipnrwkSDPvlRSMVKLMQECWSENPHARLTALR 279

                ....*...
gi 204138   587 LVEALDKV 594
Cdd:cd14056 280 VKKTLAKL 287
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
317-583 3.47e-21

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 93.49  E-value: 3.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdsSRPDQTsIVAVKMLK--DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd08224   4 IEKKIGKGQFSVVYRAR------CLLDGR-LVALKKVQifEMMDAKARQDCLKEIDLLQQL-NHPNIIKYLASFIENNEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRPPGPdlspdgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd08224  76 NIVLELADAGDLSRLIKHFKKQKR------------LIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVV 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARgvhhidYYK-KTSNGRLPVK---WMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGiPVEELFSLL 550
Cdd:cd08224 144 KLGDLGLGR------FFSsKTTAAHSLVGtpyYMSPERIREQGYDFKSDIWSLGCLLYEMAAL-QSPFYG-EKMNLYSLC 215
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   551 REGHRMERPPnCPSELY-----GLMRECWHAAPSQRPT 583
Cdd:cd08224 216 KKIEKCEYPP-LPADLYsqelrDLVAACIQPDPEKRPD 252
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
321-592 4.83e-21

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 93.09  E-value: 4.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDssrpdqtsiVAVKMLKDNASDKDLADLISEMEMMkligRHKNIINLLGVCTQegPLYVIVEY 400
Cdd:cd14068   2 LGDGGFGSVYRAVYRGED---------VAVKIFNKHTSFRLLRQELVVLSHL----HHPSLVALLAAGTA--PRMLVMEL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV-----TEDDVMK 475
Cdd:cd14068  67 APKGSLDALLQ---------------QDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAK 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARgvHHIDYYKKTSNGRLPVKwmAPE-ALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGH 554
Cdd:cd14068 132 IADYGIAQ--YCCRMGIKTSEGTPGFR--APEvARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQG 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   555 RMERPP---NCP--SELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14068 208 KLPDPVkeyGCApwPGVEALIKDCLKENPQCRPTSAQVFDILN 250
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
321-600 5.14e-21

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 93.44  E-value: 5.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLiGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14026   5 LSRGAFGTVSRAR-------HADWRVTVAIKCLKLDSpvGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGIVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppGPDLSPDgprssegpLSFPALVSCAYQVARGMQYLE--SRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd14026  77 EYMTNGSLNELLH-----EKDIYPD--------VAWPLRLRILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGvHHIDYYKKTSNGRLP----VKWMAPEALFDRVYTHQS---DVWSFGILLWEIFTLgGSPYPGI--PVEELF 547
Cdd:cd14026 144 ADFGLSKW-RQLSISQSRSSKSAPeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSR-KIPFEEVtnPLQIMY 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   548 SLLReGHRMER-----PPNCPSE--LYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSE 600
Cdd:cd14026 222 SVSQ-GHRPDTgedslPVDIPHRatLINLIESGWAQNPDERPSFLKCLIELEPVLRTFDE 280
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
319-547 5.88e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 94.20  E-value: 5.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGvCTQ-EGPLY 395
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDE-------LYAIKVLKKEViiEDDDVECTMTEKRVLALANRHPFLTGLHA-CFQtEDRLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLR-EFLRARRppgpdlspdgprssegplsFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd05570  73 FVMEYVNGGDLMfHIQRARR-------------------FTEERARFYaaEICLALQFLHERGIIYRDLKLDNVLLDAEG 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   473 VMKIADFGLARgvHHIDYYKKTSN--GRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELF 547
Cdd:cd05570 134 HIKIADFGMCK--EGIWGGNTTSTfcGTP--DYIAPEILREQDYGFSVDWWALGVLLYE-MLAGQSPFEGDDEDELF 205
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
321-540 6.49e-21

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 93.40  E-value: 6.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSsrpdqtsIVAVK-MLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGP------ 393
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGE-------LVALKkIRMENEKEGFPITAIREIKLLQKL-DHPNVVRLKEIVTSKGSakykgs 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAakgnlrEFlrarrppgpDLSpdG-PRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd07840  79 IYMVFEYM------DH---------DLT--GlLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDG 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   473 VMKIADFGLARgvhhidYYKKTSNGRLPVK----WM-APEALF-DRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd07840 142 VLKLADFGLAR------PYTKENNADYTNRvitlWYrPPELLLgATRYGPEVDMWSVGCILAELFT-GKPIFQG 208
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
314-586 1.04e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 93.02  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVcaeaLGMDSSRpDQtsIVAVKMLKDN--ASDKDLADL--ISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd07841   1 RYEKGKKLGEGTYAVVY----KARDKET-GR--IVAIKKIKLGerKEAKDGINFtaLREIKLLQEL-KHPNIIGLLDVFG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAkGNLREFLRARRppgpdlspdgprssegpLSF-PALVSC-AYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd07841  73 HKSNINLVFEFME-TDLEKVIKDKS-----------------IVLtPADIKSyMLMTLRGLEYLHSNWILHRDLKPNNLL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARgVHHIDYYKKTSNgrLPVKWM-APEALFD-RVYTHQSDVWSFGILLWE---------------- 529
Cdd:cd07841 135 IASDGVLKLADFGLAR-SFGSPNRKMTHQ--VVTRWYrAPELLFGaRHYGVGVDMWSVGCIFAElllrvpflpgdsdidq 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   530 ---IFTLGGSP-------------------YPGIPVEELFsllreghrmerpPNCPSELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd07841 212 lgkIFEALGTPteenwpgvtslpdyvefkpFPPTPLKQIF------------PAASDDALDLLQRLLTLNPNKRITARQ 278
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
315-588 1.06e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 92.31  E-value: 1.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVVCAEALGMDSSRPDQTSI-----VAVKMLKDNASDKDLAdLISEMEMMKLIGrHKNIINLLGVCT 389
Cdd:cd05077   1 IVQGEHLGRGTRTQIYAGILNYKDDDEDEGYSYekeikVILKVLDPSHRDISLA-FFETASMMRQVS-HKHIVLLYGVCV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgpRSSEgPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd05077  79 RDVENIMVEEFVEFGPLDLFMH--------------RKSD-VLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDV-------MKIADFGLARGVhhidYYKKTSNGRLPvkWMAPEALFD-RVYTHQSDVWSFGILLWEIFTLGGSPYPGI 541
Cdd:cd05077 144 REGIdgecgpfIKLSDPGIPITV----LSRQECVERIP--WIAPECVEDsKNLSIAADKWSFGTTLWEICYNGEIPLKDK 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   542 PVEELfSLLREGHRMERPPNCpSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd05077 218 TLAEK-ERFYEGQCMLVTPSC-KELADLMTHCMNYDPNQRPFFRAIM 262
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
321-589 1.65e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 91.45  E-value: 1.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV--VcaealgmdSSRPDQtSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLG--VCTQEGPLY 395
Cdd:cd08217   8 IGKGSFGTVrkV--------RRKSDG-KILVWKEIDyGKMSEKEKQQLVSEVNILREL-KHPNIVRYYDriVDRANTTLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFL-RARRppgpdlspDGPRSSEgplsfPALVSCAYQVARGMQYLESR-----KCIHRDLAARNVLVT 469
Cdd:cd08217  78 IVMEYCEGGDLAQLIkKCKK--------ENQYIPE-----EFIWKIFTQLLLALYECHNRsvgggKILHRDLKPANIFLD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFSL 549
Cdd:cd08217 145 SDNNVKLGDFGLARVLSHDSSFAKTYVGT-PY-YMSPELLNEQSYDEKSDIWSLGCLIYELCAL-HPPFQAANQLELAKK 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   550 LREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd08217 222 IKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
321-589 1.90e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 91.65  E-value: 1.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSrpdQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRhKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd06640  12 IGKGSFGEVF----KGIDNR---TQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDS-PYVTKYYGSYLKGTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRArrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd06640  84 LGGGSALDLLRA-----------------GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYPGI-PVEELFSLlreghrmerP 559
Cdd:cd06640 147 VAGQLTDTQIKRNTFVGT-PF-WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMhPMRVLFLI---------P 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   560 PNCPSELYG--------LMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06640 215 KNNPPTLVGdfskpfkeFIDACLNKDPSFRPTAKELLK 252
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
321-589 2.05e-20

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 91.66  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSRPDqtsIVAVKMLKDNASDKDLADLISEMEMMKLIGRhKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd06642  12 IGKGSFGEVY----KGIDNRTKE---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDS-PYITRYYGSYLKGTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRArrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd06642  84 LGGGSALDLLKP-----------------GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYPGI-PVEELFSLlreghrmerP 559
Cdd:cd06642 147 VAGQLTDTQIKRNTFVGT-PF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLhPMRVLFLI---------P 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   560 PNCPSELYG--------LMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06642 215 KNSPPTLEGqhskpfkeFVEACLNKDPRFRPTAKELLK 252
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
316-589 2.92e-20

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 91.33  E-value: 2.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKpLGEGCFGQVvcaealgMDSSRPDQTSIVAVKMLKDNASDKDLADL-ISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd07846   5 NLGL-VGEGSYGMV-------MKCRHKETGQIVAIKKFLESEDDKMVKKIaMREIKMLKQL-RHENLVNLIEVFRRKKRW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRArrppgpdlsPDGprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd07846  76 YLVFEFVDHTVLDDLEKY---------PNG-------LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLAR-----GVHHIDYykktsngrLPVKWM-APEALF-DRVYTHQSDVWSFGILLWEIFTlgGSPY-PG------ 540
Cdd:cd07846 140 KLCDFGFARtlaapGEVYTDY--------VATRWYrAPELLVgDTKYGKAVDVWAVGCLVTEMLT--GEPLfPGdsdidq 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   541 -----------IP-VEELFSLLREGHRMERP------------PNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd07846 210 lyhiikclgnlIPrHQELFQKNPLFAGVRLPevkeveplerryPKLSGVVIDLAKKCLHIDPDKRPSCSELLH 282
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
321-589 4.18e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 90.48  E-value: 4.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdSSRPDQTsIVAVKMLKDNASDKDLADLISEMEMMkligrHK----NIINLLGVCTQEGPLYV 396
Cdd:cd06605   9 LGEGNGGVVSKV------RHRPSGQ-IMAVKVIRLEIDEALQKQILRELDVL-----HKcnspYIVGFYGAFYSEGDISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYL-ESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd06605  77 CMEYMDGGSLDKILK----------------EVGRIPERILGKIAVAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQVK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVhhIDYYKKTSNGRLPvkWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYPGIPVEE---LFSLLRE 552
Cdd:cd06605 141 LCDFGVSGQL--VDSLAKTFVGTRS--YMAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFPYPPPNAKPsmmIFELLSY 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   553 GHRMErPPNCPS-----ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06605 216 IVDEP-PPLLPSgkfspDFQDFVSQCLQKDPTERPSYKELME 256
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
364-587 4.83e-20

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 90.16  E-value: 4.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   364 DLISEMEMMkligRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpDLSPDGPRSSegplsfpalvSCAYQ 443
Cdd:cd14043  45 NVFSKLREL----RHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRND-----DMKLDWMFKS----------SLLLD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   444 VARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVKWMAPEALFDRVY----THQSD 519
Cdd:cd14043 106 LIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEILEAQNLPLPEPAPE-ELLWTAPELLRDPRLerrgTFPGD 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   520 VWSFGILLWEIFTLGGsPYP--GIPVEELFSLLReghrmERPPNC---------PSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14043 185 VFSFAIIMQEVIVRGA-PYCmlGLSPEEIIEKVR-----SPPPLCrpsvsmdqaPLECIQLMKQCWSEAPERRPTFDQI 257
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
311-606 5.18e-20

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 90.58  E-value: 5.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKpLGEGCFGQVVCAEalgmdsSRPDQTsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd06620   4 NQDLETLKD-LGAGNGGSVSKVL------HIPTGT-IMAKKVIHIDAKSSVRKQILRELQILHEC-HSPYIVSFYGAFLN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVI-VEYAAKGNLreflrarrppgpdlspDGPRSSEGPLSFPALVSCAYQVARGMQYL-ESRKCIHRDLAARNVLV 468
Cdd:cd06620  75 ENNNIIIcMEYMDCGSL----------------DKILKKKGPFPEEVLGKIAVAVLEGLTYLyNVHRIIHRDIKPSNILV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHH--IDYYKKTSNgrlpvkWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYPGIPVEEL 546
Cdd:cd06620 139 NSKGQIKLCDFGVSGELINsiADTFVGTST------YMSPERIQGGKYSVKSDVWSLGLSIIEL-ALGEFPFAGSNDDDD 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   547 FSLLREG-----HRM--ERPPNCPS------ELYGLMRECWHAAPSQRPTFKQLvEALDKVLLAVSEEYLDLR 606
Cdd:cd06620 212 GYNGPMGildllQRIvnEPPPRLPKdrifpkDLRDFVDRCLLKDPRERPSPQLL-LDHDPFIQAVRASDVDLR 283
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
313-589 6.40e-20

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 90.16  E-value: 6.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKplgeGCFGQVVCAEALGmdssrpDQTSIvAVKMLkdnaSDKDLADLISEMEMMKLIGR--HKNIINLLGVCTQ 390
Cdd:cd06624  12 ERVVLGK----GTFGVVYAARDLS------TQVRI-AIKEI----PERDSREVQPLHEEIALHSRlsHKNIVQYLGSVSE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRPPGPDlspdgprsSEGPLSFpalvscaY--QVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd06624  77 DGFFKIFMEQVPGGSLSALLRSKWGPLKD--------NENTIGY-------YtkQILEGLKYLHDNKIVHRDIKGDNVLV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 -TEDDVMKIADFGLARGVHHIDYYKKTSNGRLpvKWMAPEALfD---RVYTHQSDVWSFGILLWEIFTlGGSPY--PGIP 542
Cdd:cd06624 142 nTYSGVVKISDFGTSKRLAGINPCTETFTGTL--QYMAPEVI-DkgqRGYGPPADIWSLGCTIIEMAT-GKPPFieLGEP 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   543 VEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06624 218 QAAMFKVGMFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQ 264
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
321-589 6.97e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 90.13  E-value: 6.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSrpdQTSIVAVKMLKDNASDKDLADLISEMEMMKLIGRhKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd06641  12 IGKGSFGEVF----KGIDNR---TQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDS-PYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRArrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd06641  84 LGGGSALDLLEP-----------------GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   481 LARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYPGI-PVEELFSLLReghrmERP 559
Cdd:cd06641 147 VAGQLTDTQIKRN*FVGT-PF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELhPMKVLFLIPK-----NNP 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 204138   560 P----NCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06641 219 PtlegNYSKPLKEFVEACLNKEPSFRPTAKELLK 252
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
358-587 8.32e-20

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 89.48  E-value: 8.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   358 SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQegPLYVIVEYAAKGNLREFLrarrppgpdlspdgprSSEgPLSFPAL 437
Cdd:cd14025  35 DDSERMELLEEAKKMEMA-KFRHILPVYGICSE--PVGLVMEYMETGSLEKLL----------------ASE-PLPWELR 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   438 VSCAYQVARGMQYLESRK--CIHRDLAARNVLVTEDDVMKIADFGLAR---GVHHIDYYKKTSNGRLpvKWMAPEALF-- 510
Cdd:cd14025  95 FRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDLSRDGLRGTI--AYLPPERFKek 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   511 DRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPvEELFSLLR--EGHRMERPPNC---PSE---LYGLMRECWHAAPSQRP 582
Cdd:cd14025 173 NRCPDTKHDVYSFAIVIWGILT-QKKPFAGEN-NILHIMVKvvKGHRPSLSPIPrqrPSEcqqMICLMKRCWDQDPRKRP 250

                ....*
gi 204138   583 TFKQL 587
Cdd:cd14025 251 TFQDI 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
317-555 8.38e-20

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 89.28  E-value: 8.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdSSRPDQTsiVAVKML-KDNASDKDLAD-LISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14162   4 VGKTLGHGSYAVVKKAY-----STKHKCK--VAIKIVsKKKAPEDYLQKfLPREIEVIKGL-KHPNLICFYEAIETTSRV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd14162  76 YIIMELAENGDLLDYIR----------------KNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHhidyykKTSNGRLPVK--------WMAPEALFDRVYTHQ-SDVWSFGILLweiFTL--GGSPYPGipv 543
Cdd:cd14162 140 KITDFGFARGVM------KTKDGKPKLSetycgsyaYASPEILRGIPYDPFlSDIWSMGVVL---YTMvyGRLPFDD--- 207
                       250
                ....*....|..
gi 204138   544 EELFSLLREGHR 555
Cdd:cd14162 208 SNLKVLLKQVQR 219
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
319-582 8.59e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 89.70  E-value: 8.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALgMDSSRPDQTSIVAVKMLKDNASDkdlaDLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd08228   8 KKIGRGQFSEVYRATCL-LDRKPVALKKVQIFEMMDAKARQ----DCVKEIDLLKQLN-HPNVIKYLDSFIEDNELNIVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLRE----FLRARRppgpdLSPDgprssegplsfPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd08228  82 ELADAGDLSQmikyFKKQKR-----LIPE-----------RTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGvhhidYYKKTSNGRLPVK---WMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVeELFSLLR 551
Cdd:cd08228 146 KLGDLGLGRF-----FSSKTTAAHSLVGtpyYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGDKM-NLFSLCQ 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 204138   552 EGHRMERPPnCPSELYG-----LMRECWHAAPSQRP 582
Cdd:cd08228 219 KIEQCDYPP-LPTEHYSeklreLVSMCIYPDPDQRP 253
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
319-589 9.20e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 89.10  E-value: 9.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEalgmdsSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd08218   6 KKIGEGSFGKALLVK------SKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKM-KHPNIVQYQESFEENGNLYIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRppGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd08218  79 DYCDGGDLYKRINAQR--GVLFPED------------QILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLReGHRMER 558
Cdd:cd08218 145 FGIARVLNSTVELARTCIGT-PY-YLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIR-GSYPPV 221
                       250       260       270
                ....*....|....*....|....*....|.
gi 204138   559 PPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd08218 222 PSRYSYDLRSLVSQLFKRNPRDRPSINSILE 252
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
317-587 1.10e-19

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 89.15  E-value: 1.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAealgmdsSRPDQTSIVAVKMLKDNASDKDLAD--LISEMEMMKLIgRHKNIINL---LGVCTqe 391
Cdd:cd14164   4 LGTTIGEGSFSKVKLA-------TSQKYCCKVAIKIVDRRRASPDFVQkfLPRELSILRRV-NHPNIVQMfecIEVAN-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLRARRPPGPDLSpdgprssegplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd14164  74 GRLYIVMEAAATDLLQKIQEVHHIPKDLAR-----------------DMFAQMVGAVNYLHDMNIVHRDLKCENILLSAD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 D-VMKIADFGLARGVHHIDYYKKTSNGRlpVKWMAPEALFDRVYTHQS-DVWSFGILLWEIFTlGGSPYPgipvEELFSL 549
Cdd:cd14164 137 DrKIKIADFGFARFVEDYPELSTTFCGS--RAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFD----ETNVRR 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   550 LReghRMERPPNCPSEL------YGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14164 210 LR---LQQRGVLYPSGValeepcRALIRTLLQFNPSTRPSIQQV 250
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
314-527 1.49e-19

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 88.95  E-value: 1.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEALgmdssRPDQTsiVAVKML-KDNASDKDLADLIS-----EMEMMKLIGRHKNIINLLGV 387
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDL-----RTGRK--YAIKCLyKSGPNSKDGNDFQKlpqlrEIDLHRRVSRHPNIITLHDV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd13993  74 FETEVAIYIVLEYCPNGDLFEAITENR--------------IYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENIL 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDD-VMKIADFGLARGvhhidyyKKTSN--GRLPVKWMAPEaLFDRV-------YTHQSDVWSFGILL 527
Cdd:cd13993 140 LSQDEgTVKLCDFGLATT-------EKISMdfGVGSEFYMAPE-CFDEVgrslkgyPCAAGDIWSLGIIL 201
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
319-537 1.56e-19

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 90.16  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqVVCAealGMDSSRPDQTSiVAVKMLKDNASDKDLAD-LISEMEMMKLIGRHKNIINLLGVctqegplyVI 397
Cdd:cd07857   6 KELGQGAYG-IVCS---ARNAETSEEET-VAIKKITNVFSKKILAKrALRELKLLRHFRGHKNITCLYDM--------DI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYaakGNLREFLRARRPPGPDLSPDgPRSSEgPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd07857  73 VFP---GNFNELYLYEELMEADLHQI-IRSGQ-PLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKIC 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVH--------HIDYYKKTsngrlpvKWM-APEALFD-RVYTHQSDVWSFGILLWEIftLGGSP 537
Cdd:cd07857 148 DFGLARGFSenpgenagFMTEYVAT-------RWYrAPEIMLSfQSYTKAIDVWSVGCILAEL--LGRKP 208
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
317-586 2.52e-19

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 88.08  E-value: 2.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEalgmdSSRPDQTsiVAVKMLKDNASDKD--LADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14081   5 LGKTLGKGQTGLVKLAK-----HCVTGQK--VAIKIVNKEKLSKEsvLMKVEREIAIMKLI-EHPNVLKLYDVYENKKYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARrppgpdlspdGPRSSEGPLSFpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd14081  77 YLVLEYVSGGELFDYLVKK----------GRLTEKEARKF------FRQIISALDYCHSHSICHRDLKPENLLLDEKNNI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARgVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQ-SDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREG 553
Cdd:cd14081 141 KIADFGMAS-LQPEGSLLETSCGSP--HYACPEVIKGEKYDGRkADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRG 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 204138   554 hRMERPPNCPSELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd14081 217 -VFHIPHFISPDAQDLLRRMLEVNPEKRITIEE 248
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
321-581 2.73e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 89.29  E-value: 2.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDE-------LYAVKILKKDVviQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05616  81 EYVNGGDLMYHIQ----------------QVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIAD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHIDYYKKTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREgHRMER 558
Cdd:cd05616 145 FGMCKENIWDGVTTKTFCGT-P-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSIME-HNVAY 220
                       250       260
                ....*....|....*....|...
gi 204138   559 PPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd05616 221 PKSMSKEAVAICKGLMTKHPGKR 243
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
319-532 3.03e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 89.12  E-value: 3.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqVVCAealGMDSSRPDQtsiVAVKMLKDNASDKDLADLI-SEMEMMKLIgRHKNIINLLGVCTQEGP---- 393
Cdd:cd07834   6 KPIGSGAYG-VVCS---AYDKRTGRK---VAIKKISNVFDDLIDAKRIlREIKILRHL-KHENIIGLLDILRPPSPeefn 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 -LYVIVEYAAKgNLREFLRARRPpgpdLSPDGPRssegplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd07834  78 dVYIVTELMET-DLHKVIKSPQP----LTDDHIQ------------YFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   473 VMKIADFGLARGVHHID------------YYKktsngrlpvkwmAPEAL--FDRvYTHQSDVWSFGILLWEIFT 532
Cdd:cd07834 141 DLKICDFGLARGVDPDEdkgflteyvvtrWYR------------APELLlsSKK-YTKAIDIWSVGCIFAELLT 201
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
316-551 3.30e-19

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 88.15  E-value: 3.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKpLGEGCFGQVVCAEalgmDSSRPDqtsIVAVK-MLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPL 394
Cdd:cd07832   4 ILGR-IGEGAHGIVFKAK----DRETGE---TVALKkVALRKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAakgnlreflrarrppGPDLSpDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd07832  76 VLVFEYM---------------LSSLS-EVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARgVHHIDYYKKTSNgRLPVKW-MAPEALF-DRVYTHQSDVWSFGILLWEIftLGGSP-YPG-IPVEELFSLL 550
Cdd:cd07832 140 KIADFGLAR-LFSEEDPRLYSH-QVATRWyRAPELLYgSRKYDEGVDLWAVGCIFAEL--LNGSPlFPGeNDIEQLAIVL 215

                .
gi 204138   551 R 551
Cdd:cd07832 216 R 216
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
312-589 3.35e-19

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 88.22  E-value: 3.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVvcaeALGMDSSRPDQtsiVAVKMLKDN-------ASDKDLADLISEMEMMKLIgRHKNIINL 384
Cdd:cd14084   5 RKKYIMSRTLGSGACGEV----KLAYDKSTCKK---VAIKIINKRkftigsrREINKPRNIETEIEILKKL-SHPCIIKI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   385 LGVCTQEGPLYVIVEYAAKGNLreFLRARrppgpdlSPDGPRSSEGPLSFpalvscaYQVARGMQYLESRKCIHRDLAAR 464
Cdd:cd14084  77 EDFFDAEDDYYIVLELMEGGEL--FDRVV-------SNKRLKEAICKLYF-------YQMLLAVKYLHSNGIIHRDLKPE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDD---VMKIADFGLARGVHHiDYYKKTSNGrlPVKWMAPEAL--FDRV-YTHQSDVWSFGILLWeiFTLGGSP- 537
Cdd:cd14084 141 NVLLSSQEeecLIKITDFGLSKILGE-TSLMKTLCG--TPTYLAPEVLrsFGTEgYTRAVDCWSLGVILF--ICLSGYPp 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   538 ----YPGIPVEE--LFSLLREGHRMERppNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14084 216 fseeYTQMSLKEqiLSGKYTFIPKAWK--NVSEEAKDLVKKMLVVDPSRRPSIEEALE 271
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
314-583 3.83e-19

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 87.44  E-value: 3.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVvcaeALGMDSSRPDQtsiVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQE 391
Cdd:cd14073   2 RYELLETLGKGTYGKV----KLAIERATGRE---VAIKSIKKDKieDEQDMVRIRREIEIMSSL-NHPHIIRIYEVFENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLRARRppgpDLSPDGPRSsegplSFPALVSCAYqvargmqYLESRKCIHRDLAARNVLVTED 471
Cdd:cd14073  74 DKIVIVMEYASGGELYDYISERR----RLPEREARR-----IFRQIVSAVH-------YCHKNGVVHRDLKLENILLDQN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLArGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTH-QSDVWSFGILLWeIFTLGGSPYPGIPVEELFSLL 550
Cdd:cd14073 138 GNAKIADFGLS-NLYSKDKLLQTFCGS-PL-YASPEIVNGTPYQGpEVDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQI 213
                       250       260       270
                ....*....|....*....|....*....|...
gi 204138   551 REGHRMErpPNCPSELYGLMRECWHAAPSQRPT 583
Cdd:cd14073 214 SSGDYRE--PTQPSDASGLIRWMLTVNPKRRAT 244
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
307-540 4.62e-19

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 88.89  E-value: 4.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   307 LWEFPrDRLVLGKPLGEGCFGQVVCAEALGMDS-------SRPDQTSIVAVKMLKdnasdkdladlisEMEMMKLIgRHK 379
Cdd:cd07851  10 VWEVP-DRYQNLSPVGSGAYGQVCSAFDTKTGRkvaikklSRPFQSAIHAKRTYR-------------ELRLLKHM-KHE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   380 NIINLLGVCTQEGPL------YVIVEYAAKgNLREFLRARRppgpdLSPDGPRssegplsFpaLVscaYQVARGMQYLES 453
Cdd:cd07851  75 NVIGLLDVFTPASSLedfqdvYLVTHLMGA-DLNNIVKCQK-----LSDDHIQ-------F--LV---YQILRGLKYIHS 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   454 RKCIHRDLAARNVLVTEDDVMKIADFGLARgvhHIDyykKTSNGRLPVKW-MAPEALFDRV-YTHQSDVWSFGILLWEIF 531
Cdd:cd07851 137 AGIIHRDLKPSNLAVNEDCELKILDFGLAR---HTD---DEMTGYVATRWyRAPEIMLNWMhYNQTVDIWSVGCIMAELL 210
                       250
                ....*....|
gi 204138   532 TlgGSP-YPG 540
Cdd:cd07851 211 T--GKTlFPG 218
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
348-587 4.70e-19

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 87.06  E-value: 4.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLrarrppgpdlspdgpr 426
Cdd:cd14071  28 VAIKIIdKSQLDEENLKKIYREVQIMKML-NHPHIIKLYQVMETKDMLYLVTEYASNGEIFDYL---------------- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   427 SSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLArgvhhiDYYK-----KTSNGRLPv 501
Cdd:cd14071  91 AQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS------NFFKpgellKTWCGSPP- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   502 kWMAPEALFDRVYTH-QSDVWSFGILLWeIFTLGGSPYPGIPVEELFSLLREGhRMERPPNCPSELYGLMRECWHAAPSQ 580
Cdd:cd14071 164 -YAAPEVFEGKEYEGpQLDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVLSG-RFRIPFFMSTDCEHLIRRMLVLDPSK 240

                ....*..
gi 204138   581 RPTFKQL 587
Cdd:cd14071 241 RLTIEQI 247
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
354-587 4.95e-19

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 87.03  E-value: 4.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   354 KDNASDKDLADLISEME-MMKLigRHKNIINLLGVCTQEGP------LYVIVEYAAKGNLREFLrarrppgpdlspdgpr 426
Cdd:cd14012  34 KTSNGKKQIQLLEKELEsLKKL--RHPNLVSYLAFSIERRGrsdgwkVYLLTEYAPGGSLSELL---------------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   427 SSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV---TEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVKW 503
Cdd:cd14012  96 DSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSLDEFK-QTYW 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   504 MAPE-ALFDRVYTHQSDVWSFGILLWEIFTlggspypGIPVEELFSLLREGHrmeRPPNCPSELYGLMRECWHAAPSQRP 582
Cdd:cd14012 175 LPPElAQGSKSPTRKTDVWDLGLLFLQMLF-------GLDVLEKYTSPNPVL---VSLDLSASLQDFLSKCLSLDPKKRP 244

                ....*
gi 204138   583 TFKQL 587
Cdd:cd14012 245 TALEL 249
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
317-589 4.96e-19

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 87.19  E-value: 4.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEAL--GMDssrpdqtsiVAVKML-KDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGP 393
Cdd:cd14072   4 LLKTIGKGNFAKVKLARHVltGRE---------VAIKIIdKTQLNPSSLQKLFREVRIMKILN-HPNIVKLFEVIETEKT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARrppgpdlspDGPRSSEGPLSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14072  74 LYLVMEYASGGEVFDYLVAH---------GRMKEKEARAKFRQIVS-------AVQYCHQKRIVHRDLKAENLLLDADMN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARgvhhidyyKKTSNGRLPV-----KWMAPEALFDRVYTH-QSDVWSFGILLWEIFTlGGSPYPGIPVEELF 547
Cdd:cd14072 138 IKIADFGFSN--------EFTPGNKLDTfcgspPYAAPELFQGKKYDGpEVDVWSLGVILYTLVS-GSLPFDGQNLKELR 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   548 S-LLREGHRMerPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14072 209 ErVLRGKYRI--PFYMSTDCENLLKKFLVLNPSKRGTLEQIMK 249
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
317-589 6.31e-19

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 86.69  E-value: 6.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALGMDSSrpdqtsiVAVKML-KDNASDKDLADLIS-EMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14663   4 LGRTLGEGTFAKVKFARNTKTGES-------VAIKIIdKEQVAREGMVEQIKrEIAIMKLL-RHPNIVELHEVMATKTKI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRArrppGPDLSPDGPRSsegplSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd14663  76 FFVMELVTGGELFSKIAK----NGRLKEDKARK-----YFQQLID-------AVDYCHSRGVFHRDLKPENLLLDEDGNL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHHIDyykktSNGRLPVK-----WMAPEALFDRVYT-HQSDVWSFGILLWEIFTlGGSPYPGIPVEELFS 548
Cdd:cd14663 140 KISDFGLSALSEQFR-----QDGLLHTTcgtpnYVAPEVLARRGYDgAKADIWSCGVILFVLLA-GYLPFDDENLMALYR 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   549 LLREGhRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14663 214 KIMKG-EFEYPRWFSPGAKSLIKRILDPNPSTRITVEQIMA 253
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
317-589 6.36e-19

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 86.62  E-value: 6.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVvcaeALGMDSSRPDQtsiVAVKML-KDNASDKD---LADLISEMEMMkligRHKNIINLLGVCTQEG 392
Cdd:cd14075   6 IRGELGSGNFSQV----KLGIHQLTKEK---VAIKILdKTKLDQKTqrlLSREISSMEKL----HHPNIIRLYEVVETLS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14075  75 KLHLVMEYASGGELYTKI----------------STEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARgvhHIDYYKK--TSNGRLPvkWMAPEaLF--DRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFS 548
Cdd:cd14075 139 CVKVGDFGFST---HAKRGETlnTFCGSPP--YAAPE-LFkdEHYIGIYVDIWALGVLLYFMVT-GVMPFRAETVAKLKK 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   549 LLREGHrMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14075 212 CILEGT-YTIPSYVSEPCQELIRGILQPVPSDRYSIDEIKN 251
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
316-589 7.58e-19

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 86.76  E-value: 7.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVCA--EALGMDssrpdqtsiVAVKML-KDNASDKDLAD-LISEMEMMKLIgRHKNIINLLGVC-TQ 390
Cdd:cd14165   4 ILGINLGEGSYAKVKSAysERLKCN---------VAIKIIdKKKAPDDFVEKfLPRELEILARL-NHKSIIKTYEIFeTS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRPPGPDLSpdgprssegplsfpalvSCAY-QVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd14165  74 DGKVYIVMELGVQGDLLEFIKLRGALPEDVA-----------------RKMFhQLSSAIKYCHELDIVHRDLKCENLLLD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVhhidyyKKTSNGRLPVK--------WMAPEALFDRVYTHQ-SDVWSFGILLWeIFTLGGSPYPG 540
Cdd:cd14165 137 KDFNIKLTDFGFSKRC------LRDENGRIVLSktfcgsaaYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMPYDD 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   541 IPVEELFSLLREgHRMERPPNC--PSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14165 210 SNVKKMLKIQKE-HRVRFPRSKnlTSECKDLIYRLLQPDVSQRLCIDEVLS 259
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
312-588 1.05e-18

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 86.53  E-value: 1.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQvvCAEALGMDSSRPDQTSIVAVKML-KDNASDKdladliseMEMMKLIGR---HKNIINLLGV 387
Cdd:cd14187   6 RRRYVRGRFLGKGGFAK--CYEITDADTKEVFAGKIVPKSLLlKPHQKEK--------MSMEIAIHRslaHQHVVGFHGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd14187  76 FEDNDFVYVVLELCRRRSLLELHKRRKA----------------LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLF 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELF 547
Cdd:cd14187 140 LNDDMEVKIGDFGLATKVEYDGERKKTLCG--TPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPPFETSCLKETY 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   548 SLLREgHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd14187 217 LRIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 256
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
321-588 1.09e-18

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 85.90  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdsSRPDqTSIVAVKMLKDN-ASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd13997   8 IGSGSFSEVFKVR------SKVD-GCLYAVKKSKKPfRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRArrppgpdLSPDGPRSSEGPLSFpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd13997  81 LCENGSLQDALEE-------LSPISKLSEAEVWDL------LLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLARgvhhidyykktsngRLPVKW---------MAPEALFD-RVYTHQSDVWSFGILLWEIFTlgGSPYP--GipveELF 547
Cdd:cd13997 148 GLAT--------------RLETSGdveegdsryLAPELLNEnYTHLPKADIFSLGVTVYEAAT--GEPLPrnG----QQW 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 204138   548 SLLREGhRMERPPNCP--SELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd13997 208 QQLRQG-KLPLPPGLVlsQELTRLLKVMLDPDPTRRPTADQLL 249
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
318-537 1.22e-18

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 86.50  E-value: 1.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVcaEALGMDSSRPdqtsiVAVKMLkdnasDKDLadLISEME----------MMKLigRHKNIINLLGV 387
Cdd:cd05581   6 GKPLGEGSYSTVV--LAKEKETGKE-----YAIKVL-----DKRH--IIKEKKvkyvtiekevLSRL--AHPGIVKLYYT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd05581  70 FQDESKLYFVLEYAPNGDLLEYIRKY----------------GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENIL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLAR-----GVHHIDYYKKTSNGRLPVK----------WMAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd05581 134 LDEDMHIKITDFGTAKvlgpdSSPESTKGDADSQIAYNQAraasfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLT 213

                ....*
gi 204138   533 lgGSP 537
Cdd:cd05581 214 --GKP 216
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
321-547 1.24e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 87.36  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdssrpdQTSIVAVKMLK--DNASDKDLADLISEMEMMKLIG--RHKNIINLLGvCTQEgPLYV 396
Cdd:cd05589   7 LGRGHFGKVLLAEYKP-------TGELFAIKALKkgDIIARDEVESLMCEKRIFETVNsaRHPFLVNLFA-CFQT-PEHV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 --IVEYAAKGNLREFLRArrppgpDLSPDgPRSSegplsFPAlvSCayqVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd05589  78 cfVMEYAAGGDLMMHIHE------DVFSE-PRAV-----FYA--AC---VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYV 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   475 KIADFGLAR-GVHHIDyykKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELF 547
Cdd:cd05589 141 KIADFGLCKeGMGFGD---RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPGDDEEEVF 210
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
359-594 1.30e-18

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 86.01  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   359 DKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGplyviveYAAKGNLREFLRARRppgpdLSPDGPRSSEGPLSFPALV 438
Cdd:cd13975  38 DKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYS-------YGGGSSIAVLLIMER-----LHRDLYTGIKAGLSLEERL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   439 SCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGvhhidyyKKTSNGRL---PVKwMAPEaLFDRVYT 515
Cdd:cd13975 106 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFSGKYD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   516 HQSDVWSFGILLWEIFTlGGSPYPGI-----PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEA 590
Cdd:cd13975 177 NSVDVYAFGILFWYLCA-GHVKLPEAfeqcaSKDHLWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPK 255

                ....
gi 204138   591 LDKV 594
Cdd:cd13975 256 LQGI 259
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
321-615 1.37e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 86.40  E-value: 1.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdssRPDQT-SIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd07860   8 IGEGTYGVVYKA--------RNKLTgEVVALKKIRlDTETEGVPSTAIREISLLKEL-NHPNIVKLLDVIHTENKLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKgNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd07860  79 EFLHQ-DLKKFMDASALTG--------------IPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLAD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLAR--GVHHIDYYKKTsngrLPVKWMAPEALFD-RVYTHQSDVWSFGILLWEIFTLgGSPYPG-IPVEELFsllregh 554
Cdd:cd07860 144 FGLARafGVPVRTYTHEV----VTLWYRAPEILLGcKYYSTAVDIWSLGCIFAEMVTR-RALFPGdSEIDQLF------- 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138   555 RMERPPNCPSElyglmrECWHAA---PSQRPTF-KQLVEALDKVLLAVSEEYLDLRLTFGPYSPN 615
Cdd:cd07860 212 RIFRTLGTPDE------VVWPGVtsmPDYKPSFpKWARQDFSKVVPPLDEDGRDLLSQMLHYDPN 270
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
321-591 1.39e-18

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 86.19  E-value: 1.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdsSRPDQTSiVAVKMLKDNASDKDLADLISEMEMM-KLigRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd13996  14 LGSGGFGSVYKVR------NKVDGVT-YAIKKIRLTEKSSASEKVLREVKALaKL--NHPNIVRYYTAWVEEPPLYIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARrppgpDLSPDGPRSSEgplsfpalVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD-VMKIAD 478
Cdd:cd13996  85 LCEGGTLRDWIDRR-----NSSSKNDRKLA--------LELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDlQVKIGD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLAR---GVHHIDYYKKTSNGR----LPVK-----WMAPEALFDRVYTHQSDVWSFGILLWEIFtlggspYPGIPVEEL 546
Cdd:cd13996 152 FGLATsigNQKRELNNLNNNNNGntsnNSVGigtplYASPEQLDGENYNEKADIYSLGIILFEML------HPFKTAMER 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   547 FSLLREGHRMERPPNCPSELY---GLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd13996 226 STILTDLRNGILPESFKAKHPkeaDLIQSLLSKNPEERPSAEQLLRSL 273
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
347-574 1.46e-18

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 86.61  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   347 IVAVKMLkdNASDKdlADLISEMEMMKLIG-RHKNIINLLGVCTQEGPLYV----IVEYAAKGNLREFLRARRppgpdls 421
Cdd:cd14053  20 LVAVKIF--PLQEK--QSWLTEREIYSLPGmKHENILQFIGAEKHGESLEAeywlITEFHERGSLCDYLKGNV------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   422 pdgprssegpLSFPALVSCAYQVARGMQYL---------ESRKCI-HRDLAARNVLVTEDDVMKIADFGLARgvhHIDYY 491
Cdd:cd14053  89 ----------ISWNELCKIAESMARGLAYLhedipatngGHKPSIaHRDFKSKNVLLKSDLTACIADFGLAL---KFEPG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   492 KKTSNGRLPV---KWMAPEAL-----FDRVYTHQSDVWSFGILLWEI---FTLGGSPYPG--IPVE-ELFS-----LLRE 552
Cdd:cd14053 156 KSCGDTHGQVgtrRYMAPEVLegainFTRDAFLRIDMYAMGLVLWELlsrCSVHDGPVDEyqLPFEeEVGQhptleDMQE 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 204138   553 --GHRMERPPNCPS--------ELYGLMRECW 574
Cdd:cd14053 236 cvVHKKLRPQIRDEwrkhpglaQLCETIEECW 267
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
319-583 1.90e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 85.41  E-value: 1.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQvvcaeALGMDSSRPDQTSIVAVKMLKDNASD----KDLADLISEMemmkligRHKNIINLLGVCTQEGPL 394
Cdd:cd08219   6 RVVGEGSFGR-----ALLVQHVNSDQKYAMKEIRLPKSSSAvedsRKEAVLLAKM-------KHPNIVAFKESFEADGHL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAY-QVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd08219  74 YIVMEYCDGGDLMQKIKLQR---------------GKLFPEDTILQWFvQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFSLLREG 553
Cdd:cd08219 139 VKLGDFGSARLLTSPGAYACTYVGT-PY-YVPPEIWENMPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQG 215
                       250       260       270
                ....*....|....*....|....*....|
gi 204138   554 HRMERPPNCPSELYGLMRECWHAAPSQRPT 583
Cdd:cd08219 216 SYKPLPSHYSYELRSLIKQMFKRNPRSRPS 245
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
317-540 2.70e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 86.35  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    317 LGKPLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLAD-------------LISEMEMMKLIgRHKNIIN 383
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGK-------IVAIKKVKIIEISNDVTKdrqlvgmcgihftTLRELKIMNEI-KHENIMG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    384 LLGVCTQEGPLYVIVEYAAkGNLREFLRARrppgpdlspdgPRSSEgplsfpALVSC-AYQVARGMQYLESRKCIHRDLA 462
Cdd:PTZ00024  85 LVDVYVEGDFINLVMDIMA-SDLKKVVDRK-----------IRLTE------SQVKCiLLQILNGLNVLHKWYFMHRDLS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    463 ARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVK-----------WM-APEALF-DRVYTHQSDVWSFGILLWE 529
Cdd:PTZ00024 147 PANIFINSKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYrAPELLMgAEKYHFAVDMWSVGCIFAE 226
                        250
                 ....*....|..
gi 204138    530 IftLGGSP-YPG 540
Cdd:PTZ00024 227 L--LTGKPlFPG 236
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
292-589 3.09e-18

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 85.43  E-value: 3.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   292 PLLTGLVSLDLPLDPlWEfprdrlvLGKPLGEGCFGQVvcaealgMDSSRPDQTSIVAVKMLkDNASDKDlADLISEMEM 371
Cdd:cd06639   9 SSMLGLESLADPSDT-WD-------IIETIGKGTYGKV-------YKVTNKKDGSLAAVKIL-DPISDVD-EEIEAEYNI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   372 MKLIGRHKNIINLLGVCTQE-----GPLYVIVEYAAKGNLREFLRArrppgpdLSPDGPRSSEGPLSFpalvsCAYQVAR 446
Cdd:cd06639  72 LRSLPNHPNVVKFYGMFYKAdqyvgGQLWLVLELCNGGSVTELVKG-------LLKCGQRLDEAMISY-----ILYGALL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   447 GMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEAL-----FDRVYTHQSDVW 521
Cdd:cd06639 140 GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRRNTSVGT-PF-WMAPEVIaceqqYDYSYDARCDVW 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   522 SFGILLWEIFTlGGSPYPGI-PVEELFSLLRE-GHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06639 218 SLGITAIELAD-GDPPLFDMhPVKALFKIPRNpPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLE 286
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
314-608 3.21e-18

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 85.17  E-value: 3.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAealgmdSSRPDQTSIVAVKMLKDNASD-KDLADLISEMEMMKLIGR--HKNIINLLGVCTQ 390
Cdd:cd14052   1 RFANVELIGSGEFSQVYKV------SERVPTGKVYAVKKLKPNYAGaKDRLRRLEEVSILRELTLdgHDNIVQLIDSWEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd14052  75 HGHLYIQTELCENGSLDVFLSEL-------------GLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARgvhhidyykktsngRLPV----------KWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPG 540
Cdd:cd14052 142 EGTLKIGDFGMAT--------------VWPLirgieregdrEYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNG 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   541 IPVEElfslLREGHRMERPPNCPSELYGLMRECWHAAPSQrPTFKQLVEALDKVLLAVSEEYLDLRLT 608
Cdd:cd14052 208 DAWQK----LRSGDLSDAPRLSSTDLHSASSPSSNPPPDP-PNMPILSGSLDRVVRWMLSPEPDRRPT 270
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
319-547 3.74e-18

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 85.90  E-value: 3.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEAlgmdssrPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05592   1 KVLGKGSFGKVMLAEL-------KGTNQYFAIKALKKDVvlEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRarrppgpdlspDGPRSSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05592  74 VMEYLNGGDLMFHIQ-----------QSGRFDEDRARF-----YGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKI 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   477 ADFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELF 547
Cdd:cd05592 138 ADFGMCK--ENIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPFHGEDEDELF 205
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
316-588 4.08e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 84.41  E-value: 4.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVcaealgMDSSRPDQTSIVAVKMLKDNASDKDL------ADLISEMemmkligRHKNIINLL-GVC 388
Cdd:cd08223   3 QFLRVIGKGSYGEVW------LVRHKRDRKQYVIKKLNLKNASKRERkaaeqeAKLLSKL-------KHPNIVSYKeSFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   389 TQEGPLYVIVEYAAKGNLREFLRARRPPgpdlspdgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd08223  70 GEDGFLYIVMGFCEGGDLYTRLKEQKGV--------------LLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSpYPGIPVEELFS 548
Cdd:cd08223 136 TKSNIIKVGDLGIARVLESSSDMATTLIGT-PY-YMSPELFSNKPYNHKSDVWALGCCVYEMATLKHA-FNAKDMNSLVY 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   549 LLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd08223 213 KILEGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRIL 252
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
308-572 4.45e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 84.68  E-value: 4.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLVlgkplGEGCFGQVVCAEalgmdsSRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd14202   2 FEFSRKDLI-----GHGAFAVVFKGR------HKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKEL-KHENIVALYDF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLRARRPpgpdLSPDGPRssegplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd14202  70 QEIANSVYLVMEYCNGGDLADYLHTMRT----LSEDTIR------------LFLQQIAGAMKMLHSKGIIHRDLKPQNIL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VT---------EDDVMKIADFGLARGVHHiDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd14202 134 LSysggrksnpNNIRIKIADFGFARYLQN-NMMAATLCGS-PM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPF 209
                       250       260       270
                ....*....|....*....|....*....|....
gi 204138   539 PGIPVEELfSLLREGHRmERPPNCPSELYGLMRE 572
Cdd:cd14202 210 QASSPQDL-RLFYEKNK-SLSPNIPRETSSHLRQ 241
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
311-589 4.50e-18

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 85.06  E-value: 4.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVvcaealgMDSSRPDQTSIVAVKMLkDNASDKDlADLISEMEMMKLIGRHKNIINLLGVCTQ 390
Cdd:cd06638  16 PSDTWEIIETIGKGTYGKV-------FKVLNKKNGSKAAVKIL-DPIHDID-EEIEAEYNILKALSDHPNVVKFYGMYYK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EG-----PLYVIVEYAAKGNLREFLRArrppgpdLSPDGPRSSEgplsfPALVSCAYQVARGMQYLESRKCIHRDLAARN 465
Cdd:cd06638  87 KDvkngdQLWLVLELCNGGSVTDLVKG-------FLKRGERMEE-----PIIAYILHEALMGLQHLHVNKTIHRDVKGNN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEAL-----FDRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd06638 155 ILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGT-PF-WMAPEVIaceqqLDSTYDARCDVWSLGITAIELGD-GDPPLAD 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   541 I-PVEELFSLLRE-GHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06638 232 LhPMRALFKIPRNpPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQ 282
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
321-581 4.61e-18

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 84.11  E-value: 4.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALgmDSSRpdqtsIVAVKML-KDNASDKDLAD-LISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05123   1 LGKGSFGKVLLVRKK--DTGK-----LYAMKVLrKKEIIKRKEVEhTLNERNILERV-NHPFIVKLHYAFQTEEKLYLVL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05123  73 DYVPGGELFSHLSKEG-----------RFPEERARF-----YAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHHIDYYKKTSNGRLPvkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELF-SLLREGHRMe 557
Cdd:cd05123 137 FGLAKELSSDGDRTYTFCGTPE--YLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYeKILKSPLKF- 212
                       250       260
                ....*....|....*....|....
gi 204138   558 rPPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd05123 213 -PEYVSPEAKSLISGLLQKDPTKR 235
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
318-587 5.32e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 84.40  E-value: 5.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQvvCAEAlgmdssRPDQT-SIVAVKMLK---DNASDKD--LADLISEMEMMKLIgRHKNIINLLGVCTQE 391
Cdd:cd06630   5 GPLLGTGAFSS--CYQA------RDVKTgTLMAVKQVSfcrNSSSEQEevVEAIREEIRMMARL-NHPNIVRMLGATQHK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV-TE 470
Cdd:cd06630  76 SHFNIFVEWMAGGSVASLL----------------SKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVdST 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHidyyKKTSNGRL------PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVE 544
Cdd:cd06630 140 GQRLRIADFGAAARLAS----KGTGAGEFqgqllgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPWNAEKIS 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   545 ELFSLLREGHRMERPPNCPSELYGLMRE----CWHAAPSQRPTFKQL 587
Cdd:cd06630 215 NHLALIFKIASATTPPPIPEHLSPGLRDvtlrCLELQPEDRPPAREL 261
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
321-549 6.72e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 84.66  E-value: 6.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVvcaealgMDSSRPDQTSIVAVKMLKDNASDKDLADL-ISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd07848   9 VGEGAYGVV-------LKCRHKETKEIVAIKKFKDSEENEEVKETtLRELKMLRTL-KQENIVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKgNLREFLRaRRPPGpdLSPDGPRSSegplsfpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd07848  81 YVEK-NMLELLE-EMPNG--VPPEKVRSY------------IYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDF 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   480 GLARGVHHIDYYKKTSngRLPVKWM-APEALFDRVYTHQSDVWSFGILLWEIFTlgGSP-YPG-IPVEELFSL 549
Cdd:cd07848 145 GFARNLSEGSNANYTE--YVATRWYrSPELLLGAPYGKAVDMWSVGCILGELSD--GQPlFPGeSEIDQLFTI 213
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
307-551 7.41e-18

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 85.48  E-value: 7.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   307 LWEFPrDRLVLGKPLGEGCFGQVVCAealgMDS-----------SRPDQTSIVAVKMLKdnasdkdladlisEMEMMKLI 375
Cdd:cd07877  12 IWEVP-ERYQNLSPVGSGAYGSVCAA----FDTktglrvavkklSRPFQSIIHAKRTYR-------------ELRLLKHM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   376 gRHKNIINLLGVCTQEGPL-----YVIVEYAAKGNLREFLRARRppgpdLSPDGprssegpLSFpalvsCAYQVARGMQY 450
Cdd:cd07877  74 -KHENVIGLLDVFTPARSLeefndVYLVTHLMGADLNNIVKCQK-----LTDDH-------VQF-----LIYQILRGLKY 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   451 LESRKCIHRDLAARNVLVTEDDVMKIADFGLARgvhHIDyykKTSNGRLPVKWM-APEALFDRVYTHQS-DVWSFGILLW 528
Cdd:cd07877 136 IHSADIIHRDLKPSNLAVNEDCELKILDFGLAR---HTD---DEMTGYVATRWYrAPEIMLNWMHYNQTvDIWSVGCIMA 209
                       250       260
                ....*....|....*....|....
gi 204138   529 EIFTlGGSPYPGIP-VEELFSLLR 551
Cdd:cd07877 210 ELLT-GRTLFPGTDhIDQLKLILR 232
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
317-537 7.85e-18

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 84.17  E-value: 7.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDN--ASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd05580   5 FLKTLGTGSFGRVRLVKHK-------DSGKYYALKILKKAkiIKLKQVEHVLNEKRILSEV-RHPFIVNLLGSFQDDRNL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRppgpdlspdgprssegplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd05580  77 YMVMEYVPGGELFSLLRRSG------------------RFPNDVAKFYaaEVVLALEYLHSLDIVYRDLKPENLLLDSDG 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138   473 VMKIADFGLARgvhHIDYYKKTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEIftLGGSP 537
Cdd:cd05580 139 HIKITDFGFAK---RVKDRTYTLCGT-P-EYLAPEIILSKGHGKAVDWWALGILIYEM--LAGYP 196
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
314-589 8.26e-18

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 83.52  E-value: 8.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQvvCAEALGMDSSRPDQTSIVA-VKMLKDNASDKdladLISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd14188   2 RYCRGKVLGKGGFAK--CYEMTDLTTNKVYAAKIIPhSRVSKPHQREK----IDKEIELHRIL-HHKHVVQFYHYFEDKE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14188  75 NIYILLEYCSRRSMAHILKARKV----------------LTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENM 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELFSLLRE 552
Cdd:cd14188 139 ELKVGDFGLAARLEPLEHRRRTICG--TPNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLKETYRCIRE 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   553 GhRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14188 216 A-RYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEIIR 251
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
316-589 8.35e-18

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 83.65  E-value: 8.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVCAEALGmdssrpdQTSIVAVKML--KDNASDKDLADLISEMEMMK--------LIG---RHKNII 382
Cdd:cd14077   4 EFVKTIGAGSMGKVKLAKHIR-------TGEKCAIKIIprASNAGLKKEREKRLEKEISRdirtireaALSsllNHPHIC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   383 NLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLA 462
Cdd:cd14077  77 RLRDFLRTPNHYYMLFEYVDGGQLLDYIISH----------------GKLKEKQARKFARQIASALDYLHRNSIVHRDLK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   463 ARNVLVTEDDVMKIADFGLArGVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTH-QSDVWSFGILLWeIFTLGGSPYPGI 541
Cdd:cd14077 141 IENILISKSGNIKIIDFGLS-NLYDPRRLLRTFCGSL--YFAAPELLQAQPYTGpEVDVWSFGVVLY-VLVCGKVPFDDE 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   542 PVEELFSLLREGhRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14077 217 NMPALHAKIKKG-KVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLN 263
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
319-581 9.59e-18

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 84.37  E-value: 9.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALgmdsSRPDQTSIVAVKMLKdNASDKDLADLISEMEMMKLIG-RHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05582   1 KVLGQGSFGKVFLVRKI----TGPDAGTLYAMKVLK-KATLKVRDRVRTKMERDILADvNHPFIVKLHYAFQTEGKLYLI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLreFLRarrppgpdLSPDGPRSSEGPLSFPAlvscayQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05582  76 LDFLRGGDL--FTR--------LSKEVMFTEEDVKFYLA------ELALALDHLHSLGIIYRDLKPENILLDEDGHIKLT 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGhRME 557
Cdd:cd05582 140 DFGLSK--ESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMILKA-KLG 215
                       250       260
                ....*....|....*....|....
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd05582 216 MPQFLSPEAQSLLRALFKRNPANR 239
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
350-594 1.29e-17

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 83.40  E-value: 1.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   350 VKMLKDNASDKDLADLISEMEMMKLIG-RHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdLS-PDGPRs 427
Cdd:cd14044  33 VVILKDLKNNEGNFTEKQKIELNKLLQiDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDK------ISyPDGTF- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 segpLSFPALVSCAYQVARGMQYLESRKC-IHRDLAARNVLVTEDDVMKIADFGlargvhhidyykktSNGRLPVK---W 503
Cdd:cd14044 106 ----MDWEFKISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFG--------------CNSILPPSkdlW 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   504 MAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYpgipVEELFSLLREGHRMERPPNC----PS-----------ELYG 568
Cdd:cd14044 168 TAPEHLRQAGTSQKGDVYSYGIIAQEIILRKETFY----TAACSDRKEKIYRVQNPKGMkpfrPDlnlesagererEVYG 243
                       250       260
                ....*....|....*....|....*.
gi 204138   569 LMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14044 244 LVKNCWEEDPEKRPDFKKIENTLAKI 269
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
321-532 1.41e-17

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 83.13  E-value: 1.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmDSSRPDQTSIVAVKMLK---DNASDKDLAD-LISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd13994   1 IGKGATSVVRIV-----TKKNPRSGVLYAVKEYRrrdDESKRKDYVKrLTSEYIISSKL-HHPNIVKVLDLCQDLHGKWC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IV-EYAAKGNLREFLRARRPPGPDlspdgprssEGPLSFpalvscaYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd13994  75 LVmEYCPGGDLFTLIEKADSLSLE---------EKDCFF-------KQILRGVAYLHSHGIAHRDLKPENILLDEDGVLK 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   476 IADFGLARGVH-HIDYYKKTSN---GRLPvkWMAPEALFDRVYTHQS-DVWSFGILLWEIFT 532
Cdd:cd13994 139 LTDFGTAEVFGmPAEKESPMSAglcGSEP--YMAPEVFTSGSYDGRAvDVWSCGIVLFALFT 198
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
347-589 1.67e-17

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 83.36  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   347 IVAVKMLKDNASDKDLADLISEMEMMkligrHK----NIINLLGVCTQEGPLYVIVEYAAKGNLreflrarrppgpDLSP 422
Cdd:cd06622  28 TMAMKEIRLELDESKFNQIIMELDIL-----HKavspYIVDFYGAFFIEGAVYMCMEYMDAGSL------------DKLY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   423 DGPRSSEGpLSFPALVSCAYQVARGMQYL-ESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVhhIDYYKKTSNGrlPV 501
Cdd:cd06622  91 AGGVATEG-IPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNL--VASLAKTNIG--CQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   502 KWMAPE------ALFDRVYTHQSDVWSFGILLWEIfTLGGSPYPGIPVEELFSLLR---EGHrmerPPNCPSELYGLMRE 572
Cdd:cd06622 166 SYMAPEriksggPNQNPTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIFAQLSaivDGD----PPTLPSGYSDDAQD 240
                       250       260
                ....*....|....*....|.
gi 204138   573 ----CWHAAPSQRPTFKQLVE 589
Cdd:cd06622 241 fvakCLNKIPNRRPTYAQLLE 261
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
316-533 1.91e-17

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 83.09  E-value: 1.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKpLGEGCFGQVVCAEalgmdsSRPDQTSiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQE--GP 393
Cdd:cd07831   3 ILGK-IGEGTFSEVLKAQ------SRKTGKY-YAIKCMKKHFKSLEQVNNLREIQALRRLSPHPNILRLIEVLFDRktGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAaKGNLREFLRARRPPGPDLSpdgprssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVtEDDV 473
Cdd:cd07831  75 LALVFELM-DMNLYELIKGRKRPLPEKR---------------VKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDI 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   474 MKIADFGLARGVHhidyykktsnGRLP------VKWM-APEALF-DRVYTHQSDVWSFGILLWEIFTL 533
Cdd:cd07831 138 LKLADFGSCRGIY----------SKPPyteyisTRWYrAPECLLtDGYYGPKMDIWAVGCVFFEILSL 195
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
311-589 1.97e-17

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 82.49  E-value: 1.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGqVVCAeALGMDSSRpdqtsIVAVKMLkDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd06648   5 PRSDLDNFVKIGEGSTG-IVCI-ATDKSTGR-----QVAVKKM-DLRKQQRRELLFNEVVIMRDY-QHPNIVEMYSSYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06648  76 GDELWVVMEFLEGGALTDIVTHTR-----------------MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTS 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHiDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLL 550
Cdd:cd06648 139 DGRVKLSDFGFCAQVSK-EVPRRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYFNEPPLQAMKRI 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   551 R--EGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06648 216 RdnEPPKLKNLHKVSPRLRSFLDRMLVRDPAQRATAAELLN 256
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
348-583 1.99e-17

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 83.26  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLkdnaSDKDLADLISEMEMMKLIG-RHKNIINLLG----VCTQEGPLYVIVEYAAKGNLREFLRARrppgpdlsp 422
Cdd:cd13998  21 VAVKIF----SSRDKQSWFREKEIYRTPMlKHENILQFIAaderDTALRTELWLVTAFHPNGSL*DYLSLH--------- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   423 dgprssegPLSFPALVSCAYQVARGMQYLESRKCI---------HRDLAARNVLVTEDDVMKIADFGLA-RGVHHIDYYK 492
Cdd:cd13998  88 --------TIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIADFGLAvRLSPSTGEED 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   493 KTSNGRLPVK-WMAPEALFDRVYTH------QSDVWSFGILLWEIFT----LGGS------PY----PGIP-VEELFSL- 549
Cdd:cd13998 160 NANNGQVGTKrYMAPEVLEGAINLRdfesfkRVDIYAMGLVLWEMASrctdLFGIveeykpPFysevPNHPsFEDMQEVv 239
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   550 LREGHRMERPP---NCPS--ELYGLMRECWHAAPSQRPT 583
Cdd:cd13998 240 VRDKQRPNIPNrwlSHPGlqSLAETIEECWDHDAEARLT 278
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
321-589 2.13e-17

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 83.23  E-value: 2.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaealgmdSSRPDQTSIVAVKMLKDNASDKDlADLISEMEMMKLIGRHKNIINLLGVCTQEGP------L 394
Cdd:cd06637  14 VGNGTYGQVY--------KGRHVKTGQLAAIKVMDVTGDEE-EEIKQEINMLKKYSHHRNIATYYGAFIKKNPpgmddqL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRppgpdlspdGPRSSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd06637  85 WLVMEFCGAGSVTDLIKNTK---------GNTLKEEWIAY-----ICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGILLWEIfTLGGSPYPGI-PVEELFS 548
Cdd:cd06637 151 KLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDFKSDLWSLGITAIEM-AEGAPPLCDMhPMRALFL 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   549 LLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06637 228 IPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMK 268
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
317-594 2.37e-17

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 82.71  E-value: 2.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALGMdssrpdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd14152   4 LGELIGQGRWGKVHRGRWHGE----------VAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRarrppgpdlspdGPRSSegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMkI 476
Cdd:cd14152  74 ITSFCKGRTLYSFVR------------DPKTS---LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-I 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGL--ARGVHHIDyyKKTSNGRLPVKW---MAPEALFDRV---------YTHQSDVWSFGILLWEIfTLGGSPYPGIP 542
Cdd:cd14152 138 TDFGLfgISGVVQEG--RRENELKLPHDWlcyLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYEL-QARDWPLKNQP 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   543 VEELFSLLREGHRMERPPNCPS---ELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14152 215 AEALIWQIGSGEGMKQVLTTISlgkEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
321-589 2.56e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 82.09  E-value: 2.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd08221   8 LGRGAFGEAVLYR-------KTEDNSLVVWKEVNlSRLSEKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLReflrarrppgpdlspDGPRSSEGPLsFP--ALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd08221  80 YCNGGNLH---------------DKIAQQKNQL-FPeeVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARgVHHIDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVeELFSLLREGHRME 557
Cdd:cd08221 144 DFGISK-VLDSESSMAESIVGTPY-YMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPL-RLAVKIVQGEYED 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 204138   558 RPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd08221 221 IDEQYSEEIIQLVHDCLHQDPEDRPTAEELLE 252
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
321-589 3.42e-17

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 82.36  E-value: 3.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaealgmdSSRPDQT-SIVAVKMLkdNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGP------ 393
Cdd:cd06636  24 VGNGTYGQVY--------KGRHVKTgQLAAIKVM--DVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPpghddq 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd06636  94 LWLVMEFCGAGSVTDLVKNTK--GNALKED------------WIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGILLWEIfTLGGSPYPGI-PVEELF 547
Cdd:cd06636 160 VKLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPPLCDMhPMRALF 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   548 SLLReghrmERPPNCPS-----ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06636 237 LIPR-----NPPPKLKSkkwskKFIDFIEGCLVKNYLSRPSTEQLLK 278
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
319-582 4.22e-17

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 82.39  E-value: 4.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALgMDSSrpdqtsIVAVKMLK--DNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYV 396
Cdd:cd08229  30 KKIGRGQFSEVYRATCL-LDGV------PVALKKVQifDLMDAKARADCIKEIDLLKQLN-HPNVIKYYASFIEDNELNI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNL----REFLRARRppgpdLSPDgprssegplsfPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd08229 102 VLELADAGDLsrmiKHFKKQKR-----LIPE-----------KTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGvhhidYYKKTSNGRLPVK---WMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVeELFSL 549
Cdd:cd08229 166 VVKLGDLGLGRF-----FSSKTTAAHSLVGtpyYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGDKM-NLYSL 238
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   550 LREGHRMERPPnCPS-----ELYGLMRECWHAAPSQRP 582
Cdd:cd08229 239 CKKIEQCDYPP-LPSdhyseELRQLVNMCINPDPEKRP 275
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
321-540 4.39e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 82.14  E-value: 4.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaealgmdSSRPDQTS-IVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd07836   8 LGEGTYATVY--------KGRNRTTGeIVALKEIHLDAEEGTPSTAIREISLMKEL-KHENIVRLHDVIHTENKLMLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKgNLREFLRARRPPGPdLSPDGPRSsegplsFpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd07836  79 YMDK-DLKKYMDTHGVRGA-LDPNTVKS------F------TYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADF 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138   480 GLAR--GVHhidyYKKTSNGRLPVKWMAPEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPG 540
Cdd:cd07836 145 GLARafGIP----VNTFSNEVVTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMIT--GRPlFPG 203
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
319-559 6.47e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 81.91  E-value: 6.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGmdssrpdQTSIVAVKMLKDNAS--DKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05620   1 KVLGKGSFGKVLLAELKG-------KGEYFAVKALKKDVVliDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05620  74 VMEFLNGGDLMFHIQDK----------------GRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKI 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYKKTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELFsllrEGHRM 556
Cdd:cd05620 138 ADFGMCKENVFGDNRASTFCGT-P-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELF----ESIRV 210

                ...
gi 204138   557 ERP 559
Cdd:cd05620 211 DTP 213
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
321-540 6.61e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 82.03  E-value: 6.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssrpDQTS--IVAVKMLKDNaSDKDLADLISEMEMMKLIG-RHKNIINLLGVCT--QEGPLY 395
Cdd:cd07845  15 IGEGTYGIVYRAR---------DTTSgeIVALKKVRMD-NERDGIPISSLREITLLLNlRHPNIVELKEVVVgkHLDSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAK--GNLREFLRArrppgpdlspdgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd07845  85 LVMEYCEQdlASLLDNMPT------------------PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIDyykKTSNGRLPVKWM-APEALF-DRVYTHQSDVWSFGILLWEIftLGGSP-YPG 540
Cdd:cd07845 147 LKIADFGLARTYGLPA---KPMTPKVVTLWYrAPELLLgCTTYTTAIDMWAVGCILAEL--LAHKPlLPG 211
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
321-571 8.37e-17

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 80.49  E-value: 8.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSRPDQTsiVAVK-MLKDN-ASDKDLadLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14120   1 IGHGAFAVVF----KGRHRKKPDLP--VAIKcITKKNlSKSQNL--LGKEIKILKEL-SHENVVALLDCQETSSSVYLVM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRppgpDLSPDGPRSsegplsFpaLVscayQVARGMQYLESRKCIHRDLAARNVLVTEDD------ 472
Cdd:cd14120  72 EYCNGGDLADYLQAKG----TLSEDTIRV------F--LQ----QIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpsp 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 ---VMKIADFGLARGVHHiDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSL 549
Cdd:cd14120 136 ndiRLKIADFGFARFLQD-GMMAATLCGS-PM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAF 211
                       250       260       270
                ....*....|....*....|....*....|
gi 204138   550 LREGHRMErpPNCPSE--------LYGLMR 571
Cdd:cd14120 212 YEKNANLR--PNIPSGtspalkdlLLGLLK 239
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
317-589 9.30e-17

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 80.88  E-value: 9.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKpLGEGCFGQVV-CAEAlgmdssrpDQTSIVAVKMLKDNASD---KDLAdlISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd07847   6 LSK-IGEGSYGVVFkCRNR--------ETGQIVAIKKFVESEDDpviKKIA--LREIRMLKQL-KHPNLVNLIEVFRRKR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFlrARRPPG-PDLSpdgprssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd07847  74 KLHLVFEYCDHTVLNEL--EKNPRGvPEHL---------------IKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQ 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLAR-----GVHHIDYykktsngrLPVKWM-APEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPG--- 540
Cdd:cd07847 137 GQIKLCDFGFARiltgpGDDYTDY--------VATRWYrAPELLVgDTQYGPPVDVWAIGCVFAELLT--GQPlWPGksd 206
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   541 --------------IPV-EELFSL--------LREGHRME----RPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd07847 207 vdqlylirktlgdlIPRhQQIFSTnqffkglsIPEPETREplesKFPNISSPALSFLKGCLQMDPTERLSCEELLE 282
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
339-594 1.18e-16

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 80.91  E-value: 1.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   339 SSRPDQT-SIVAVKMLKDNASDKDLAD----LISEMEMMKLIgRHKNIINLLGVCTQE-GPLYVIVEYAAKgNLREFLRA 412
Cdd:cd14001  21 SPRGGSSrSPWAVKKINSKCDKGQRSLyqerLKEEAKILKSL-NHPNIVGFRAFTKSEdGSLCLAMEYGGK-SLNDLIEE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   413 RRPPGpdlspdgprssEGPlsFPA--LVSCAYQVARGMQYLESRKCI-HRDLAARNVLVTED-DVMKIADFGLArgvhhi 488
Cdd:cd14001  99 RYEAG-----------LGP--FPAatILKVALSIARALEYLHNEKKIlHGDIKSGNVLIKGDfESVKLCDFGVS------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   489 dyYKKTSNGRLPVK----------WMAPEALF-DRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFSLLREGHRME 557
Cdd:cd14001 160 --LPLTENLEVDSDpkaqyvgtepWKAKEALEeGGVITDKADIFAYGLVLWEMMTL-SVPHLNLLDIEDDDEDESFDEDE 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   558 --------RPPNCPSELYGLMRE-----------CWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14001 237 edeeayygTLGTRPALNLGELDDsyqkvielfyaCTQEDPKDRPSAAHIVEALEAH 292
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
321-588 1.18e-16

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 80.62  E-value: 1.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV--VCAEAlgmdssrpDQTSIVAVKML---------KDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCT 389
Cdd:cd08528   8 LGSGAFGCVykVRKKS--------NGQTLLALKEInmtnpafgrTEQERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCI-HRDLAARNVLV 468
Cdd:cd08528  80 ENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTED------------RIWNIFVQMVLALRYLHKEKQIvHRDLKPNNIML 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARGVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGgspyPGIPVEELFS 548
Cdd:cd08528 148 GEDDKVTITDFGLAKQKGPESSKMTSVVGTI--LYSCPEIVQNEPYGEKADIWALGCILYQMCTLQ----PPFYSTNMLT 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   549 LLREGHRMERPPnCPSELY-----GLMRECWHAAPSQRPTFKQLV 588
Cdd:cd08528 222 LATKIVEAEYEP-LPEGMYsdditFVIRSCLTPDPEARPDIVEVS 265
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
321-532 1.24e-16

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 80.06  E-value: 1.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdsSRPDQTSiVAVKMLKDNASDkdLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV-E 399
Cdd:cd13987   1 LGEGTYGKVLLAV------HKGSGTK-MALKFVPKPSTK--LKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAqE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD--VMKIA 477
Cdd:cd13987  72 YAPYGDLFSIIPPQVG----------------LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLC 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   478 DFGLARGVhhiDYYKKTSNGRLPvkWMAPEAL-------FdrVYTHQSDVWSFGILLWEIFT 532
Cdd:cd13987 136 DFGLTRRV---GSTVKRVSGTIP--YTAPEVCeakknegF--VVDPSIDVWAFGVLLFCCLT 190
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
321-583 1.38e-16

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 80.56  E-value: 1.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDssrpdqtsiVAVKMLkdnaSDKDLADLISEMEMMKLIG-RHKNIINLL-------GVCTQeg 392
Cdd:cd14143   3 IGKGRFGEVWRGRWRGED---------VAVKIF----SSREERSWFREAEIYQTVMlRHENILGFIaadnkdnGTWTQ-- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 pLYVIVEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYL-------ESRKCI-HRDLAAR 464
Cdd:cd14143  68 -LWLVSDYHEHGSLFDYL-----------------NRYTVTVEGMIKLALSIASGLAHLhmeivgtQGKPAIaHRDLKSK 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDDVMKIADFGLArgVHH---IDYYKKTSNGRLPVK-WMAPEALFDRVYTH------QSDVWSFGILLWEIF--- 531
Cdd:cd14143 130 NILVKKNGTCCIADLGLA--VRHdsaTDTIDIAPNHRVGTKrYMAPEVLDDTINMKhfesfkRADIYALGLVFWEIArrc 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   532 TLGGS------PY----PGIP-VEELFSLLREghRMERP--PNCPSE------LYGLMRECWHAAPSQRPT 583
Cdd:cd14143 208 SIGGIhedyqlPYydlvPSDPsIEEMRKVVCE--QKLRPniPNRWQScealrvMAKIMRECWYANGAARLT 276
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
321-611 1.49e-16

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 80.40  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdssrpdQTSIVAVKMLKDNASDKDL-ADLISEMEMMKLIGR--HKNIINLLGVC-----TQEG 392
Cdd:cd07838   7 IGEGAYGTVYKARDLQ-------DGRFVALKKVRVPLSEEGIpLSTIREIALLKQLESfeHPNVVRLLDVChgprtDREL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKgNLREFLRarRPPGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd07838  80 KLTLVFEHVDQ-DLATYLD--KCPKPGLPPE------------TIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARgvhhidyyKKTSNGRL-PVK---WM-APEALFDRVYTHQSDVWSFGILLWEIFT---LGGSPYPGIPVE 544
Cdd:cd07838 145 QVKLADFGLAR--------IYSFEMALtSVVvtlWYrAPEVLLQSSYATPVDMWSVGCIFAELFNrrpLFRGSSEADQLG 216
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   545 ELFSLLREGHRMERPPNCPselygLMRECWHaaPSQRPTFKQLVEALDKvllavseEYLDL---RLTFGP 611
Cdd:cd07838 217 KIFDVIGLPSEEEWPRNSA-----LPRSSFP--SYTPRPFKSFVPEIDE-------EGLDLlkkMLTFNP 272
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
309-589 1.63e-16

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 79.91  E-value: 1.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   309 EFPRDRLVLGKPLGEGCFGQVVCAealgmdssRPDQTS-IVAVKMLKDNASDKDLAD--LISEMEMMKLIgRHKNIINLL 385
Cdd:cd14117   2 KFTIDDFDIGRPLGKGKFGNVYLA--------REKQSKfIVALKVLFKSQIEKEGVEhqLRREIEIQSHL-RHPNILRLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   386 GVCTQEGPLYVIVEYAAKGNL-REFLRARRPpgpdlspDGPRSSegplsfpalvSCAYQVARGMQYLESRKCIHRDLAAR 464
Cdd:cd14117  73 NYFHDRKRIYLILEYAPRGELyKELQKHGRF-------DEQRTA----------TFMEELADALHYCHEKKVIHRDIKPE 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDDVMKIADFGLArgVHHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVE 544
Cdd:cd14117 136 NLLMGYKGELKIADFGWS--VHAPSLRRRTMCGTL--DYLPPEMIEGRTHDEKVDLWCIGVLCYE-LLVGMPPFESASHT 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 204138   545 ELFSLLREGHrMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14117 211 ETYRRIVKVD-LKFPPFLSDGSRDLISKLLRYHPSERLPLKGVME 254
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
321-531 2.28e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 80.08  E-value: 2.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALgmdssrPDQTSIVAVKMLKDNASDKDLA-DLISEMEMMKLIG--RHKNIINLLGVCT-----QEG 392
Cdd:cd07862   9 IGEGAYGKVFKARDL------KNGGRFVALKRVRVQTGEEGMPlSTIREVAVLRHLEtfEHPNVVRLFDVCTvsrtdRET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKgNLREFLRarRPPGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd07862  83 KLTLVFEHVDQ-DLTTYLD--KVPEPGVPTE------------TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   473 VMKIADFGLARgvhHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIF 531
Cdd:cd07862 148 QIKLADFGLAR---IYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF 203
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
11-87 2.42e-16

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 74.35  E-value: 2.42e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138    11 GNTVKFRCPAAGNPMPTIHWLKNGQAFHGENrigGIRLRHQHwSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:cd20978  16 GQDVTLPCQVTGVPQPKITWLHNGKPLQGPM---ERATVEDG-TLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
348-589 2.82e-16

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 78.96  E-value: 2.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdlspDGPRS 427
Cdd:cd14078  31 VAIKIMDKKALGDDLPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVLEYCPGGELFDYIVAK---------DRLSE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 SEGPLSFPALVSCayqVArgmqYLESRKCIHRDLAARNVLVTEDDVMKIADFGL-ARGVHHIDYYKKTSNGRLpvKWMAP 506
Cdd:cd14078 101 DEARVFFRQIVSA---VA----YVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGGMDHHLETCCGSP--AYAAP 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   507 EALFDRVYT-HQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGhRMERPPNCPSELYGLMRECWHAAPSQRPTFK 585
Cdd:cd14078 172 ELIQGKPYIgSEADVWSMGVLLYALLC-GFLPFDDDNVMALYRKIQSG-KYEEPEWLSPSSKLLLDQMLQVDPKKRITVK 249

                ....
gi 204138   586 QLVE 589
Cdd:cd14078 250 ELLN 253
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
307-540 3.03e-16

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 80.48  E-value: 3.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   307 LWEFPrDRLVLGKPLGEGCFGQVVCAEALGMDS-------SRPDQTSIVAVKMLKdnasdkdladlisEMEMMKLIgRHK 379
Cdd:cd07878  10 VWEVP-ERYQNLTPVGSGAYGSVCSAYDTRLRQkvavkklSRPFQSLIHARRTYR-------------ELRLLKHM-KHE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   380 NIINLLGVCTQEGPLYVIVEYAAKGNLReflrarrppGPDLSP--DGPRSSEGPLSFpaLVscaYQVARGMQYLESRKCI 457
Cdd:cd07878  75 NVIGLLDVFTPATSIENFNEVYLVTNLM---------GADLNNivKCQKLSDEHVQF--LI---YQLLRGLKYIHSAGII 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   458 HRDLAARNVLVTEDDVMKIADFGLARGVhhidyyKKTSNGRLPVKWM-APEALFDRVYTHQS-DVWSFGILLWEIFTlGG 535
Cdd:cd07878 141 HRDLKPSNVAVNEDCELRILDFGLARQA------DDEMTGYVATRWYrAPEIMLNWMHYNQTvDIWSVGCIMAELLK-GK 213

                ....*
gi 204138   536 SPYPG 540
Cdd:cd07878 214 ALFPG 218
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
378-592 3.32e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 78.79  E-value: 3.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   378 HKNIINLLGVCTQeGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCI 457
Cdd:cd14208  61 HKHLVLLHGVCVG-KDSIMVQEFVCHGALDLYLKKQQ-------------QKGPVAISWKLQVVKQLAYALNYLEDKQLV 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   458 HRDLAARNVLVTEDD------VMKIADFGLARGVHHIDYYKKtsngRLPvkWMAPEALFD-RVYTHQSDVWSFGILLWEI 530
Cdd:cd14208 127 HGNVSAKKVLLSREGdkgsppFIKLSDPGVSIKVLDEELLAE----RIP--WVAPECLSDpQNLALEADKWGFGATLWEI 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   531 FTLGGSPYPGIPVEELFSLLREghRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14208 201 FSGGHMPLSALDPSKKLQFYND--RKQLPAPHWIELASLIQQCMSYNPLLRPSFRAIIRDLN 260
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
318-589 3.46e-16

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 78.82  E-value: 3.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQvvCAEALGMDSSrpdqtSIVAVKMLKDN--ASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd14189   6 GRLLGKGGFAR--CYEMTDLATN-----KTYAVKVIPHSrvAKPHQREKIVNEIELHRDL-HHKHVVKFSHHFEDAENIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd14189  78 IFLELCSRKSLAHIWKARHT----------------LLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVHHIDYYKKTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGHR 555
Cdd:cd14189 142 VGDFGLAARLEPPEQRKKTICGT-P-NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFETLDLKETYRCIKQVKY 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 204138   556 MeRPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14189 219 T-LPASLSLPARHLLAGILKRNPGDRLTLDQILE 251
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
8-87 3.99e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 73.69  E-value: 3.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138        8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:smart00410   6 VKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
316-528 4.62e-16

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 78.46  E-value: 4.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVvcaeALGMDSSRPDQtsiVAVKML-KDNASDKDLADLIS-EMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:cd14079   5 ILGKTLGVGSFGKV----KLAEHELTGHK---VAVKILnRQKIKSLDMEEKIRrEIQILKLF-RHPHIIRLYEVIETPTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFL--RARrppgpdLSPDGPRSsegplSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd14079  77 IFMVMEYVSGGELFDYIvqKGR------LSEDEARR-----FFQQIIS-------GVEYCHRHMVVHRDLKPENLLLDSN 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   472 DVMKIADFGLARGVHHIDYYkKTSNGRlPvKWMAPEALFDRVYT-HQSDVWSFGILLW 528
Cdd:cd14079 139 MNVKIADFGLSNIMRDGEFL-KTSCGS-P-NYAAPEVISGKLYAgPEVDVWSCGVILY 193
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
321-581 4.73e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 80.04  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDE-------LYAIKILKKDVviQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05615  91 EYVNGGDLMYHIQ----------------QVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIAD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGvHHIDYYKKTSNGRLPvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREgHRMER 558
Cdd:cd05615 155 FGMCKE-HMVEGVTTRTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME-HNVSY 230
                       250       260
                ....*....|....*....|...
gi 204138   559 PPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd05615 231 PKSLSKEAVSICKGLMTKHPAKR 253
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
341-589 5.38e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 78.47  E-value: 5.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   341 RPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQegPLYVIVEYAAKGNLREFLrarrppgpdl 420
Cdd:cd14067  33 RTDGSADTMLKHLRAADAMKNFSEFRQEASMLHSL-QHPCIVYLIGISIH--PLCFALELAPLGSLNTVL---------- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   421 SPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV-----MKIADFGLARGVHHidyykkts 495
Cdd:cd14067 100 EENHKGSSFMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVqehinIKLSDYGISRQSFH-------- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   496 NGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGHR--MERPPNCP-SELYG 568
Cdd:cd14067 172 EGALGVEgtpgYQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAKKLSKGIRpvLGQPEEVQfFRLQA 250
                       250       260
                ....*....|....*....|.
gi 204138   569 LMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14067 251 LMMECWDTKPEKRPLACSVVE 271
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
318-589 5.64e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 78.50  E-value: 5.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVcaEALGMDSSrpdqtSIVAVKMLK----DNASDKDLADlisEMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:cd06626   5 GNKIGEGTFGKVY--TAVNLDTG-----ELMAMKEIRfqdnDPKTIKEIAD---EMKVLEGL-DHPNLVRYYGVEVHREE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpdlspdgprssegplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd06626  74 VYIFMEYCQEGTLEELLRHGR------------------ILDEAVIRVYtlQLLEGLAYLHENGIVHRDIKPANIFLDSN 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLArgvhhidyyKKTSNGRLPVK------------WMAPEalfdrVYTHQ--------SDVWSFGILLWEIF 531
Cdd:cd06626 136 GLIKLGDFGSA---------VKLKNNTTTMApgevnslvgtpaYMAPE-----VITGNkgeghgraADIWSLGCVVLEMA 201
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   532 TlGGSPYPGIpvEELFSLLREGHRMERPPNCPSEL-----YGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06626 202 T-GKRPWSEL--DNEWAIMYHVGMGHKPPIPDSLQlspegKDFLSRCLESDPKKRPTASELLD 261
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
321-548 6.33e-16

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 78.97  E-value: 6.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05587   4 LGKGSFGKVMLAE-------RKGTDELYAIKILKKDViiQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05587  77 EYVNGGDLMYHIQ----------------QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIAD 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFS 548
Cdd:cd05587 141 FGMCK--EGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQ 207
PHA02988 PHA02988
hypothetical protein; Provisional
348-591 6.46e-16

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 78.63  E-value: 6.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    348 VAVKMLK-DNASDKDLADL-ISEMEMMKLIGRHkNIINLLG----VCTQEGPLYVIVEYAAKGNLREFLRarrppgpdls 421
Cdd:PHA02988  46 VIIRTFKkFHKGHKVLIDItENEIKNLRRIDSN-NILKIYGfiidIVDDLPRLSLILEYCTRGYLREVLD---------- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    422 pdgprsSEGPLSFPALVSCAYQVARGMQYL-ESRKCIHRDLAARNVLVTEDDVMKIADFGLargvhhidyYKKTSNGrlP 500
Cdd:PHA02988 115 ------KEKDLSFKTKLDMAIDCCKGLYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGL---------EKILSSP--P 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    501 VKWMAPEALFDR--------VYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLLREGHRMER-PPNCPSELYGLMR 571
Cdd:PHA02988 178 FKNVNFMVYFSYkmlndifsEYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIINKNNSLKlPLDCPLEIKCIVE 256
                        250       260
                 ....*....|....*....|
gi 204138    572 ECWHAAPSQRPTFKQLVEAL 591
Cdd:PHA02988 257 ACTSHDSIKRPNIKEILYNL 276
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
314-583 6.71e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 77.85  E-value: 6.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEALGMDSSRpdqtsivAVKMLKDnASDKDLA--DLISEMEMMKLIGR--HKNIINLLGVCT 389
Cdd:cd08222   1 RYRVVRKLGSGNFGTVYLVSDLKATADE-------ELKVLKE-ISVGELQpdETVDANREAKLLSKldHPAIVKFHDSFV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRARRPPGPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVt 469
Cdd:cd08222  73 EKESFCIVTEYCEGGDLDDKISEYKKSGTTIDEN------------QILDWFIQLLLAVQYMHERRILHRDLKAKNIFL- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSpYPGipvEELFSL 549
Cdd:cd08222 140 KNNVIKVGDFGISRILMGTSDLATTFTGT-PY-YMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHA-FDG---QNLLSV 213
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   550 LR---EGHRMERPPNCPSELYGLMRECWHAAPSQRPT 583
Cdd:cd08222 214 MYkivEGETPSLPDKYSKELNAIYSRMLNKDPALRPS 250
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
315-592 6.93e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 78.07  E-value: 6.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGQVV--CAEALGmDSSRPDQTSIVaVKMLkDNASDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEG 392
Cdd:cd05078   1 LIFNESLGQGTFTKIFkgIRREVG-DYGQLHETEVL-LKVL-DKAHRNYSESFFEAASMMSQLS-HKHLVLNYGVCVCGD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRARRppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT-ED 471
Cdd:cd05078  77 ENILVQEYVKFGSLDTYLKKNK---------------NCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIrEE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 D-------VMKIADFGLARGVHHIDYYKKtsngRLPvkWMAPEALFD-RVYTHQSDVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd05078 142 DrktgnppFIKLSDPGISITVLPKDILLE----RIP--WVPPECIENpKNLSLATDKWSFGTTLWEICSGGDKPLSALDS 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 204138   544 EELFSLLREGHRMERPPncPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd05078 216 QRKLQFYEDRHQLPAPK--WTELANLINNCMDYEPDHRPSFRAIIRDLN 262
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
313-589 7.21e-16

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 78.23  E-value: 7.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGQVvcaealgmDSSRPDQT-SIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQE 391
Cdd:cd06617   1 DDLEVIEELGRGAYGVV--------DKMRHVPTgTIMAVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEyAAKGNLREFLRARRPPGPDLsPDgprssegplsfPALVSCAYQVARGMQYLESR-KCIHRDLAARNVLVTE 470
Cdd:cd06617  73 GDVWICME-VMDTSLDKFYKKVYDKGLTI-PE-----------DILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINR 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARgvHHIDYYKKTSN-GRLPvkWMAPE----ALFDRVYTHQSDVWSFGILLWEIFTlGGSPYP--GIPV 543
Cdd:cd06617 140 NGQVKLCDFGISG--YLVDSVAKTIDaGCKP--YMAPErinpELNQKGYDVKSDVWSLGITMIELAT-GRFPYDswKTPF 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   544 EELFSLLReghrmERPPNCPSELYGL-----MRECWHAAPSQRPTFKQLVE 589
Cdd:cd06617 215 QQLKQVVE-----EPSPQLPAEKFSPefqdfVNKCLKKNYKERPNYPELLQ 260
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
348-595 9.12e-16

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 78.25  E-value: 9.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLkdnaSDKDLADLISEMEMMKLIG-RHKNIINLLGV-------CTQegpLYVIVEYAAKGNLREFLrarrppgpd 419
Cdd:cd14142  31 VAVKIF----SSRDEKSWFRETEIYNTVLlRHENILGFIASdmtsrnsCTQ---LWLITHYHENGSLYDYL--------- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   420 lspdgprsSEGPLSFPALVSCAYQVARGMQYL-------ESRKCI-HRDLAARNVLVTEDDVMKIADFGLArgVHH---I 488
Cdd:cd14142  95 --------QRTTLDHQEMLRLALSAASGLVHLhteifgtQGKPAIaHRDLKSKNILVKSNGQCCIADLGLA--VTHsqeT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   489 DYYKKTSNGRLPVK-WMAPEALFDRVYT------HQSDVWSFGILLWEI---FTLGG-----SP--YPGIPVEELFSLLR 551
Cdd:cd14142 165 NQLDVGNNPRVGTKrYMAPEVLDETINTdcfesyKRVDIYAFGLVLWEVarrCVSGGiveeyKPpfYDVVPSDPSFEDMR 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   552 -----EGHRmerpPNCP---------SELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd14142 245 kvvcvDQQR----PNIPnrwssdptlTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
321-531 9.32e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 78.08  E-value: 9.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNASDKDLAdlISEMEMMKLIGR-----HKNIINLLGVCT-----Q 390
Cdd:cd07863   8 IGVGAYGTVYKAR-------DPHSGHFVALKSVRVQTNEDGLP--LSTVREVALLKRleafdHPNIVRLMDVCAtsrtdR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKgNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd07863  79 ETKVTLVFEHVDQ-DLRTYLDKVPPPG--------------LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTS 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   471 DDVMKIADFGLARgvhhIDYYKKTSNGRLPVKWM-APEALFDRVYTHQSDVWSFGILLWEIF 531
Cdd:cd07863 144 GGQVKLADFGLAR----IYSCQMALTPVVVTLWYrAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
319-595 9.83e-16

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 77.76  E-value: 9.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDSSrpdqtsiVAVKMLKDNASDkDLADLISEMEMMKLIGRHKNIINLLG---VCTQEGPLY 395
Cdd:cd13985   6 KQLGEGGFSYVYLAHDVNTGRR-------YALKRMYFNDEE-QLRVAIKEIEIMKRLCGHPNIVQYYDsaiLSSEGRKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIV-EYAaKGNLREFLRaRRPPGPdlspdgprssegpLSFPALVSCAYQVARGMQYL--ESRKCIHRDLAARNVLVTEDD 472
Cdd:cd13985  78 LLLmEYC-PGSLVDILE-KSPPSP-------------LSEEEVLRIFYQICQAVGHLhsQSPPIIHRDIKIENILFSNTG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVHHIDYYKKTSN-------GRLPVKWMAPEA--LFDRV-YTHQSDVWSFGILLWEI--FTLggsPY-P 539
Cdd:cd13985 143 RFKLCDFGSATTEHYPLERAEEVNiieeeiqKNTTPMYRAPEMidLYSKKpIGEKADIWALGCLLYKLcfFKL---PFdE 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   540 GIPVEELFSllreGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd13985 220 SSKLAIVAG----KYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIITKDT 271
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
321-545 1.05e-15

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 78.17  E-value: 1.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSRPdqtsiVAVKMLKdnASDKDLadLISEMEMMKLIG-RHKNIINLLGVCTQEGPL----Y 395
Cdd:cd14054   3 IGQGRYGTVW----KGSLDERP-----VAVKVFP--ARHRQN--FQNEKDIYELPLmEHSNILRFIGADERPTADgrmeY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIV-EYAAKGNLREFLRarrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLES--------RKCI-HRDLAARN 465
Cdd:cd14054  70 LLVlEYAPKGSLCSYLR-----------------ENTLDWMSSCRMALSLTRGLAYLHTdlrrgdqyKPAIaHRDLNSRN 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   466 VLVTEDDVMKIADFGLA---RGVHHIDYYKKTSNGRLP-----VKWMAPEALFDRV-------YTHQSDVWSFGILLWEI 530
Cdd:cd14054 133 VLVKADGSCVICDFGLAmvlRGSSLVRGRPGAAENASIsevgtLRYMAPEVLEGAVnlrdcesALKQVDVYALGLVLWEI 212
                       250
                ....*....|....*
gi 204138   531 FTLGGSPYPGIPVEE 545
Cdd:cd14054 213 AMRCSDLYPGESVPP 227
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
321-559 1.28e-15

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 77.13  E-value: 1.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSSRpdqtsivAVKML---KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14098   8 LGSGTFAEVKKAVEVETGKMR-------AIKQIvkrKVAGNDKNLQLFQREINILKSL-EHPGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD--VMK 475
Cdd:cd14098  80 MEYVEGGDLMDFI----------------MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARgVHHIDYYKKTSNGRLpvKWMAPEALFDR------VYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSL 549
Cdd:cd14098 144 ISDFGLAK-VIHTGTFLVTFCGTM--AYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKR 219
                       250
                ....*....|
gi 204138   550 LREGHRMERP 559
Cdd:cd14098 220 IRKGRYTQPP 229
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
311-588 1.31e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 77.38  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDNASDkDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd06646   7 PQHDYELIQRVGSGTYGDVYKARNL-------HTGELAAVKIIKLEPGD-DFSLIQQEIFMVKEC-KHCNIVAYFGSYLS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRArrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06646  78 REKLWICMEYCGGGSLQDIYHV----------------TGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTD 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPE-ALFDRV--YTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd06646 142 NGDVKLADFGVAAKITATIAKRKSFIGT-PY-WMAPEvAAVEKNggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALF 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   548 SLLREGHrmeRPPNCPSEL------YGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd06646 220 LMSKSNF---QPPKLKDKTkwsstfHNFVKISLTKNPKKRPTAERLL 263
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
321-587 1.80e-15

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 76.58  E-value: 1.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdsSRPDqTSIVAVKMLKDN-ASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd14050   9 LGEGSFGEVFKVR------SRED-GKLYAVKRSRSRfRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKgNLREFLRARrppgPDLSPDgprssegplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd14050  82 LCDT-SLQQYCEET----HSLPES------------EVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GL-----ARGVHHIdyykktSNGrlPVKWMAPEALfDRVYTHQSDVWSFGILLWEIFTLGGSPYPGipveELFSLLREGH 554
Cdd:cd14050 145 GLvveldKEDIHDA------QEG--DPRYMAPELL-QGSFTKAADIFSLGITILELACNLELPSGG----DGWHQLRQGY 211
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 204138   555 rmeRPPNC----PSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14050 212 ---LPEEFtaglSPELRSIIKLMMDPDPERRPTAEDL 245
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
317-588 1.87e-15

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 76.99  E-value: 1.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQV-VCAEAlgmDSSRPdqtsiVAVKML----KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT-- 389
Cdd:cd06653   6 LGKLLGRGAFGEVyLCYDA---DTGRE-----LAVKQVpfdpDSQETSKEVNALECEIQLLKNL-RHDRIVQYYGCLRdp 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd06653  77 EEKKLSIFVEYMPGGSVKDQLKAY----------------GALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRD 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARGVHHIdyyKKTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVE 544
Cdd:cd06653 141 SAGNVKLGDFGASKRIQTI---CMSGTGIKSVTgtpyWMSPEVISGEGYGRKADVWSVACTVVEMLT-EKPPWAEYeAMA 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   545 ELFSLLREGHRMERPPNCPSELYGLMRECWhAAPSQRPTFKQLV 588
Cdd:cd06653 217 AIFKIATQPTKPQLPDGVSDACRDFLRQIF-VEEKRRPTAEFLL 259
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
313-589 1.90e-15

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 77.08  E-value: 1.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGQVvcaealGMDSSRPDQTsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT--Q 390
Cdd:cd06621   1 DKIVELSSLGEGAGGSV------TKCRLRNTKT-IFALKTITTDPNPDVQKQILRELEINKSC-ASPYIVKYYGAFLdeQ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRarrppgpDLSPDGPRSSEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06621  73 DSSIGIAMEYCEGGSLDSIYK-------KVKKKGGRIGEKVLG-----KIAESVLKGLSYLHSRKIIHRDIKPSNILLTR 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFG--------LARGVHHIDYYkktsngrlpvkwMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYP--G 540
Cdd:cd06621 141 KGQVKLCDFGvsgelvnsLAGTFTGTSYY------------MAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFPpeG 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   541 IPVEELFSLLREGHRMERP--PNCPS-------ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06621 208 EPPLGPIELLSYIVNMPNPelKDEPEngikwseSFKDFIEKCLEKDGTRRPGPWQMLA 265
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
1-87 1.92e-15

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 71.81  E-value: 1.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     1 MEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENrIGgiRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIR 80
Cdd:cd05856   9 MRRRVIARPVGSSVRLKCVASGNPRPDITWLKDNKPLTPPE-IG--ENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEIN 85

                ....*..
gi 204138    81 YSYLLDV 87
Cdd:cd05856  86 ATYKVDV 92
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
311-589 2.37e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 76.62  E-value: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDNASDkDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd06645   9 PQEDFELIQRIGSGTYGDVYKARNV-------NTGELAAIKVIKLEPGE-DFAVVQQEIIMMKDC-KHSNIVAYFGSYLR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRArrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06645  80 RDKLWICMEFCGGGSLQDIYHV----------------TGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPE-ALFDRV--YTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELF 547
Cdd:cd06645 144 NGHVKLADFGVSAQITATIAKRKSFIGT-PY-WMAPEvAAVERKggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALF 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 204138   548 SLLREGHrmeRPPNCPSEL------YGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06645 222 LMTKSNF---QPPKLKDKMkwsnsfHHFVKMALTKNPKKRPTAEKLLQ 266
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
321-550 3.01e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 76.97  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd07873  10 LGEGTYATVYKGRSKLTDN-------LVALKEIRLEHEEGAPCTAIREVSLLKDL-KHANIVTLHDIIHTEKSLTLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKgNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd07873  82 LDK-DLKQYLD---------------DCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   481 LARGVhhiDYYKKTSNGRLPVKWMAPEALF--DRVYTHQSDVWSFGILLWEIFTlgGSP-YPGIPVEE----LFSLL 550
Cdd:cd07873 146 LARAK---SIPTKTYSNEVVTLWYRPPDILlgSTDYSTQIDMWGVGCIFYEMST--GRPlFPGSTVEEqlhfIFRIL 217
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
322-533 3.09e-15

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 76.94  E-value: 3.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   322 GEGCFGQVVCAealgmDSSRPDQTSIVAVKMLKdnaSDKDLADLIS-----EMEMMKLIgRHKNIINLLGVC--TQEGPL 394
Cdd:cd07842   9 GRGTYGRVYKA-----KRKNGKDGKEYAIKKFK---GDKEQYTGISqsacrEIALLREL-KHENVVSLVEVFleHADKSV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAaKGNLREFLRARRPPGPDLSPDgprssegplsfPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT----E 470
Cdd:cd07842  80 YLLFDYA-EHDLWQIIKFHRQAKRVSIPP-----------SMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMgegpE 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   471 DDVMKIADFGLARGVHhiDYYKKTSNGRLPVK--WM-APEALFD-RVYTHQSDVWSFGILLWEIFTL 533
Cdd:cd07842 148 RGVVKIGDLGLARLFN--APLKPLADLDPVVVtiWYrAPELLLGaRHYTKAIDIWAIGCIFAELLTL 212
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
318-553 3.18e-15

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 76.05  E-value: 3.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVVcaEALGMDSsrpdQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14097   6 GRKLGQGSFGVVI--EATHKET----QTKWAIKKINREKAGSSAVKLLEREVDILKHV-NHAHIIHLEEVFETPKRMYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRppgpDLSPDGPRSsegplsfpaLVSCayqVARGMQYLESRKCIHRDLAARNVLVTEDDV---- 473
Cdd:cd14097  79 MELCEDGELKELLLRKG----FFSENETRH---------IIQS---LASAVAYLHKNDIVHRDLKLENILVKSSIIdnnd 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 ---MKIADFGLA-----RGVHHIdyykkTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPGIPVEE 545
Cdd:cd14097 143 klnIKVTDFGLSvqkygLGEDML-----QETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEK 215

                ....*...
gi 204138   546 LFSLLREG 553
Cdd:cd14097 216 LFEEIRKG 223
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
321-532 4.00e-15

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 76.40  E-value: 4.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdssrpdQTSIVAVKMLKDNAS---DKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14159   1 IGEGGFGCVYQAVM---------RNTEYAVKRLKEDSEldwSVVKNSFLTEVEKLSRF-RHPNIVDLAGYSAQQGNYCLI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRarrppgpdlspdgPRSSEGPLSFPALVSCAYQVARGMQYL--ESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd14159  71 YVYLPNGSLEDRLH-------------CQVSCPCLSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPK 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   476 IADFGLARgvhhidYYKKTSNG------------RLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd14159 138 LGDFGLAR------FSRRPKQPgmsstlartqtvRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT 200
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
317-589 4.09e-15

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 75.75  E-value: 4.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQV-VCaealgmdssRP-DQTSIVAVKMLkDNASDKDLADLI-SEMEMMKLIGrHKNIINLLGVCTQEGP 393
Cdd:cd14185   4 IGRTIGDGNFAVVkEC---------RHwNENQEYAMKII-DKSKLKGKEDMIeSEILIIKSLS-HPNIVKLFEVYETEKE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLRE-FLRARRPPGPDlspdgprssegplsfPALVscAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14185  73 IYLILEYVRGGDLFDaIIESVKFTEHD---------------AALM--IIDLCEALVYIHSKHIVHRDLKPENLLVQHNP 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 ----VMKIADFGLARGVHHIDYykkTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY--PGIPVEEL 546
Cdd:cd14185 136 dkstTLKLADFGLAKYVTGPIF---TVCGT-PT-YVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFrsPERDQEEL 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 204138   547 FSLLREGHRMERPP---NCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14185 210 FQIIQLGHYEFLPPywdNISEAAKDLISRLLVVDPEKRYTAKQVLQ 255
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
349-589 4.19e-15

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 76.22  E-value: 4.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLkdnasDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLRE-FLRARrppgpdlspdgpRS 427
Cdd:cd14175  30 AVKVI-----DKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDkILRQK------------FF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 SEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTED----DVMKIADFGLARGVhhidyykKTSNGRL---- 499
Cdd:cd14175  93 SEREAS-----SVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsgnpESLRICDFGFAKQL-------RAENGLLmtpc 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   500 -PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY---PGIPVEELFSLLREGHRMERPPN---CPSELYGLMRE 572
Cdd:cd14175 161 yTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFangPSDTPEEILTRIGSGKFTLSGGNwntVSDAAKDLVSK 239
                       250
                ....*....|....*..
gi 204138   573 CWHAAPSQRPTFKQLVE 589
Cdd:cd14175 240 MLHVDPHQRLTAKQVLQ 256
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
102-196 4.30e-15

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.61  E-value: 4.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138      102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKHiviNGSSLGADGfpyvqvlKTTDINSSEVEVLYLRNVSAEDAGEYTCLA 181
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQ---GGKLLAESG-------RFSVSRSGSTSTLTISNVTPEDSGTYTCAA 70
                           90
                   ....*....|....*
gi 204138      182 GNSIGLSYQSAWLTV 196
Cdd:smart00410  71 TNSSGSASSGTTLTV 85
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
319-589 4.55e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 76.63  E-value: 4.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAealgmdssRPDQTS-IVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd06635  31 REIGHGSFGAVYFA--------RDVRTSeVVAIKKMSYSGkqSNEKWQDIIKEVKFLQRI-KHPNSIEYKGCYLREHTAW 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAkGNLREFLRARRPPGPDLSpdgprssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd06635 102 LVMEYCL-GSASDLLEVHKKPLQEIE---------------IAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVHHIDYYKKTSngrlpvKWMAPE---ALFDRVYTHQSDVWSFGILLWEIftlgGSPYPGIPVEELFSLLRE 552
Cdd:cd06635 166 LADFGSASIASPANSFVGTP------YWMAPEvilAMDEGQYDGKVDVWSLGITCIEL----AERKPPLFNMNAMSALYH 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   553 GHRMERPPNCPSELYGLMR----ECWHAAPSQRPTFKQLVE 589
Cdd:cd06635 236 IAQNESPTLQSNEWSDYFRnfvdSCLQKIPQDRPTSEELLK 276
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
319-552 5.78e-15

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 76.46  E-value: 5.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqVVCaealgmdSSRPDQTSI-VAVKMLKDNASDKDLAD-LISEMEMMKLIgRHKNIINLLGVCTQegPL-- 394
Cdd:cd07856  16 QPVGMGAFG-LVC-------SARDQLTGQnVAVKKIMKPFSTPVLAKrTYRELKLLKHL-RHENIISLSDIFIS--PLed 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 -YVIVEYAAKgNLREFLRARrppgpdlspdgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd07856  85 iYFVTELLGT-DLHRLLTSR-----------------PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLAR-------GVHHIDYYKktsngrlpvkwmAPEALFD-RVYTHQSDVWSFGILLWEIftLGGSP-YPGIPVE 544
Cdd:cd07856 147 LKICDFGLARiqdpqmtGYVSTRYYR------------APEIMLTwQKYDVEVDIWSAGCIFAEM--LEGKPlFPGKDHV 212

                ....*...
gi 204138   545 ELFSLLRE 552
Cdd:cd07856 213 NQFSIITE 220
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
317-532 5.94e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 75.47  E-value: 5.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQV-VCAEAlgmDSSRPdqtsiVAVKMLKDNA----SDKDLADLISEMEMMKLIgRHKNIINLLGVC--T 389
Cdd:cd06652   6 LGKLLGQGAFGRVyLCYDA---DTGRE-----LAVKQVQFDPespeTSKEVNALECEIQLLKNL-LHERIVQYYGCLrdP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd06652  77 QERTLSIFMEYMPGGSIKDQLKSY----------------GALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRD 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   470 EDDVMKIADFGLARGVHHIDYykkTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd06652 141 SVGNVKLGDFGASKRLQTICL---SGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
394-588 6.33e-15

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 75.41  E-value: 6.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14010  69 LWLVVEYCTGGDLETLLR----------------QDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGT 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLAR-----------GVHHIDYYKKTSNGRLPV---KWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYP 539
Cdd:cd14010 133 LKLSDFGLARregeilkelfgQFSDEGNVNKVSKKQAKRgtpYYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFV 211
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   540 GIPVEEL--------FSLLREGHRMERPPNCPSELYGLMREcwhaAPSQRPTFKQLV 588
Cdd:cd14010 212 AESFTELvekilnedPPPPPPKVSSKPSPDFKSLLKGLLEK----DPAKRLSWDELV 264
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
348-565 6.39e-15

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 75.43  E-value: 6.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprs 427
Cdd:cd14201  35 VAIKSINKKNLSKSQILLGKEIKILKEL-QHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLQAK-------------- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 seGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD---------VMKIADFGLARGVHHiDYYKKTSNGR 498
Cdd:cd14201 100 --GTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYLQS-NMMAATLCGS 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   499 lPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELFSLLREGHRMErpPNCPSE 565
Cdd:cd14201 177 -PM-YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDLRMFYEKNKNLQ--PSIPRE 238
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
321-551 6.44e-15

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 75.40  E-value: 6.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALgmdssRPDQtsIVAVKMLKDNASDKDL-ADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd07835   7 IGEGTYGVVYKARDK-----LTGE--IVALKKIRLETEDEGVpSTAIREISLLKEL-NHPNIVRLLDVVHSENKLYLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKgNLREFLrarrppgpDLSPDGPRSsegplsfPALV-SCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd07835  79 FLDL-DLKKYM--------DSSPLTGLD-------PPLIkSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLAD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLARGVHhidyykktsngrLPVK---------WM-APEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPG-IPVEE 545
Cdd:cd07835 143 FGLARAFG------------VPVRtythevvtlWYrAPEILLgSKHYSTPVDIWSVGCIFAEMVT--RRPlFPGdSEIDQ 208

                ....*.
gi 204138   546 LFSLLR 551
Cdd:cd07835 209 LFRIFR 214
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
307-532 6.70e-15

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 76.53  E-value: 6.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   307 LWEFPrDRLVLGKPLGEGCFGqVVCAEALGMDSSRpdqtsiVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLL 385
Cdd:cd07880  10 IWEVP-DRYRDLKQVGSGAYG-TVCSALDRRTGAK------VAIKKLyRPFQSELFAKRAYRELRLLKHM-KHENVIGLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   386 GVCTQEGPLyviveyaakGNLREFLRARRPPGPDLSP--DGPRSSEGPLSFpaLVscaYQVARGMQYLESRKCIHRDLAA 463
Cdd:cd07880  81 DVFTPDLSL---------DRFHDFYLVMPFMGTDLGKlmKHEKLSEDRIQF--LV---YQMLKGLKYIHAAGIIHRDLKP 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   464 RNVLVTEDDVMKIADFGLARgvhHIDyykKTSNGRLPVKWM-APEALFDRV-YTHQSDVWSFGILLWEIFT 532
Cdd:cd07880 147 GNLAVNEDCELKILDFGLAR---QTD---SEMTGYVVTRWYrAPEVILNWMhYTQTVDIWSVGCIMAEMLT 211
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
321-530 6.82e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 75.84  E-value: 6.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdsSRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd06633  29 IGHGSFGAVYFA-------TNSHTNEVVAIKKMSYSGkqTNEKWQDIIKEVKFLQQL-KHPNTIEYKGCYLKDHTAWLVM 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAkGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd06633 101 EYCL-GSASDLLEVHKKP---------------LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLAD 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   479 FGLARGVHHIDYYKKTSngrlpvKWMAPE---ALFDRVYTHQSDVWSFGILLWEI 530
Cdd:cd06633 165 FGSASIASPANSFVGTP------YWMAPEvilAMDEGQYDGKVDIWSLGITCIEL 213
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
321-532 7.03e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 75.87  E-value: 7.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdssRPDQTS-IVAVKM-LKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQE------- 391
Cdd:cd07865  20 IGQGTFGEVFKA--------RHRKTGqIVALKKvLMENEKEGFPITALREIKILQLL-KHENVVNLIEICRTKatpynry 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 -GPLYVIVEYAAKgnlreflrarrppgpDLSpdgprsseGPLSFPALVSCAYQVARGMQ-------YLESRKCIHRDLAA 463
Cdd:cd07865  91 kGSIYLVFEFCEH---------------DLA--------GLLSNKNVKFTLSEIKKVMKmllnglyYIHRNKILHRDMKA 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   464 RNVLVTEDDVMKIADFGLARGVHhidyYKKTSN-----GRLPVKWM-APEALF-DRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd07865 148 ANILITKDGVLKLADFGLARAFS----LAKNSQpnrytNRVVTLWYrPPELLLgERDYGPPIDMWGAGCIMAEMWT 219
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
319-540 7.80e-15

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 75.90  E-value: 7.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALgmdsSRPDQTSIVAVKMLKDNA---SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd05584   2 KVLGKGGYGKVFQVRKT----TGSDKGKIFAMKVLKKASivrNQKDTAHTKAERNILEAV-KHPFIVDLHYAFQTGGKLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLreFLRARRppgpdlspdgprssEGplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05584  77 LILEYLSGGEL--FMHLER--------------EG--IFMEDTACFYlaEITLALGHLHSLGIIYRDLKPENILLDAQGH 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   474 MKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd05584 139 VKLTDFGLCKESIHDGTVTHTFCG--TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTA 202
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
319-583 7.83e-15

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 75.21  E-value: 7.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDssrpdqtsiVAVKMLKDNASdkdlADLISEMEMMK-LIGRHKNIINLL-------GVCTQ 390
Cdd:cd14144   1 RSVGKGRYGEVWKGKWRGEK---------VAVKIFFTTEE----ASWFRETEIYQtVLMRHENILGFIaadikgtGSWTQ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 egpLYVIVEYAAKGNLREFLRARRppgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKC--------IHRDLA 462
Cdd:cd14144  68 ---LYLITDYHENGSLYDFLRGNT-----------------LDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIK 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   463 ARNVLVTEDDVMKIADFGLA-RGVHHIDYYKKTSNGRLPVK-WMAPEAL--------FDRVytHQSDVWSFGILLWEIFT 532
Cdd:cd14144 128 SKNILVKKNGTCCIADLGLAvKFISETNEVDLPPNTRVGTKrYMAPEVLdeslnrnhFDAY--KMADMYSFGLVLWEIAR 205
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   533 LGGSP----------YPGIPVEELFSLLREGHRMER-PPNCPSELYG---------LMRECWHAAPSQRPT 583
Cdd:cd14144 206 RCISGgiveeyqlpyYDAVPSDPSYEDMRRVVCVERrRPSIPNRWSSdevlrtmskLMSECWAHNPAARLT 276
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
344-594 9.47e-15

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 74.45  E-value: 9.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   344 QTSIVAvKMLK-DNASDKDLADLISEMEMMKlIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRArrppGPDLSP 422
Cdd:cd14057  18 GNDIVA-KILKvRDVTTRISRDFNEEYPRLR-IFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHE----GTGVVV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   423 DGPRSsegplsfpalVSCAYQVARGMQYLESRKCI--HRDLAARNVLVTEDDVMKI--ADFGLARgvhhidyykkTSNGR 498
Cdd:cd14057  92 DQSQA----------VKFALDIARGMAFLHTLEPLipRHHLNSKHVMIDEDMTARInmADVKFSF----------QEPGK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   499 L--PVkWMAPEALF---DRVYTHQSDVWSFGILLWEIFTLGgSPYPGI-PVEELFSLLREGHRMERPPNCPSELYGLMRE 572
Cdd:cd14057 152 MynPA-WMAPEALQkkpEDINRRSADMWSFAILLWELVTRE-VPFADLsNMEIGMKIALEGLRVTIPPGISPHMCKLMKI 229
                       250       260
                ....*....|....*....|..
gi 204138   573 CWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14057 230 CMNEDPGKRPKFDMIVPILEKM 251
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
311-589 1.08e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 75.15  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAE--ALGMDssrpdqtsiVAVKMLK-DNASDKDLadLISEMEMMKLIgRHKNIINLLGV 387
Cdd:cd06655  17 PKKKYTRYEKIGQGASGTVFTAIdvATGQE---------VAIKQINlQKQPKKEL--IINEILVMKEL-KNPNIVNFLDS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   388 CTQEGPLYVIVEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd06655  85 FLVGDELFVVMEYLAGGSLTDVV-----------------TETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   468 VTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEEL 546
Cdd:cd06655 148 LGMDGSVKLTDFGFCAQITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNEnPLRAL 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   547 FSLLREGH-RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06655 225 YLIATNGTpELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQ 268
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
316-586 1.16e-14

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 74.47  E-value: 1.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVVcaEALGMDSSRPdqtsiVAVKMLKDNASDKD---LADLISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd14070   5 LIGRKLGEGSFAKVR--EGLHAVTGEK-----VAIKVIDKKKAKKDsyvTKNLRREGRIQQMI-RHPNITQLLDILETEN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRarrppgpdlspDGPRSSEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14070  77 SYYLVMELCPGGNLMHRIY-----------DKKRLEEREAR-----RYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEND 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIP--VEELFSLL 550
Cdd:cd14070 141 NIKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVEPfsLRALHQKM 219
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 204138   551 REGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd14070 220 VDKEMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQ 255
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
321-545 1.44e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 74.39  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd07839   8 IGEGTYGTVFKAK-------NRETHEIVALKRVRlDDDDEGVPSSALREICLLKEL-KHKNIVRLYDVLHSDKKLTLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKgNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd07839  80 YCDQ-DLKKYFD---------------SCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADF 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   480 GLARgvhhidyykktsNGRLPVK----------WMAPEALFD-RVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEE 545
Cdd:cd07839 144 GLAR------------AFGIPVRcysaevvtlwYRPPDVLFGaKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDD 208
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
311-589 1.46e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 74.76  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAealgMDSSRPDQTSIVAVKMlkDNASDKDLadLISEMEMMKLiGRHKNIINLLGVCTQ 390
Cdd:cd06654  18 PKKKYTRFEKIGQGASGTVYTA----MDVATGQEVAIRQMNL--QQQPKKEL--IINEILVMRE-NKNPNIVNYLDSYLV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06654  89 GDELWVVMEYLAGGSLTDVV-----------------TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSL 549
Cdd:cd06654 152 DGSVKLTDFGFCAQITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNEnPLRALYLI 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   550 LREGH-RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06654 229 ATNGTpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQ 269
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
312-532 1.46e-14

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 75.04  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKpLGEGCFGQVVCAEalgmdsSRPDQTSIVAVKMLKDNAsdKDLADL--ISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd07866   8 RDYEILGK-LGEGTFGEVYKAR------QIKTGRVVALKKILMHNE--KDGFPItaLREIKILKKL-KHPNVVPLIDMAV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGP--------LYVIVEYAAKgnlreflrarrppgpDLSpdgprsseGPLSFPAL------VSC-AYQVARGMQYLESR 454
Cdd:cd07866  78 ERPDkskrkrgsVYMVTPYMDH---------------DLS--------GLLENPSVkltesqIKCyMLQLLEGINYLHEN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   455 KCIHRDLAARNVLVTEDDVMKIADFGLARGvhhidYY-KKTSNGRLP------------VKWM-APEALF-DRVYTHQSD 519
Cdd:cd07866 135 HILHRDIKAANILIDNQGILKIADFGLARP-----YDgPPPNPKGGGgggtrkytnlvvTRWYrPPELLLgERRYTTAVD 209
                       250
                ....*....|...
gi 204138   520 VWSFGILLWEIFT 532
Cdd:cd07866 210 IWGIGCVFAEMFT 222
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
340-589 1.46e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 76.59  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    340 SRPDQTSIVAVKMLKDnasDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpd 419
Cdd:PTZ00267  90 SDPKEKVVAKFVMLND---ERQAAYARSELHCLAAC-DHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQR------ 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    420 LSPDGP-RSSEGPLSFpalvscaYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARgvhhidyyKKTSNGR 498
Cdd:PTZ00267 160 LKEHLPfQEYEVGLLF-------YQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSK--------QYSDSVS 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    499 LPVK--------WMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFSLLREGHRMERPPNCPSELYGLM 570
Cdd:PTZ00267 225 LDVAssfcgtpyYLAPELWERKRYSKKADMWSLGVILYELLTL-HRPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALL 303
                        250
                 ....*....|....*....
gi 204138    571 RECWHAAPSQRPTFKQLVE 589
Cdd:PTZ00267 304 DPLLSKNPALRPTTQQLLH 322
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
307-532 1.57e-14

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 75.32  E-value: 1.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   307 LWEFPRdRLVLGKPLGEGCFGQVVCA------EALGMDS-SRPDQTSIVAVKMLKdnasdkdladlisEMEMMKLIgRHK 379
Cdd:cd07879  10 VWELPE-RYTSLKQVGSGAYGSVCSAidkrtgEKVAIKKlSRPFQSEIFAKRAYR-------------ELTLLKHM-QHE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   380 NIINLLGVCTQEGPLYviveyaakgNLREFLRARrppgPDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHR 459
Cdd:cd07879  75 NVIGLLDVFTSAVSGD---------EFQDFYLVM----PYMQTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHR 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138   460 DLAARNVLVTEDDVMKIADFGLARgvhHIDyykKTSNGRLPVKWM-APEALFDRV-YTHQSDVWSFGILLWEIFT 532
Cdd:cd07879 142 DLKPGNLAVNEDCELKILDFGLAR---HAD---AEMTGYVVTRWYrAPEVILNWMhYNQTVDIWSVGCIMAEMLT 210
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
321-538 1.89e-14

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 73.81  E-value: 1.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCA--EALGMDssrpdqtsiVAVKMLkdNASDKDLADLI-SEMEMMKLiGRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd06647  15 IGQGASGTVYTAidVATGQE---------VAIKQM--NLQQQPKKELIiNEILVMRE-NKNPNIVNYLDSYLVGDELWVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd06647  83 MEYLAGGSLTDVV-----------------TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLT 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   478 DFGLARGVHHiDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd06647 146 DFGFCAQITP-EQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 203
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
319-589 2.22e-14

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 73.57  E-value: 2.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVvcaealgMDSSRPDQTSIVAVKMLKDN-------ASDKDLADLISEMEMMKLI--GRHKNIINLLGVCT 389
Cdd:cd14004   6 KEMGEGAYGQV-------NLAIYKSKGKEVVIKFIFKErilvdtwVRDRKLGTVPLEIHILDTLnkRSHPNIVKLLDFFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGnLREFLRARRPPGPDlspdgprSSEGPLSFpalvscaYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd14004  79 DDEFYYLVMEKHGSG-MDLFDFIERKPNMD-------EKEAKYIF-------RQVADAVKHLHDQGIVHRDIKDENVILD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLARgvhhidYYK--KTSNGRLPVKWMAPEALFDRVYTHQS-DVWSFGILLWEIFtLGGSPYpgIPVEEL 546
Cdd:cd14004 144 GNGTIKLIDFGSAA------YIKsgPFDTFVGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLV-FKENPF--YNIEEI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   547 FSllreghRMERPPNCPS-ELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14004 215 LE------ADLRIPYAVSeDLIDLISRMLNRDVGDRPTIEELLT 252
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
317-550 2.27e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 73.89  E-value: 2.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKpLGEGCFGQVVcaealgmdSSRPDQT-SIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd07871  10 LDK-LGEGTYATVF--------KGRSKLTeNLVALKEIRLEHEEGAPCTAIREVSLLKNL-KHANIVTLHDIIHTERCLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAaKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd07871  80 LVFEYL-DSDLKQYLD---------------NCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   476 IADFGLARGVHHIDyyKKTSNGRLPVKWMAPEALFDRV-YTHQSDVWSFGILLWEIFTlgGSP-YPGIPVEELFSLL 550
Cdd:cd07871 144 LADFGLARAKSVPT--KTYSNEVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMAT--GRPmFPGSTVKEELHLI 216
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
394-589 3.36e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 73.37  E-value: 3.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSFpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14048  90 LYIQMQLCRKENLKDWMNRRC-----------TMESRELFV--CLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDV 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLargVHHID--------------YYKKTsnGRLPVK-WMAPEALFDRVYTHQSDVWSFGILLWEIFtlggspY 538
Cdd:cd14048 157 VKVGDFGL---VTAMDqgepeqtvltpmpaYAKHT--GQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELI------Y 225
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   539 PGIPVEELFSLLREGHRMERPP----NCPSElYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14048 226 SFSTQMERIRTLTDVRKLKFPAlftnKYPEE-RDMVQQMLSPSPSERPEAHEVIE 279
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
319-538 3.95e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 73.86  E-value: 3.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    319 KPLGEGCFGQVVCAealgmdSSRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:PTZ00426  36 RTLGTGSFGRVILA------TYKNEDFPPVAIKRFEKSKiiKQKQVDHVFSERKILNYI-NHPFCVNLYGSFKDESYLYL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    397 IVEYAAKGNLREFLRARRppgpdlspdgprssegplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:PTZ00426 109 VLEFVIGGEFFTFLRRNK------------------RFPNDVGCFYaaQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFI 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138    475 KIADFGLARGVHHIDYykkTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPY 538
Cdd:PTZ00426 171 KMTDFGFAKVVDTRTY---TLCG--TPEYIAPEILLNVGHGKAADWWTLGIFIYEIL-VGCPPF 228
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
319-552 4.76e-14

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 73.68  E-value: 4.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDE-------VYAIKVLKKDVilQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLR-EFLRARRPpgpdlspDGPRSSegplSFPALVSCAyqvargMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd05591  74 VMEYVNGGDLMfQIQRARKF-------DEPRAR----FYAAEVTLA------LMFLHRHGVIYRDLKLDNILLDAEGHCK 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   476 IADFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELF-SLLRE 552
Cdd:cd05591 137 LADFGMCK--EGILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFeSILHD 211
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
319-586 4.92e-14

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 72.69  E-value: 4.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAealGMDSSRPdqtsiVAVK-MLKDNAS--DKDLADLISEMEmmkligrHKNIINLLGVCTQEGPLY 395
Cdd:cd13982   7 KVLGYGSEGTIVFR---GTFDGRP-----VAVKrLLPEFFDfaDREVQLLRESDE-------HPNVIRYFCTEKDRQFLY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAkGNLREFLRarrppGPDLSPDGPRSSegplsfPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV-- 473
Cdd:cd13982  72 IALELCA-ASLQDLVE-----SPRESKLFLRPG------LEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAhg 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 ---MKIADFGLAR----GVHHidyYKKTSNGRLPVKWMAPEALFDRVYTHQS---DVWSFGILLWEIFTLGGSPYPGIPV 543
Cdd:cd13982 140 nvrAMISDFGLCKkldvGRSS---FSRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGSHPFGDKLE 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   544 EE---------LFSLLREGHrmerppnCPSELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd13982 217 REanilkgkysLDKLLSLGE-------HGPEAQDLIERMIDFDPEKRPSAEE 261
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
348-538 5.32e-14

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 72.26  E-value: 5.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLKDN-ASDKDLADLISEMEMMKLIgRHKNIINLLG--VCTQEGPLYVIVEYAAKGNLREFLRarRPPGPDLspdg 424
Cdd:cd13983  29 VAWNEIKLRkLPKAERQRFKQEIEILKSL-KHPNIIKFYDswESKSKKEVIFITELMTSGTLKQYLK--RFKRLKL---- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   425 prssegplsfPALVSCAYQVARGMQYLESRK--CIHRDLAARNVLVT-EDDVMKIADFGLARGVHHidYYKKTSNGRLpv 501
Cdd:cd13983 102 ----------KVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQ--SFAKSVIGTP-- 167
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 204138   502 KWMAPEaLFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd13983 168 EFMAPE-MYEEHYDEKVDIYAFGMCLLEMAT-GEYPY 202
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
321-525 5.44e-14

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 72.48  E-value: 5.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdssRPDQTS-IVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd06607   9 IGHGSFGAVYYA--------RNKRTSeVVAIKKMSYSGkqSTEKWQDIIKEVKFLRQL-RHPNTIEYKGCYLREHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAkGNLREFLRARRPPgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd06607  80 MEYCL-GSASDIVEVHKKP---------------LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLA 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 204138   478 DFGLARGVHHIDYYKKTsngrlPVkWMAPE---ALFDRVYTHQSDVWSFGI 525
Cdd:cd06607 144 DFGSASLVCPANSFVGT-----PY-WMAPEvilAMDEGQYDGKVDVWSLGI 188
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
7-87 5.64e-14

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 67.42  E-value: 5.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     7 AVPAGNTVKFRCPAAGNPMPTIHWLKNGqafhGENRIGGIRLRHQHwSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLD 86
Cdd:cd05725   8 VVLVDDSAEFQCEVGGDPVPTVRWRKED----GELPKGRYEILDDH-SLKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82

                .
gi 204138    87 V 87
Cdd:cd05725  83 V 83
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
314-540 6.74e-14

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 72.54  E-value: 6.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEALgmdssrpDQTSIVAVK-MLKD----NasdkdladliSEMEMMKLIgRHKNIINLLGVC 388
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLL-------ETGEVVAIKkVLQDkrykN----------RELQIMRRL-KHPNIVKLKYFF 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   389 -TQEGP-----LYVIVEYAAKgNL----REFLRARRPPgpdlspdgprssegPLSFPALVScaYQVARGMQYLESRKCIH 458
Cdd:cd14137  67 ySSGEKkdevyLNLVMEYMPE-TLyrviRHYSKNKQTI--------------PIIYVKLYS--YQLFRGLAYLHSLGICH 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   459 RDLAARNVLVTEDD-VMKIADFG----LARG---VHHI--DYYKktsngrlpvkwmAPEALFD-RVYTHQSDVWSFGILL 527
Cdd:cd14137 130 RDIKPQNLLVDPETgVLKLCDFGsakrLVPGepnVSYIcsRYYR------------APELIFGaTDYTTAIDIWSAGCVL 197
                       250
                ....*....|....
gi 204138   528 WEIFTlgGSP-YPG 540
Cdd:cd14137 198 AELLL--GQPlFPG 209
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
14-77 7.28e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 66.58  E-value: 7.28e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138    14 VKFRCPAAGNPMPTIHWLKNGQAFhGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPL-PPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
314-591 1.06e-13

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 71.77  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEALGMDSSrpdqtsiVAVKMLKDNASDKDLAdLISEMEMMKLIGRHKNIINLLGVCT---- 389
Cdd:cd14036   1 KLRIKRVIAEGGFAFVYEAQDVGTGKE-------YALKRLLSNEEEKNKA-IIQEINFMKKLSGHPNIVQFCSAASigke 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 ---QEGPLYVIVEYAAKGNLREFLRARRPPGPdLSPDgprssegplsfpALVSCAYQVARGMQYLESRK--CIHRDLAAR 464
Cdd:cd14036  73 esdQGQAEYLLLTELCKGQLVDFVKKVEAPGP-FSPD------------TVLKIFYQTCRAVQHMHKQSppIIHRDLKIE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   465 NVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRLPVK----------WMAPEALfdRVY-----THQSDVWSFGILLWE 529
Cdd:cd14036 140 NLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEdeitrnttpmYRTPEMI--DLYsnypiGEKQDIWALGCILYL 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138   530 IFtlggspYPGIPVEELFSLLREGHRMERPPNcPSE---LYGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd14036 218 LC------FRKHPFEDGAKLRIINAKYTIPPN-DTQytvFHDLIRSTLKVNPEERLSITEIVEQL 275
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
314-594 1.20e-13

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 71.58  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   314 RLVLGKPLGEGCFGQVVCAEALGMdssrpdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEgP 393
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHGE----------VAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSP-P 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGnlREFLRARRPPGPDLSPDGPRSsegplsfpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14153  70 HLAIITSLCKG--RTLYSVVRDAKVVLDVNKTRQ------------IAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MkIADFGLARGVHHIDYYKKTSNGRLPVKW-----------MAPEALFDRV-YTHQSDVWSFGILLWEIFTLGGsPYPGI 541
Cdd:cd14153 136 V-ITDFGLFTISGVLQAGRREDKLRIQSGWlchlapeiirqLSPETEEDKLpFSKHSDVFAFGTIWYELHAREW-PFKTQ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   542 PVEELFSLLREGHRmerpPNCPS-----ELYGLMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14153 214 PAEAIIWQVGSGMK----PNLSQigmgkEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
311-589 1.27e-13

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 72.06  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVCAealgMDSSRPDQTSIVAVKMlkDNASDKDLadLISEMEMMKLiGRHKNIINLLGVCTQ 390
Cdd:cd06656  17 PKKKYTRFEKIGQGASGTVYTA----IDIATGQEVAIKQMNL--QQQPKKEL--IINEILVMRE-NKNPNIVNYLDSYLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06656  88 GDELWVVMEYLAGGSLTDVV-----------------TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGI-PVEELFSL 549
Cdd:cd06656 151 DGSVKLTDFGFCAQITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNEnPLRALYLI 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   550 LREGH-RMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06656 228 ATNGTpELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQ 268
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
442-588 1.32e-13

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 71.58  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESR-KCIHRDLAARNVLVTEDDVMKIADFGLARGVHH---IDYYKKTSNGRLPV------KWMAPEALFD 511
Cdd:cd14011 121 LQISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCISSEQatdQFPYFREYDPNLPPlaqpnlNYLAPEYILS 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   512 RVYTHQSDVWSFGILLWEIFTLGGSPY-PGIPVEELFSLLREGHRMERPP--NCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd14011 201 KTCDPASDMFSLGVLIYAIYNKGKPLFdCVNNLLSYKKNSNQLRQLSLSLleKVPEELRDHVKTLLNVTPEVRPDAEQLS 280
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
321-530 1.43e-13

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 71.64  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgMDSSRPDQTSIVAVKM--LKDNASDKDLADLISEMEMmkligRHKNIINLL-----GVCTQEgP 393
Cdd:cd14055   3 VGKGRFAEVWKAK---LKQNASGQYETVAVKIfpYEEYASWKNEKDIFTDASL-----KHENILQFLtaeerGVGLDR-Q 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARrppgpdlspdgprssegPLSFPALVSCAYQVARGMQYLESRK---------CIHRDLAAR 464
Cdd:cd14055  74 YWLITAYHENGSLQDYLTRH-----------------ILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSS 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138   465 NVLVTEDDVMKIADFGLARGVH---HIDYYKKTSNGRLPvKWMAPEALFDRVYTH------QSDVWSFGILLWEI 530
Cdd:cd14055 137 NILVKNDGTCVLADFGLALRLDpslSVDELANSGQVGTA-RYMAPEALESRVNLEdlesfkQIDVYSMALVLWEM 210
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
320-591 1.50e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 71.37  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   320 PLGEGCFGQVVCAEalgmdsSRPDQtSIVAVKMLKDNASD-----KDLADLisememmkligRHKNIINLLgvCTQEGP- 393
Cdd:cd14047  13 LIGSGGFGQVFKAK------HRIDG-KTYAIKRVKLNNEKaerevKALAKL-----------DHPNIVRYN--GCWDGFd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 -----------------LYVIVEYAAKGNLREFLRARRppGPDLSPdgprssegplsFPALVsCAYQVARGMQYLESRKC 456
Cdd:cd14047  73 ydpetsssnssrsktkcLFIQMEFCEKGTLESWIEKRN--GEKLDK-----------VLALE-IFEQITKGVEYIHSKKL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   457 IHRDLAARNVLVTEDDVMKIADFGLargVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGS 536
Cdd:cd14047 139 IHRDLKPSNIFLVDTGKVKIGDFGL---VTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDS 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   537 pypGIPVEELFSLLREGhrmERPPN----CPSELyGLMRECWHAAPSQRPTFKQLVEAL 591
Cdd:cd14047 216 ---AFEKSKFWTDLRNG---ILPDIfdkrYKIEK-TIIKKMLSKKPEDRPNASEILRTL 267
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
319-589 1.62e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 71.59  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd06634  21 REIGHGSFGAVYFARDV-------RNNEVVAIKKMSYSGkqSNEKWQDIIKEVKFLQKL-RHPNTIEYRGCYLREHTAWL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAkGNLREFLRARRPPGPDLSpdgprssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd06634  93 VMEYCL-GSASDLLEVHKKPLQEVE---------------IAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVHHIDYYKKTSngrlpvKWMAPE---ALFDRVYTHQSDVWSFGILLWEIftlgGSPYPGIPVEELFSLLREG 553
Cdd:cd06634 157 GDFGSASIMAPANSFVGTP------YWMAPEvilAMDEGQYDGKVDVWSLGITCIEL----AERKPPLFNMNAMSALYHI 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 204138   554 HRMERP---PNCPSELY-GLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06634 227 AQNESPalqSGHWSEYFrNFVDSCLQKIPQDRPTSDVLLK 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
315-547 1.76e-13

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 70.84  E-value: 1.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   315 LVLGKPLGEGCFGqVVCaealgmdSSRPDQTSI-VAVKMLKDNASDKD-LADLISEMEMMKLIGRHKNIINLLGVCTQEG 392
Cdd:cd14106  10 TVESTPLGRGKFA-VVR-------KCIHKETGKeYAAKFLRKRRRGQDcRNEILHEIAVLELCKDCPRVVNLHEVYETRS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd14106  82 ELILILELAAGGELQTLL----------------DEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 V---MKIADFGLARGVHH----------IDYykktsngrlpvkwMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYP 539
Cdd:cd14106 146 PlgdIKLCDFGISRVIGEgeeireilgtPDY-------------VAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFG 211

                ....*...
gi 204138   540 GIPVEELF 547
Cdd:cd14106 212 GDDKQETF 219
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
319-611 1.90e-13

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 72.12  E-value: 1.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAealgMDSsRPDQTsiVAVK--MLKDNASDKDLadlISEMEMMKLIgRHKNIINL------------ 384
Cdd:cd07854  11 RPLGCGSNGLVFSA----VDS-DCDKR--VAVKkiVLTDPQSVKHA---LREIKIIRRL-DHDNIVKVyevlgpsgsdlt 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   385 --LGVCTQEGPLYVIVEYAaKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLA 462
Cdd:cd07854  80 edVGSLTELNSVYIVQEYM-ETDLANVL-----------------EQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   463 ARNVLV-TEDDVMKIADFGLARGVH-HIDYYKKTSNGrLPVKWM-APEALFD-RVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd07854 142 PANVFInTEDLVLKIGDFGLARIVDpHYSHKGYLSEG-LVTKWYrSPRLLLSpNNYTKAIDMWAAGCIFAEMLT-GKPLF 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   539 PGIPVEELFSLL-------REGHRMErppnCPSELYGLMREcwHAAPSQRPtfkqlveaLDKVLLAVSEEYLDLR---LT 608
Cdd:cd07854 220 AGAHELEQMQLIlesvpvvREEDRNE----LLNVIPSFVRN--DGGEPRRP--------LRDLLPGVNPEALDFLeqiLT 285

                ...
gi 204138   609 FGP 611
Cdd:cd07854 286 FNP 288
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
316-528 2.08e-13

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 70.98  E-value: 2.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   316 VLGKPLGEGCFGQVvcaeALG--MDSSRPDQTSIVAVKM-LKDNASDKD-LADLISEMEMMKLIGrHKNIINLLGVCTQE 391
Cdd:cd14076   4 ILGRTLGEGEFGKV----KLGwpLPKANHRSGVQVAIKLiRRDTQQENCqTSKIMREINILKGLT-HPNIVRLLDVLKTK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLRARRPPgpdlspdgpRSSEGPLSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVTED 471
Cdd:cd14076  79 KYIGIVLEFVSGGELFDYILARRRL---------KDSVACRLFAQLIS-------GVAYLHKKGVVHRDLKLENLLLDKN 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   472 DVMKIADFGLARGV-HHIDYYKKTSNGRlPVkWMAPE-ALFDRVYT-HQSDVWSFGILLW 528
Cdd:cd14076 143 RNLVITDFGFANTFdHFNGDLMSTSCGS-PC-YAAPElVVSDSMYAgRKADIWSCGVILY 200
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
441-591 2.51e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 71.44  E-value: 2.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDyykktSNGRLPV-------KWM-APEALF-D 511
Cdd:cd07852 113 MYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLE-----EDDENPVltdyvatRWYrAPEILLgS 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   512 RVYTHQSDVWSFGILLWEIftLGGSP-YPG---------I------PVEE-------------LFSLLREGHRM--ERPP 560
Cdd:cd07852 188 TRYTKGVDMWSVGCILGEM--LLGKPlFPGtstlnqlekIievigrPSAEdiesiqspfaatmLESLPPSRPKSldELFP 265
                       170       180       190
                ....*....|....*....|....*....|.
gi 204138   561 NCPSELYGLMRECWHAAPSQRPTfkqLVEAL 591
Cdd:cd07852 266 KASPDALDLLKKLLVFNPNKRLT---AEEAL 293
I-set pfam07679
Immunoglobulin I-set domain;
7-78 2.72e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 65.74  E-value: 2.72e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138       7 AVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIgGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGS 78
Cdd:pfam07679  11 EVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRF-KVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
321-550 2.95e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 71.18  E-value: 2.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd07872  14 LGEGTYATVFKGRSKLTEN-------LVALKEIRLEHEEGAPCTAIREVSLLKDL-KHANIVTLHDIVHTDKSLTLVFEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKgNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd07872  86 LDK-DLKQYMD---------------DCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 204138   481 LARGVhhiDYYKKTSNGRLPVKWMAPE--ALFDRVYTHQSDVWSFGILLWEIFTlgGSP-YPGIPVEELFSLL 550
Cdd:cd07872 150 LARAK---SVPTKTYSNEVVTLWYRPPdvLLGSSEYSTQIDMWGVGCIFFEMAS--GRPlFPGSTVEDELHLI 217
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
377-594 3.90e-13

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 70.45  E-value: 3.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   377 RHKNI-------INLLGVCTQegpLYVIVEYAAKGNLREFLRArrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQ 449
Cdd:cd14220  47 RHENIlgfiaadIKGTGSWTQ---LYLITDYHENGSLYDFLKC-----------------TTLDTRALLKLAYSAACGLC 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   450 YLESR--------KCIHRDLAARNVLVTEDDVMKIADFGLA----RGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQ 517
Cdd:cd14220 107 HLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPEVLDESLNKNH 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   518 ------SDVWSFGILLWEIF---TLGG-------SPYPGIPVEELFSLLREGHRME--RP--------PNCPSELYGLMR 571
Cdd:cd14220 185 fqayimADIYSFGLIIWEMArrcVTGGiveeyqlPYYDMVPSDPSYEDMREVVCVKrlRPtvsnrwnsDECLRAVLKLMS 264
                       250       260
                ....*....|....*....|...
gi 204138   572 ECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14220 265 ECWAHNPASRLTALRIKKTLAKM 287
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
378-538 6.10e-13

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 69.61  E-value: 6.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   378 HKNIINLLGVCT--QEGPLYVIVEYAAKGNLREFlrarrPPGPDLSPDGPRssegpLSFPALVscayqvaRGMQYLESRK 455
Cdd:cd14199  84 HPNVVKLVEVLDdpSEDHLYMVFELVKQGPVMEV-----PTLKPLSEDQAR-----FYFQDLI-------KGIEYLHYQK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   456 CIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFD--RVYTHQS-DVWSFGILLWeIFT 532
Cdd:cd14199 147 IIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGT-PA-FMAPETLSEtrKIFSGKAlDVWAMGVTLY-CFV 223

                ....*.
gi 204138   533 LGGSPY 538
Cdd:cd14199 224 FGQCPF 229
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
321-540 6.50e-13

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 69.22  E-value: 6.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALgmdssrpDQTSIVAVKMLKDNasdKDLADL-ISEMEMMKLIGRH-----KNIINLLGVCTQEGPL 394
Cdd:cd14133   7 LGKGTFGQVVKCYDL-------LTGEEVALKIIKNN---KDYLDQsLDEIRLLELLNKKdkadkYHIVRLKDVFYFKNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 yVIVEYAAKGNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD-- 472
Cdd:cd14133  77 -CIVFELLSQNLYEFLKQNKFQY--------------LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrc 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   473 VMKIADFGLARGVH-HIDYYKKTSNGRlpvkwmAPEALFDRVYTHQSDVWSFGILLWEIFTlgGSP-YPG 540
Cdd:cd14133 142 QIKIIDFGSSCFLTqRLYSYIQSRYYR------APEVILGLPYDEKIDMWSLGCILAELYT--GEPlFPG 203
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
319-587 6.63e-13

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 69.17  E-value: 6.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAealgMDSSRpdqtSIVAVKMLK-DNASDKDLADLISEMEMMKLIGRHKNIINLLG--VCTQEGPLY 395
Cdd:cd14131   7 KQLGKGGSSKVYKV----LNPKK----KIYALKRVDlEGADEQTLQSYKNEIELLKKLKGSDRIIQLYDyeVTDEDDYLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAaKGNLREFLRARRPpgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARN-VLVteDDVM 474
Cdd:cd14131  79 MVMECG-EIDLATILKKKRP--------------KPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLV--KGRL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGV--HHIDYYKKTSNGRLpvKWMAPEALFDRVYTHQ----------SDVWSFGILLWEiFTLGGSPYPGI- 541
Cdd:cd14131 142 KLIDFGIAKAIqnDTTSIVRDSQVGTL--NYMSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQ-MVYGKTPFQHIt 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 204138   542 -PVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14131 219 nPIAKLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPEL 265
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
321-532 6.79e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 69.37  E-value: 6.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaealgmdSSRPDQT-SIVAVKMLKDNASDKDL-ADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd07861   8 IGEGTYGVVY--------KGRNKKTgQIVAMKKIRLESEEEGVpSTAIREISLLKEL-QHPNIVCLEDVLMQENRLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKgNLREFLrarrppgpDLSPDGPRSSegplsfPALV-SCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd07861  79 EFLSM-DLKKYL--------DSLPKGKYMD------AELVkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLA 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   478 DFGLARGVHhidyykktsngrLPVK----------WMAPEALFDRV-YTHQSDVWSFGILLWEIFT 532
Cdd:cd07861 144 DFGLARAFG------------IPVRvythevvtlwYRAPEVLLGSPrYSTPVDIWSIGTIFAEMAT 197
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
396-588 7.45e-13

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 71.05  E-value: 7.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    396 VIVEYAAKGNLREFLRARRPPGPDLspdgpRSSEGPLSFpalvscaYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:PTZ00283 116 LVLDYANAGDLRQEIKSRAKTNRTF-----REHEAGLLF-------IQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    476 IADFGLARgvhhidYYKKTSNGRL-------PVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTLgGSPYPGIPVEELFS 548
Cdd:PTZ00283 184 LGDFGFSK------MYAATVSDDVgrtfcgtPY-YVAPEIWRRKPYSKKADMFSLGVLLYELLTL-KRPFDGENMEEVMH 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 204138    549 LLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:PTZ00283 256 KTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
321-538 7.68e-13

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 68.73  E-value: 7.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAL--GMDssrpdqtsiVAVKMLKDNASDKD--LADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd14186   9 LGKGSFACVYRARSLhtGLE---------VAIKMIDKKAMQKAgmVQRVRNEVEIHCQL-KHPSILELYNYFEDSNYVYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRPPgpdLSPDGPRSsegplsfpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd14186  79 VLEMCHNGEMSRYLKNRKKP---FTEDEARH------------FMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKI 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   477 ADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY 538
Cdd:cd14186 144 ADFGLATQLKMPHEKHFTMCG--TPNYISPEIATRSAHGLESDVWSLGCMFY-TLLVGRPPF 202
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
317-540 7.77e-13

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 69.28  E-value: 7.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVV-CAEalgmdSSRPDQTSIVAVKMLKDNASDKDLA--DLISEMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:cd14194   9 TGEELGSGQFAVVKkCRE-----KSTGLQYAAKFIKKRRTKSSRRGVSreDIEREVSILKEI-QHPNVITLHEVYENKTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpdlspdgPRSSEGPLSFpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14194  83 VILILELVAGGELFDFLAEKE----------SLTEEEATEF------LKQILNGVYYLHSLQIAHFDLKPENIMLLDRNV 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   474 ----MKIADFGLArgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPG 540
Cdd:cd14194 147 pkprIKIIDFGLA---HKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 213
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
435-589 8.70e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 69.14  E-value: 8.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   435 PALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVhhIDYYKKTSNGrlPVKWMAPEALFDRVY 514
Cdd:cd06619  95 HVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL--VNSIAKTYVG--TNAYMAPERISGEQY 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   515 THQSDVWSFGILLWEIfTLGGSPYPGI--------PVEELFSLLREGhrmerPPNCPSELYG-----LMRECWHAAPSQR 581
Cdd:cd06619 171 GIHSDVWSLGISFMEL-ALGRFPYPQIqknqgslmPLQLLQCIVDED-----PPVLPVGQFSekfvhFITQCMRKQPKER 244

                ....*...
gi 204138   582 PTFKQLVE 589
Cdd:cd06619 245 PAPENLMD 252
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
6-74 1.02e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 63.76  E-value: 1.02e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138       6 HAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAF-HGENRIGGIRLrhqhwSLVMESVVPSDRGTYTCLVEN 74
Cdd:pfam13927  11 VVVVEGETVTLTCEASGSPPPTITWYKNGGKLsSGRTSLVGGNG-----TLTISNVTREDSGTYTCTASN 75
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
319-529 1.27e-12

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 68.55  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVV-CAEALgmdSSRpdqtsIVAVKMLKDNASDKDLADLISEMEmmkLIGR--HKNIINLLGVCTQEGPLY 395
Cdd:cd14046  12 QVLGKGAFGQVVkVRNKL---DGR-----YYAIKKIKLRSESKNNSRILREVM---LLSRlnHQHVVRYYQAWIERANLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRArrppgpDLSPDGPRssegplsfpaLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd14046  81 IQMEYCEKSTLRDLIDS------GLFQDTDR----------LWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVK 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   476 IADFGLARGVH-----------HIDYYKKTSNGRLPVK-----WMAPEAL--FDRVYTHQSDVWSFGILLWE 529
Cdd:cd14046 145 IGDFGLATSNKlnvelatqdinKSTSAALGSSGDLTGNvgtalYVAPEVQsgTKSTYNEKVDMYSLGIIFFE 216
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
440-589 1.32e-12

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 68.40  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   440 CAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLAR----GVHHIDYYKKTSNGRLPVK---------WMAP 506
Cdd:cd05579  98 YIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvRRQIKLSIQKKSNGAPEKEdrrivgtpdYLAP 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   507 EALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELFSLLREGhRMERP--PNCPSELYGLMRECWHAAPSQRPTF 584
Cdd:cd05579 178 EILLGQGHGKTVDWWSLGVILYE-FLVGIPPFHAETPEEIFQNILNG-KIEWPedPEVSDEAKDLISKLLTPDPEKRLGA 255

                ....*
gi 204138   585 KQLVE 589
Cdd:cd05579 256 KGIEE 260
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
378-589 1.33e-12

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 68.54  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   378 HKNIINLLGVC--TQEGPLYVIVEYAAKGNLREFlrarrPPGPDLSPDGPRSSegplsFPALVscayqvaRGMQYLESRK 455
Cdd:cd14118  73 HPNVVKLVEVLddPNEDNLYMVFELVDKGAVMEV-----PTDNPLSEETARSY-----FRDIV-------LGIEYLHYQK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   456 CIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALF---DRVYTHQSDVWSFGILLWeIFT 532
Cdd:cd14118 136 IIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGT-PA-FMAPEALSesrKKFSGKALDIWAMGVTLY-CFV 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   533 LGGSPYPGIPVEELFSLLR-EGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14118 213 FGRCPFEDDHILGLHEKIKtDPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKE 270
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
319-540 1.42e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 69.37  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDSSrpdqtsiVAVKMLK---DNASDKDLAdlISEMEMMKLIgRHKNIINLLGVCTQEGPL- 394
Cdd:cd07850   6 KPIGSGAQGIVCAAYDTVTGQN-------VAIKKLSrpfQNVTHAKRA--YRELVLMKLV-NHKNIIGLLNVFTPQKSLe 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 -----YVIVEYAaKGNLREFLRArrppgpDLspDGPRssegpLSFpaLVscaYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd07850  76 efqdvYLVMELM-DANLCQVIQM------DL--DHER-----MSY--LL---YQMLCGIKHLHSAGIIHRDLKPSNIVVK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDVMKIADFGLAR--GVHHI-------DYYKktsngrlpvkwmAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPG 540
Cdd:cd07850 137 SDCTLKILDFGLARtaGTSFMmtpyvvtRYYR------------APEVILGMGYKENVDIWSVGCIMGEMI-RGTVLFPG 203
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
319-581 1.69e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 68.88  E-value: 1.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCA--EALGMdssrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd05595   1 KLLGKGTFGKVILVreKATGR---------YYAMKILRKEViiAKDEVAHTVTESRVLQNT-RHPFLTALKYAFQTHDRL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRPpgpdLSPDGPRSSegplsfpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd05595  71 CFVMEYANGGELFFHLSRERV----FTEDRARFY------------GAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHHIDYYKKTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSL-LREG 553
Cdd:cd05595 135 KITDFGLCKEGITDGATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELiLMEE 211
                       250       260       270
                ....*....|....*....|....*....|
gi 204138   554 HRMER--PPNCPSELYGLMREcwhaAPSQR 581
Cdd:cd05595 212 IRFPRtlSPEAKSLLAGLLKK----DPKQR 237
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
349-588 1.76e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 68.50  E-value: 1.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLkdnasDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLRE-FLRARRppgpdlspdgprS 427
Cdd:cd14178  32 AVKII-----DKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDrILRQKC------------F 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 SEGPLSfpaLVSCAyqVARGMQYLESRKCIHRDLAARNVLVTED----DVMKIADFGLARGVhhidyykKTSNGRL---- 499
Cdd:cd14178  95 SEREAS---AVLCT--ITKTVEYLHSQGVVHRDLKPSNILYMDEsgnpESIRICDFGFAKQL-------RAENGLLmtpc 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   500 -PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIP---VEELFSLLREGHRMERPPNCPS---ELYGLMRE 572
Cdd:cd14178 163 yTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFTPFANGPddtPEEILARIGSGKYALSGGNWDSisdAAKDIVSK 241
                       250
                ....*....|....*.
gi 204138   573 CWHAAPSQRPTFKQLV 588
Cdd:cd14178 242 MLHVDPHQRLTAPQVL 257
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
321-540 1.77e-12

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 67.68  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVV-CAE-ALGMDssrpdqtsiVAVKMLKDNASDKDLAdlISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14006   1 LGRGRFGVVKrCIEkATGRE---------FAAKFIPKRDKKKEAV--LREISILNQL-QHPRIIQLHEAYESPTELVLIL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE--DDVMKI 476
Cdd:cd14006  69 ELCSGGELLDRL----------------AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKI 132
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   477 ADFGLARGVHHiDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd14006 133 IDFGLARKLNP-GEELKEIFGTP--EFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLG 192
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
321-551 1.86e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 68.31  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    321 LGEGCFGQVVCAealgmdssRPDQTS-IVAVKMLKDNASDKDL-ADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:PLN00009  10 IGEGTYGVVYKA--------RDRVTNeTIALKKIRLEQEDEGVpSTAIREISLLKEM-QHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    399 EYAAKgNLREFLrarrppgpDLSPDGPRSsegplsfPALV-SCAYQVARGMQYLESRKCIHRDLAARNVLVT-EDDVMKI 476
Cdd:PLN00009  81 EYLDL-DLKKHM--------DSSPDFAKN-------PRLIkTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    477 ADFGLARGVHhidyykktsngrLPVK----------WMAPEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPG-IPV 543
Cdd:PLN00009 145 ADFGLARAFG------------IPVRtfthevvtlwYRAPEILLgSRHYSTPVDIWSVGCIFAEMVN--QKPlFPGdSEI 210

                 ....*...
gi 204138    544 EELFSLLR 551
Cdd:PLN00009 211 DELFKIFR 218
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
321-540 2.05e-12

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 67.64  E-value: 2.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV--VCaealgmdsSRPDQTSIVAVKMLKDNASDKDLADLI-SEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05572   1 LGVGGFGRVelVQ--------LKSKGRTFALKCVKKRHIVQTRQQEHIfSEKEILEEC-NSPFIVKLYRTFKDKKYLYML 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05572  72 MEYCLGGELWTILRDR----------------GLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLV 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLArgvhhidyyKKTSNGRL-------PvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd05572 136 DFGFA---------KKLGSGRKtwtfcgtP-EYVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFGG 194
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
321-532 2.11e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 68.29  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT---------- 389
Cdd:cd07864  15 IGEGTYGQVYKAK-------DKDTGELVALKKVRlDNEKEGFPITAIREIKILRQL-NHRSVVNLKEIVTdkqdaldfkk 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKgNLREFLRArrppgpdlspdgprsseGPLSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVL 467
Cdd:cd07864  87 DKGAFYLVFEYMDH-DLMGLLES-----------------GLVHFSEDHIKSFmkQLLEGLNYCHKKNFLHRDIKCSNIL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   468 VTEDDVMKIADFGLARgVHHIDYYKKTSNGRLPVKWMAPEALF-DRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd07864 149 LNNKGQIKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFT 213
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
318-588 2.35e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 67.80  E-value: 2.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQV-VCAEalgMDSSRpdQTSIVAVKMLKDNA-SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEG--P 393
Cdd:cd06651  12 GKLLGQGAFGRVyLCYD---VDTGR--ELAAKQVQFDPESPeTSKEVSALECEIQLLKNL-QHERIVQYYGCLRDRAekT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd06651  86 LTIFMEYMPGGSVKDQLKAY----------------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIdyyKKTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILLWEIFTlggSPYPGIPVEELFSL 549
Cdd:cd06651 150 VKLGDFGASKRLQTI---CMSGTGIRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT---EKPPWAEYEAMAAI 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 204138   550 LREGHRMERPPnCPSELYGLMRE---CWHAAPSQRPTFKQLV 588
Cdd:cd06651 224 FKIATQPTNPQ-LPSHISEHARDflgCIFVEARHRPSAEELL 264
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
319-581 2.98e-12

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 67.81  E-value: 2.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVvcaealgMDSSRPDQTSIVAVKML--KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd14209   7 KTLGTGSFGRV-------MLVRHKETGNYYAMKILdkQKVVKLKQVEHTLNEKRILQAI-NFPFLVKLEYSFKDNSNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd14209  79 VMEYVPGGEMFSHLRRIG-----------RFSEPHARF-----YAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARGVhhidyykktsNGR------LPvKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELFSLL 550
Cdd:cd14209 143 TDFGFAKRV----------KGRtwtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKI 210
                       250       260       270
                ....*....|....*....|....*....|.
gi 204138   551 REGhRMERPPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd14209 211 VSG-KVRFPSHFSSDLKDLLRNLLQVDLTKR 240
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
442-577 3.38e-12

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 68.23  E-value: 3.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARgVHHIDYYKKTSNGRLPVKWMAPEALF-DRVYTHQSDV 520
Cdd:cd07853 110 YQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR-VEEPDESKHMTQEVVTQYYRAPEILMgSRHYTSAVDI 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   521 WSFGILLWE-------------------IFTLGGSPypgiPVEELFS--------LLREGHrmeRPPNCPSeLYGLMREC 573
Cdd:cd07853 189 WSVGCIFAEllgrrilfqaqspiqqldlITDLLGTP----SLEAMRSacegarahILRGPH---KPPSLPV-LYTLSSQA 260

                ....
gi 204138   574 WHAA 577
Cdd:cd07853 261 THEA 264
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
321-547 3.51e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 68.01  E-value: 3.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdssrPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05590   3 LGKGSFGKVMLARL-------KESGRLYAVKVLKKDVilQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:cd05590  76 EFVNGGDLMFHIQKSR-----------RFDEARARF-----YAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLAD 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   479 FGLAR-GVHHidyYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELF 547
Cdd:cd05590 140 FGMCKeGIFN---GKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLF 205
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
358-595 3.53e-12

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 67.32  E-value: 3.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   358 SDKDLADLISEMEMMKLIgRHKNIINLLGVCT-QEGP----LYVIVEYAAKGNLREFLRARRPPGpdlspdgprsseGPL 432
Cdd:cd13986  37 SKEDVKEAMREIENYRLF-NHPNILRLLDSQIvKEAGgkkeVYLLLPYYKRGSLQDEIERRLVKG------------TFF 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   433 SFPALVSCAYQVARGMQYL---ESRKCIHRDLAARNVLVTEDDVMKIADFG-------LARGVHHIDYYKKTSNGRLPVK 502
Cdd:cd13986 104 PEDRILHIFLGICRGLKAMhepELVPYAHRDIKPGNVLLSEDDEPILMDLGsmnpariEIEGRREALALQDWAAEHCTMP 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   503 WMAPEaLFDrVYTHQ-----SDVWSFGILLWEIFtLGGSPYPGIpVEELFSL-LREGHRMERPPNCPS---ELYGLMREC 573
Cdd:cd13986 184 YRAPE-LFD-VKSHCtidekTDIWSLGCTLYALM-YGESPFERI-FQKGDSLaLAVLSGNYSFPDNSRyseELHQLVKSM 259
                       250       260
                ....*....|....*....|..
gi 204138   574 WHAAPSQRPTFKQLVEALDKVL 595
Cdd:cd13986 260 LVVNPAERPSIDDLLSRVHDLI 281
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
311-560 3.60e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 67.70  E-value: 3.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGqVVCAeALGMDSSRPdqtsiVAVKMLkDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd06659  19 PRQLLENYVKIGEGSTG-VVCI-AREKHSGRQ-----VAVKMM-DLRKQQRRELLFNEVVIMRDY-QHPNVVEMYKSYLV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLrarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06659  90 GEELWVLMEYLQGGALTDIV-----------------SQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHiDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY-PGIPVEELFSL 549
Cdd:cd06659 153 DGRVKLSDFGFCAQISK-DVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPYfSDSPVQAMKRL 229
                       250
                ....*....|.
gi 204138   550 lreghRMERPP 560
Cdd:cd06659 230 -----RDSPPP 235
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
319-547 3.66e-12

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 67.12  E-value: 3.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLK--DNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05611   2 KPISKGAFGSVYLAK-------KRSTGDYFAIKVLKksDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARrppgpdlspdgprsseGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05611  75 VMEYLNGGDCASLIKTL----------------GGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKL 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   477 ADFGLARGVhhidyYKKTSNGRL---PvKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELF 547
Cdd:cd05611 139 TDFGLSRNG-----LEKRHNKKFvgtP-DYLAPETILGVGDDKMSDWWSLGCVIFE-FLFGYPPFHAETPDAVF 205
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
312-587 3.72e-12

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 67.31  E-value: 3.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAealgmdssRPDQTSIVAV--KMLKDNasDKDLADLISEMEMMKLIGRHKNIINLLG--- 386
Cdd:cd14037   2 SHHVTIEKYLAEGGFAHVYLV--------KTSNGGNRAAlkRVYVND--EHDLNVCKREIEIMKRLSGHKNIVGYIDssa 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQEG--PLYVIVEYAAKGNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRK--CIHRDLA 462
Cdd:cd14037  72 NRSGNGvyEVLLLMEYCKGGGVIDLMNQRLQTG--------------LTESEILKIFCDVCEAVAAMHYLKppLIHRDLK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   463 ARNVLVTEDDVMKIADFGLA-------RGVHHIDYYKKTSNGRLPVKWMAPEaLFD----RVYTHQSDVWSFGILLWEI- 530
Cdd:cd14037 138 VENVLISDSGNYKLCDFGSAttkilppQTKQGVTYVEEDIKKYTTLQYRAPE-MIDlyrgKPITEKSDIWALGCLLYKLc 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   531 -FTLggspypgiPVEELFSLLREGHRMERPPNCP--SELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd14037 217 fYTT--------PFEESGQLAILNGNFTFPDNSRysKRLHKLIRYMLEEDPEKRPNIYQV 268
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
8-87 4.07e-12

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 62.13  E-value: 4.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRiggiRLRHQ-HWSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLD 86
Cdd:cd20952  11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDE----RITTLeNGSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLD 86

                .
gi 204138    87 V 87
Cdd:cd20952  87 V 87
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
321-530 4.13e-12

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 67.78  E-value: 4.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGqVVCAealGMDSSRPDQtsiVAVKMLKdNASDK-DLAD-LISEMEMMKLIgRHKNIINLLGVCTQEGPL---- 394
Cdd:cd07855  13 IGSGAYG-VVCS---AIDTKSGQK---VAIKKIP-NAFDVvTTAKrTLRELKILRHF-KHDNIIAIRDILRPKVPYadfk 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 --YVIVEYAaKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd07855  84 dvYVVLDLM-ESDLHHIIH----------------SDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENC 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   473 VMKIADFGLARGV-----HHIDY---YKKTsngrlpvKWM-APEALF--DRvYTHQSDVWSFGILLWEI 530
Cdd:cd07855 147 ELKIGDFGMARGLctspeEHKYFmteYVAT-------RWYrAPELMLslPE-YTQAIDMWSVGCIFAEM 207
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
348-540 4.24e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 69.05  E-value: 4.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    348 VAVKMLKDN-ASDKDL-----------ADLIsememmkligrHKNIINLLGVcTQEGPLYVIV-EYAAKGNLREFLRarr 414
Cdd:NF033483  35 VAVKVLRPDlARDPEFvarfrreaqsaASLS-----------HPNIVSVYDV-GEDGGIPYIVmEYVDGRTLKDYIR--- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    415 ppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLAR----------- 483
Cdd:NF033483 100 -------------EHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARalssttmtqtn 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138    484 ---G-VHhidYykktsngrlpvkwMAPE-ALFDRVyTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:NF033483 167 svlGtVH---Y-------------LSPEqARGGTV-DARSDIYSLGIVLYEMLT-GRPPFDG 210
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
349-553 4.31e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 67.35  E-value: 4.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLkdnasDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLRE-FLRARRppgpdlspdgprS 427
Cdd:cd14177  33 AVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDrILRQKF------------F 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 SEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTED----DVMKIADFGLARGVhhidyykKTSNGRL---- 499
Cdd:cd14177  96 SEREAS-----AVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDsanaDSIRICDFGFAKQL-------RGENGLLltpc 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   500 -PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY---PGIPVEELfsLLREG 553
Cdd:cd14177 164 yTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFangPNDTPEEI--LLRIG 218
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
349-547 4.39e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 66.87  E-value: 4.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLKDNASDKDL-ADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGnlrEFLRARRPPGPDLSPDGprs 427
Cdd:cd14198  37 AAKFLKKRRRGQDCrAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAGG---EIFNLCVPDLAEMVSEN--- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 segplsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE----DDVmKIADFGLARGVHHIDYYKKTSNgrlPVKW 503
Cdd:cd14198 111 --------DIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiyplGDI-KIVDFGMSRKIGHACELREIMG---TPEY 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 204138   504 MAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELF 547
Cdd:cd14198 179 LAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQETF 221
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
349-589 5.08e-12

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 66.89  E-value: 5.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLkdnasDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprss 428
Cdd:cd14091  29 AVKII-----DKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGELLDRILRQK-------------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   429 egplSFPALVSCA--YQVARGMQYLESRKCIHRDLAARNVLVTED----DVMKIADFGLARGVHHidyykktSNGRL--P 500
Cdd:cd14091  90 ----FFSEREASAvmKTLTKTVEYLHSQGVVHRDLKPSNILYADEsgdpESLRICDFGFAKQLRA-------ENGLLmtP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   501 ---VKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY---PGIPVEELFSLLREGHRMERPPN---CPSELYGLMR 571
Cdd:cd14091 159 cytANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPFasgPNDTPEVILARIGSGKIDLSGGNwdhVSDSAKDLVR 237
                       250
                ....*....|....*...
gi 204138   572 ECWHAAPSQRPTFKQLVE 589
Cdd:cd14091 238 KMLHVDPSQRPTAAQVLQ 255
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
320-532 5.43e-12

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 67.25  E-value: 5.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   320 PLGEGCFGQVVCAEalgmDSSRPDQTsiVAVKMLKDNASDKDLADLisEMEMMKLIGRH-----KNIINLLGVCTQEGPL 394
Cdd:cd14135   7 YLGKGVFSNVVRAR----DLARGNQE--VAIKIIRNNELMHKAGLK--ELEILKKLNDAdpddkKHCIRLLRHFEHKNHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAkGNLREFLRARrppGPDLSpdgprssegpLSFPALVSCAYQVARGMQYLesRKC--IHRDLAARNVLVTED- 471
Cdd:cd14135  79 CLVFESLS-MNLREVLKKY---GKNVG----------LNIKAVRSYAQQLFLALKHL--KKCniLHADIKPDNILVNEKk 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   472 DVMKIADFGLARGVHHID--------YYKktsngrlpvkwmAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd14135 143 NTLKLCDFGSASDIGENEitpylvsrFYR------------APEIILGLPYDYPIDMWSVGCTLYELYT 199
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
366-587 5.57e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 66.29  E-value: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   366 ISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspDGPRSSEGPLSFPAlvscayQVA 445
Cdd:cd08220  47 LNEVKVLSML-HHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYIQQRK--------GSLLSEEEILHFFV------QIL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   446 RGMQYLESRKCIHRDLAARNVLVTED-DVMKIADFGLARgvhhIDYYKKTSNGRLPVK-WMAPEALFDRVYTHQSDVWSF 523
Cdd:cd08220 112 LALHHVHSKQILHRDLKTQNILLNKKrTVVKIGDFGISK----ILSSKSKAYTVVGTPcYISPELCEGKPYNQKSDIWAL 187
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   524 GILLWEIFTLGGSpYPGIPVEELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd08220 188 GCVLYELASLKRA-FEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEI 250
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
319-537 6.89e-12

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 66.69  E-value: 6.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVV-CAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMemmkligRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd05612   7 KTIGTGTFGRVHlVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEV-------SHPFIIRLFWTEHDQRFLYML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARrppgpdlspdGPRSSEGPLSFPALVSCAyqvargMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05612  80 MEYVPGGELFSYLRNS----------GRFSNSTGLFYASEIVCA------LEYLHSKEIVYRDLKPENILLDKEGHIKLT 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYykkTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEIftLGGSP 537
Cdd:cd05612 144 DFGFAKKLRDRTW---TLCGT-P-EYLAPEVIQSKGHNKAVDWWALGILIYEM--LVGYP 196
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
321-552 7.80e-12

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 66.32  E-value: 7.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSSrpdqtsiVAVKM--LKDNASDKDLADLISEMEMMKLIgRHKNIIN-------LLGVCTQE 391
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEY-------VAIKKcrQELSPSDKNRERWCLEVQIMKKL-NHPNVVSardvppeLEKLSPND 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLyVIVEYAAKGNLREFLrarrppgpdlspDGPRSSEGPLSFPALvSCAYQVARGMQYLESRKCIHRDLAARNVLVTE- 470
Cdd:cd13989  73 LPL-LAMEYCSGGDLRKVL------------NQPENCCGLKESEVR-TLLSDISSAISYLHENRIIHRDLKPENIVLQQg 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 --DDVMKIADFGlargvhhidYYKKTSNGRL------PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY-PGI 541
Cdd:cd13989 139 ggRVIYKLIDLG---------YAKELDQGSLctsfvgTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPFlPNW 208
                       250
                ....*....|.
gi 204138   542 PVEELFSLLRE 552
Cdd:cd13989 209 QPVQWHGKVKQ 219
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
349-589 8.38e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 67.16  E-value: 8.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    349 AVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLreflrarrppgpdlspDGPRSS 428
Cdd:PLN00034 103 ALKVIYGNHEDTVRRQICREIEILRDV-NHPNVVKCHDMFDHNGEIQVLLEFMDGGSL----------------EGTHIA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    429 EGPlsfpALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEA 508
Cdd:PLN00034 166 DEQ----FLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVG--TIAYMSPER 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    509 ----LFDRVYT-HQSDVWSFGILLWEiFTLGGSPypgipveelFSLLREGHR--------MERPPNCPS----ELYGLMR 571
Cdd:PLN00034 240 intdLNHGAYDgYAGDIWSLGVSILE-FYLGRFP---------FGVGRQGDWaslmcaicMSQPPEAPAtasrEFRHFIS 309
                        250
                 ....*....|....*...
gi 204138    572 ECWHAAPSQRPTFKQLVE 589
Cdd:PLN00034 310 CCLQREPAKRWSAMQLLQ 327
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
321-540 9.83e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 65.71  E-value: 9.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV-VCAE-ALGMDssrpdqtsiVAVKML-KDNASDKDLAdlISEMEMMKLIGrHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14190  12 LGGGKFGKVhTCTEkRTGLK---------LAAKVInKQNSKDKEMV--LLEIQVMNQLN-HRNLIQLYEAIETPNEIVLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLrarrppgpdLSPDGPRSSEGPLSFpalvscAYQVARGMQYLESRKCIHRDLAARNVLV--TEDDVMK 475
Cdd:cd14190  80 MEYVEGGELFERI---------VDEDYHLTEVDAMVF------VRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVK 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   476 IADFGLARgvhhidyyKKTSNGRLPVKWMAPEAL------FDRVyTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd14190 145 IIDFGLAR--------RYNPREKLKVNFGTPEFLspevvnYDQV-SFPTDMWSMGVITYMLLS-GLSPFLG 205
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
321-529 9.89e-12

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 66.09  E-value: 9.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINL------LGVCTQEGPL 394
Cdd:cd14039   1 LGTGGFGNVCLYQ-------NQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKL-NHPNVVKAcdvpeeMNFLVNDVPL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 yVIVEYAAKGNLREFLrarrppgpdlspDGPRSSEGpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD-- 472
Cdd:cd14039  73 -LAMEYCSGGDLRKLL------------NKPENCCG-LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgk 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   473 -VMKIADFGlargvhhidYYKKTSNGRL------PVKWMAPEALFDRVYTHQSDVWSFGILLWE 529
Cdd:cd14039 139 iVHKIIDLG---------YAKDLDQGSLctsfvgTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
367-554 1.05e-11

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 65.42  E-value: 1.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   367 SEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLR-ARRPPGPDLSpdgprssegplsfpALVSCayqVA 445
Cdd:cd14095  47 NEVAILRRV-KHPNIVQLIEEYDTDTELYLVMELVKGGDLFDAITsSTKFTERDAS--------------RMVTD---LA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   446 RGMQYLESRKCIHRDLAARNVLVTEDD----VMKIADFGLARGVHHIDYykkTSNGRlPVkWMAPEALFDRVYTHQSDVW 521
Cdd:cd14095 109 QALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKEPLF---TVCGT-PT-YVAPEILAETGYGLKVDIW 183
                       170       180       190
                ....*....|....*....|....*....|....*
gi 204138   522 SFGILLWeIFTLGGSPY--PGIPVEELFSLLREGH 554
Cdd:cd14095 184 AAGVITY-ILLCGFPPFrsPDRDQEELFDLILAGE 217
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
349-542 1.18e-11

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 66.58  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLkdnasDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLRE-FLRARRppgpdlspdgprS 427
Cdd:cd14176  48 AVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQKF------------F 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 SEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTED----DVMKIADFGLARGVhhidyykKTSNGRL---- 499
Cdd:cd14176 111 SEREAS-----AVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQL-------RAENGLLmtpc 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 204138   500 -PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIP 542
Cdd:cd14176 179 yTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFANGP 221
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
348-591 1.18e-11

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 65.70  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKMLkdNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprs 427
Cdd:cd05076  46 VVLKVL--DPSHHDIALAFFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEK------------- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   428 SEGPLSFPALVscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV-------MKIADFGLARGVhhidYYKKTSNGRLP 500
Cdd:cd05076 111 GHVPMAWKFVV--ARQLASALSYLENKNLVHGNVCAKNILLARLGLeegtspfIKLSDPGVGLGV----LSREERVERIP 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   501 vkWMAPEALFD-RVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMERpPNCPsELYGLMRECWHAAPS 579
Cdd:cd05076 185 --WIAPECVPGgNSLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLPE-PSCP-ELATLISQCLTYEPT 260
                       250
                ....*....|..
gi 204138   580 QRPTFKQLVEAL 591
Cdd:cd05076 261 QRPSFRTILRDL 272
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
320-616 1.20e-11

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 65.87  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   320 PLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd07844   7 KLGEGSYATVYKGRSKLTGQ-------LVALKEIRLEHEEGAPFTAIREASLLKDL-KHANIVTLHDIIHTKKTLTLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKgNLREFLRaRRPPGpdLSPDGPRSsegplsFpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADF 479
Cdd:cd07844  79 YLDT-DLKQYMD-DCGGG--LSMHNVRL------F------LFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   480 GLARGvhhidyyK----KT-SNGRLPVKWMAPEALF-DRVYTHQSDVWSFGILLWEIFTlgGSP-YPGI--PVEELfsll 550
Cdd:cd07844 143 GLARA-------KsvpsKTySNEVVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMAT--GRPlFPGStdVEDQL---- 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   551 regHRMERPPNCPSElyglmrECWHAAPSqRPTFKQL------VEALDKVL--LAVSEEYLDLRLTFGPYSPNN 616
Cdd:cd07844 210 ---HKIFRVLGTPTE------ETWPGVSS-NPEFKPYsfpfypPRPLINHAprLDRIPHGEELALKFLQYEPKK 273
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
321-540 1.26e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 66.34  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGqVVCAealGMDSSRPDQTSIVAVKMLKDNASDKdlADLISEMEMMKLIgRHKNIINLLGVCTQEGP-----LY 395
Cdd:cd07859   8 IGKGSYG-VVCS---AIDTHTGEKVAIKKINDVFEHVSDA--TRILREIKLLRLL-RHPDIVEIKHIMLPPSRrefkdIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAaKGNLREFLRARrppgPDLSPDGPRSSegplsfpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMK 475
Cdd:cd07859  81 VVFELM-ESDLHQVIKAN----DDLTPEHHQFF------------LYQLLRALKYIHTANVFHRDLKPKNILANADCKLK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   476 IADFGLAR--------GVHHIDYykktsngrLPVKWM-APE---ALFDRvYTHQSDVWSFGILLWEIFTlgGSP-YPG 540
Cdd:cd07859 144 ICDFGLARvafndtptAIFWTDY--------VATRWYrAPElcgSFFSK-YTPAIDIWSIGCIFAEVLT--GKPlFPG 210
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
444-540 1.29e-11

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 65.36  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   444 VARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHhiDYYKKTS-NGRLPvkWMAPEALFDRVYTHQSDVWS 522
Cdd:cd05578 109 IVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLT--DGTLATStSGTKP--YMAPEVFMRAGYSFAVDWWS 184
                        90
                ....*....|....*...
gi 204138   523 FGILLWEiFTLGGSPYPG 540
Cdd:cd05578 185 LGVTAYE-MLRGKRPYEI 201
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
2-83 1.29e-11

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 61.06  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138       2 EKKLHAVPAGNTVKFRCPA-AGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIR 80
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81

                  ...
gi 204138      81 YSY 83
Cdd:pfam00047  82 LST 84
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
311-589 1.39e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 65.83  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGqVVCAealgmdSSRPDQTSIVAVKMLkDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQ 390
Cdd:cd06658  20 PREYLDSFIKIGEGSTG-IVCI------ATEKHTGKQVAVKKM-DLRKQQRRELLFNEVVIMRDY-HHENVVDMYNSYLV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd06658  91 GDELWVVMEFLEGGALTDIVTHTR-----------------MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHHiDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLL 550
Cdd:cd06658 154 DGRIKLSDFGFCAQVSK-EVPKRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFNEPPLQAMRRI 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 204138   551 REG--HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06658 231 RDNlpPRVKDSHKVSSVLRGFLDLMLVREPSQRATAQELLQ 271
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
317-588 1.48e-11

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 65.13  E-value: 1.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALGMDSSrpdqtsiVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd14074   7 LEETLGRGHFAVVKLARHVFTGEK-------VAVKVIdKTKLDDVSKAHLFQEVRCMKLV-QHPNVVRLYEVIDTQTKLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLrARRPPGpdLSPDGPRSsegplsfpalvscaY--QVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14074  79 LILELGDGGDMYDYI-MKHENG--LNEDLARK--------------YfrQIVSAISYCHKLHVVHRDLKPENVVFFEKQG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 M-KIADFGLARgvHHIDYYK-KTSNGRLpvKWMAPEALFDRVYTHQS-DVWSFGILLWeIFTLGGSPYPGIPVEELFSLL 550
Cdd:cd14074 142 LvKLTDFGFSN--KFQPGEKlETSCGSL--AYSAPEILLGDEYDAPAvDIWSLGVILY-MLVCGQPPFQEANDSETLTMI 216
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 204138   551 REGhRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd14074 217 MDC-KYTVPAHVSPECKDLIRRMLIRDPKKRASLEEIE 253
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
319-540 1.81e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 65.85  E-value: 1.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqVVCAeALGMDSSRPdqtsiVAVKMLKdNASD--KDLADLISEMEMMKLIgRHKNIINLLGVCTQEG---- 392
Cdd:cd07858  11 KPIGRGAYG-IVCS-AKNSETNEK-----VAIKKIA-NAFDnrIDAKRTLREIKLLRHL-DHENVIAIKDIMPPPHreaf 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 -PLYVIVEYAaKGNLREFLRARRPpgpdLSPDgprssegplsfpalvSCAY---QVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd07858  82 nDVYIVYELM-DTDLHQIIRSSQT----LSDD---------------HCQYflyQLLRGLKYIHSANVLHRDLKPSNLLL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDVMKIADFGLARgvhhidyykkTSNGR-------LPVKWM-APEALFD-RVYTHQSDVWSFGILLWEIftLGGSP-Y 538
Cdd:cd07858 142 NANCDLKICDFGLAR----------TTSEKgdfmteyVVTRWYrAPELLLNcSEYTTAIDVWSVGCIFAEL--LGRKPlF 209

                ..
gi 204138   539 PG 540
Cdd:cd07858 210 PG 211
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
321-552 2.07e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 65.26  E-value: 2.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgMDSSRPdqtSIVAVKMLKDNASDKDLAdlISEMEMMKLIGRHK-----NIINLLGVCTQEGPLY 395
Cdd:cd14210  21 LGKGSFGQVVKC----LDHKTG---QLVAIKIIRNKKRFHQQA--LVEVKILKHLNDNDpddkhNIVRYKDSFIFRGHLC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKgNLREFLRARRPPGpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM- 474
Cdd:cd14210  92 IVFELLSI-NLYELLKSNNFQG--------------LSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSs 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 -KIADFGLARGVHHIDY-------YKktsngrlpvkwmAPEALFDRVYTHQSDVWSFGILLWEIFTlgGSP-YPGIPVEE 545
Cdd:cd14210 157 iKVIDFGSSCFEGEKVYtyiqsrfYR------------APEVILGLPYDTAIDMWSLGCILAELYT--GYPlFPGENEEE 222

                ....*..
gi 204138   546 LFSLLRE 552
Cdd:cd14210 223 QLACIME 229
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
377-591 2.17e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 64.65  E-value: 2.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   377 RHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLESRKC 456
Cdd:cd13995  54 RHENIAELYGALLWEETVHLFMEAGEGGSVLEKLE----------------SCGPMREFEIIWVTKHVLKGLDFLHSKNI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   457 IHRDLAARNVLVTEDDVMkIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLweIFTLGGS 536
Cdd:cd13995 118 IHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRG--TEIYMSPEVILCRGHNTKADIYSLGATI--IHMQTGS 192
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   537 PyPGI---PVEELFSLLREGHRmERPP--NCPSELYGLMRECWHAA----PSQRPTFKQLV--EAL 591
Cdd:cd13995 193 P-PWVrryPRSAYPSYLYIIHK-QAPPleDIAQDCSPAMRELLEAAlernPNHRSSAAELLkhEAL 256
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
308-589 2.59e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 64.69  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   308 WEFPRDRLV-LGKpLGEGCFGQVvcAEALGMDSSRpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIGRHKNIINLLG 386
Cdd:cd06616   1 YEFTAEDLKdLGE-IGRGAFGTV--NKMLHKPSGT-----IMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   387 VCTQEGPLYVIVEYAakgnlreflrarrppgpDLSPD-------GPRSSEGPLSFPALVscAYQVARGMQYL-ESRKCIH 458
Cdd:cd06616  73 ALFREGDCWICMELM-----------------DISLDkfykyvyEVLDSVIPEEILGKI--AVATVKALNYLkEELKIIH 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   459 RDLAARNVLVTEDDVMKIADFGLARgvHHIDYYKKTSN-GRLPvkWMAPEAL----FDRVYTHQSDVWSFGILLWEIFTl 533
Cdd:cd06616 134 RDVKPSNILLDRNGNIKLCDFGISG--QLVDSIAKTRDaGCRP--YMAPERIdpsaSRDGYDVRSDVWSLGITLYEVAT- 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   534 GGSPYPGIpvEELFSLLRE-----------GHRMERPPncpsELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06616 209 GKFPYPKW--NSVFDQLTQvvkgdppilsnSEEREFSP----SFVNFVNLCLIKDESKRPKYKELLK 269
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
346-546 2.89e-11

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 65.28  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   346 SIVAVKMLK-DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGpdlspdg 424
Cdd:cd08226  26 TLVTVKITNlDNCSEEHLKALQNEVVLSHFF-RHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPEG------- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   425 prssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAdfglarGVHHIdyYKKTSNGR------ 498
Cdd:cd08226  98 -------MNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLS------GLSHL--YSMVTNGQrskvvy 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   499 ---------LPvkWMAPEALFDRV--YTHQSDVWSFGILLWEIFTlGGSPYPGIPVEEL 546
Cdd:cd08226 163 dfpqfstsvLP--WLSPELLRQDLhgYNVKSDIYSVGITACELAR-GQVPFQDMRRTQM 218
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
358-589 3.54e-11

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 64.49  E-value: 3.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   358 SDKDLADLISEMEMMKligrHKNIINLLGVCTQEGPLYVIVEYAAkgnlreflrarrppGPDLSPDGPRSSEGPLSFPAL 437
Cdd:cd14094  48 STEDLKREASICHMLK----HPHIVELLETYSSDGMLYMVFEFMD--------------GADLCFEIVKRADAGFVYSEA 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   438 VSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDDV---MKIADFGLARGVHHIdyyKKTSNGRLPV-KWMAPEALFD 511
Cdd:cd14094 110 VASHYmrQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGES---GLVAGGRVGTpHFMAPEVVKR 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   512 RVYTHQSDVWSFGILLWeIFTLGGSPYPGIPVEELFSLLREGHRMERP--PNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14094 187 EPYGKPVDVWGCGVILF-ILLSGCLPFYGTKERLFEGIIKGKYKMNPRqwSHISESAKDLVRRMLMLDPAERITVYEALN 265
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
441-553 4.09e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 64.27  E-value: 4.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLArgVHHIDyyKKTSNGRL-PVKWMAPEALFDRVYTHQSD 519
Cdd:cd05630 108 AAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA--VHVPE--GQTIKGRVgTVGYMAPEVVKNERYTFSPD 183
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 204138   520 VWSFGILLWEIFTlGGSPY----PGIPVEELFSLLREG 553
Cdd:cd05630 184 WWALGCLLYEMIA-GQSPFqqrkKKIKREEVERLVKEV 220
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
321-538 4.28e-11

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 63.89  E-value: 4.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgMDSSRpdqtSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14167  11 LGTGAFSEVVLAE---EKRTQ----KLVAIKCIAKKALEGKETSIENEIAVLHKI-KHPNIVALDDIYESGGHLYLIMQL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARrppGPDLSPDGPRssegplsfpalvsCAYQVARGMQYLESRKCIHRDLAARNVL---VTEDDVMKIA 477
Cdd:cd14167  83 VSGGELFDRIVEK---GFYTERDASK-------------LIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMIS 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   478 DFGLARgVHHIDYYKKTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY 538
Cdd:cd14167 147 DFGLSK-IEGSGSVMSTACGT-P-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 203
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
319-530 6.15e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 64.34  E-value: 6.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEALGMDSSrpdqtsiVAVKMLKDNASDKDLAD-LISEMEMMKLIGrHKNIINLLGVCTqegPLYVI 397
Cdd:cd07874  23 KPIGSGAQGIVCAAYDAVLDRN-------VAIKKLSRPFQNQTHAKrAYRELVLMKCVN-HKNIISLLNVFT---PQKSL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRPPGPDLSPDGPRSSegplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd07874  92 EEFQDVYLVMELMDANLCQVIQMELDHERMS----------YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKIL 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   478 DFGLARGVhhidyykKTSNGRLPV----KWMAPEALFDRVYTHQSDVWSFGILLWEI 530
Cdd:cd07874 162 DFGLARTA-------GTSFMMTPYvvtrYYRAPEVILGMGYKENVDIWSVGCIMGEM 211
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
442-590 6.21e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 63.68  E-value: 6.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESRKCIHRDLAARNVLVTEDDV-MKIADFGLARGVHHIDYYKKTSNGRLP----------VKWMAPEALF 510
Cdd:cd14049 127 QQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIhVRIGDFGLACPDILQDGNDSTTMSRLNglthtsgvgtCLYAAPEQLE 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   511 DRVYTHQSDVWSFGILLWEIFtlggSPYpGIPVE--ELFSLLREGHRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd14049 207 GSHYDFKSDMYSIGVILLELF----QPF-GTEMEraEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSERPSASQLL 281

                ..
gi 204138   589 EA 590
Cdd:cd14049 282 ES 283
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
381-595 6.31e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 63.92  E-value: 6.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   381 IINLLGVCTQEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgpRSSEGPLSFPALVSCAyqVARGMQYL-ESRKCIHR 459
Cdd:cd06650  65 IVGFYGAFYSDGEISICMEHMDGGSLDQVLK--------------KAGRIPEQILGKVSIA--VIKGLTYLrEKHKIMHR 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   460 DLAARNVLVTEDDVMKIADFGLARGVhhIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPYP 539
Cdd:cd06650 129 DVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTR--SYMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYPIP 203
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   540 GIPVEEL---FSLLREGHRME-----RPPNCPSELYGlmrecwhaaPSQRPTFKqLVEALDKVL 595
Cdd:cd06650 204 PPDAKELelmFGCQVEGDAAEtpprpRTPGRPLSSYG---------MDSRPPMA-IFELLDYIV 257
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
11-87 6.58e-11

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205  Cd Length: 85  Bit Score: 58.77  E-value: 6.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    11 GNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRI---GGirlrhqhwSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:cd05728  14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIeveAG--------DLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
319-530 9.18e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 63.74  E-value: 9.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    319 KPLGEGCFGQVVCAealgmdsSRPDQTSIVAVKMLKDNASdkdladLISEMEMMKLigRHKNIINLLGVCTQeGPLYVIV 398
Cdd:PHA03209  72 KTLTPGSEGRVFVA-------TKPGQPDPVVLKIGQKGTT------LIEAMLLQNV--NHPSVIRMKDTLVS-GAITCMV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    399 EYAAKGNLREFLRARrppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIAD 478
Cdd:PHA03209 136 LPHYSSDLYTYLTKR---------------SRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGD 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 204138    479 FGLAR-GVHHIDYYKKTSNgrlpVKWMAPEALFDRVYTHQSDVWSFGILLWEI 530
Cdd:PHA03209 201 LGAAQfPVVAPAFLGLAGT----VETNAPEVLARDKYNSKADIWSAGIVLFEM 249
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
102-183 1.03e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 57.98  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSslgadgfpyvQVLKTTDINSSEVEVLYLRNVSAEDAGEYTCLA 181
Cdd:pfam13927   8 PSSVVVVEGETVTLTCEASGSPPPTITWYK----NGG----------KLSSGRTSLVGGNGTLTISNVTREDSGTYTCTA 73

                  ..
gi 204138     182 GN 183
Cdd:pfam13927  74 SN 75
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
315-538 1.06e-10

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 63.30  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    315 LVLGKPLGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEG 392
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGE-------YYAIKCLKKREilKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    393 PLYVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:PTZ00263  92 RVYFLLEFVVGGELFTHLR----------------KAG--RFPNDVAKFYhaELVLAFEYLHSKDIIYRDLKPENLLLDN 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138    471 DDVMKIADFGLARGVHHIDYykkTSNGRlPvKWMAPEALFDRVYTHQSDVWSFGILLWEiFTLGGSPY 538
Cdd:PTZ00263 154 KGHVKVTDFGFAKKVPDRTF---TLCGT-P-EYLAPEVIQSKGHGKAVDWWTMGVLLYE-FIAGYPPF 215
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
381-587 1.14e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 63.22  E-value: 1.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   381 IINLLGVCTQEGPLYVIVEYAAKGNLREFL-RARRPPGPDLspdgprsseGPLSfpalvscaYQVARGMQYL-ESRKCIH 458
Cdd:cd06615  61 IVGFYGAFYSDGEISICMEHMDGGSLDQVLkKAGRIPENIL---------GKIS--------IAVLRGLTYLrEKHKIMH 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   459 RDLAARNVLVTEDDVMKIADFGLARGVhhIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPY 538
Cdd:cd06615 124 RDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTR--SYMSPERLQGTHYTVQSDIWSLGLSLVEM-AIGRYPI 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   539 P-----------GIPVEELFS----LLREGHRM-----------------ERPPNCPS-----ELYGLMRECWHAAPSQR 581
Cdd:cd06615 199 PppdakeleamfGRPVSEGEAkeshRPVSGHPPdsprpmaifelldyivnEPPPKLPSgafsdEFQDFVDKCLKKNPKER 278

                ....*.
gi 204138   582 PTFKQL 587
Cdd:cd06615 279 ADLKEL 284
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
319-540 1.18e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 63.52  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqVVCAealGMDSSRPDQTSIVAVKMLKDNASDKDLAdlISEMEMMKLIGrHKNIINLLGVCTQEGPL---- 394
Cdd:cd07875  30 KPIGSGAQG-IVCA---AYDAILERNVAIKKLSRPFQNQTHAKRA--YRELVLMKCVN-HKNIIGLLNVFTPQKSLeefq 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 --YVIVEYAaKGNLREFLRarrppgpdLSPDGPRSSegplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD 472
Cdd:cd07875 103 dvYIVMELM-DANLCQVIQ--------MELDHERMS----------YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   473 VMKIADFGLARGVHHIDYYKKTSNGRLpvkWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd07875 164 TLKILDFGLARTAGTSFMMTPYVVTRY---YRAPEVILGMGYKENVDIWSVGCIMGEMIK-GGVLFPG 227
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
377-594 1.28e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 62.76  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   377 RHKNIINLL-------GVCTQegpLYVIVEYAAKGNLREFLRARrppgpdlspdgprssegPLSFPALVSCAYQVARGMQ 449
Cdd:cd14219  57 RHENILGFIaadikgtGSWTQ---LYLITDYHENGSLYDYLKST-----------------TLDTKAMLKLAYSSVSGLC 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   450 YLESR--------KCIHRDLAARNVLVTEDDVMKIADFGLArgvhhIDYYKKTSNGRLPV-------KWMAPEALFDRVY 514
Cdd:cd14219 117 HLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA-----VKFISDTNEVDIPPntrvgtkRYMPPEVLDESLN 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   515 THQ------SDVWSFGILLWEIF---TLGGS------PYPG-IPVEELFSLLRE--GHRMERP--PN------CPSELYG 568
Cdd:cd14219 192 RNHfqsyimADMYSFGLILWEVArrcVSGGIveeyqlPYHDlVPSDPSYEDMREivCIKRLRPsfPNrwssdeCLRQMGK 271
                       250       260
                ....*....|....*....|....*.
gi 204138   569 LMRECWHAAPSQRPTFKQLVEALDKV 594
Cdd:cd14219 272 LMTECWAHNPASRLTALRVKKTLAKM 297
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
312-559 1.51e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 62.32  E-value: 1.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNASDKDlADLISEMEMMKLIgRHKNIINLLGVCTQE 391
Cdd:cd14166   2 RETFIFMEVLGSGAFSEVYLVK-------QRSTGKLYALKCIKKSPLSRD-SSLENEIAVLKRI-KHENIVTLEDIYEST 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLREFLRARrppGPDLSPDGPRssegplsfpalvsCAYQVARGMQYLESRKCIHRDLAARNVL-VTE 470
Cdd:cd14166  73 THYYLVMQLVSGGELFDRILER---GVYTEKDASR-------------VINQVLSAVKYLHENGIVHRDLKPENLLyLTP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKI--ADFGLArgvhhidyyKKTSNGRLPVK-----WMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPGIPV 543
Cdd:cd14166 137 DENSKImiTDFGLS---------KMEQNGIMSTAcgtpgYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETE 206
                       250
                ....*....|....*..
gi 204138   544 EELFSLLREG-HRMERP 559
Cdd:cd14166 207 SRLFEKIKEGyYEFESP 223
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
442-532 1.57e-10

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 62.63  E-value: 1.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHidyykktsngrlPVKWM----------APEALFD 511
Cdd:cd07843 113 LQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS------------PLKPYtqlvvtlwyrAPELLLG 180
                        90       100
                ....*....|....*....|..
gi 204138   512 -RVYTHQSDVWSFGILLWEIFT 532
Cdd:cd07843 181 aKEYSTAIDMWSVGCIFAELLT 202
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
442-540 1.69e-10

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 62.71  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARgVH---HIDYYKKTSngRLPVKWM-APE-ALFDRVYTH 516
Cdd:cd07849 113 YQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR-IAdpeHDHTGFLTE--YVATRWYrAPEiMLNSKGYTK 189
                        90       100
                ....*....|....*....|....*
gi 204138   517 QSDVWSFGILLWEIFTlgGSP-YPG 540
Cdd:cd07849 190 AIDIWSVGCILAEMLS--NRPlFPG 212
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
321-540 1.75e-10

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 61.86  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVV-CAE-ALGMdssrpdqtsIVAVKMLKDNaSDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14103   1 LGRGKFGTVYrCVEkATGK---------ELAAKFIKCR-KAKDREDVRNEIEIMNQL-RHPRLLQLYDAFETPREMVLVM 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREflrarRPPGPDLSpdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDD--VMKI 476
Cdd:cd14103  70 EYVAGGELFE-----RVVDDDFE----------LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTgnQIKI 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARgvhhidyyKKTSNGRLPVKW-----MAPEAL-FDRVyTHQSDVWSFGILLWeIFTLGGSPYPG 540
Cdd:cd14103 135 IDFGLAR--------KYDPDKKLKVLFgtpefVAPEVVnYEPI-SYATDMWSVGVICY-VLLSGLSPFMG 194
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
102-196 1.76e-10

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 57.51  E-value: 1.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKhivingsslgaDGFPYVqvLKTTDINSSEVEVLYLRNVSAEDAGEYTCLA 181
Cdd:cd20952   6 PQNQTVAVGGTVVLNCQATGEPVPTISWLK-----------DGVPLL--GKDERITTLENGSLQIKGAEKSDTGEYTCVA 72
                        90
                ....*....|....*
gi 204138   182 GNSIGLSYQSAWLTV 196
Cdd:cd20952  73 LNLSGEATWSAVLDV 87
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
378-538 1.78e-10

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 62.27  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   378 HKNIINLLGVCTQ--EGPLYVIVEYAAKGnlreflrarrpPGPDLSPDGPRSSE-GPLSFPALVscayqvaRGMQYLESR 454
Cdd:cd14200  82 HVNIVKLIEVLDDpaEDNLYMVFDLLRKG-----------PVMEVPSDKPFSEDqARLYFRDIV-------LGIEYLHYQ 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   455 KCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGRlPVkWMAPEALFDrvyTHQS------DVWSFGILLW 528
Cdd:cd14200 144 KIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGT-PA-FMAPETLSD---SGQSfsgkalDVWAMGVTLY 218
                       170
                ....*....|
gi 204138   529 eIFTLGGSPY 538
Cdd:cd14200 219 -CFVYGKCPF 227
I-set pfam07679
Immunoglobulin I-set domain;
102-196 1.85e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSSLGADGfpYVQVLKTTDINSsevevLYLRNVSAEDAGEYTCLA 181
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFK----DGQPLRSSD--RFKVTYEGGTYT-----LTISNVQPDDSGKYTCVA 75
                          90
                  ....*....|....*
gi 204138     182 GNSIGLSYQSAWLTV 196
Cdd:pfam07679  76 TNSAGEAEASAELTV 90
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
313-538 1.99e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 62.05  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGqVVCaEALGMDSSRPDQTSIVAVKMLkdnaSDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd14086   1 DEYDLKEELGKGAFS-VVR-RCVQKSTGQEFAAKIINTKKL----SARDHQKLEREARICRLL-KHPNIVRLHDSISEEG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSFpalvsCAYQVARGMQYLESRKCIHRDLAARNVLV---T 469
Cdd:cd14086  74 FHYLVFDLVTGGELFEDIVARE-----------FYSEADASH-----CIQQILESVNHCHQNGIVHRDLKPENLLLaskS 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   470 EDDVMKIADFGLARGVhHIDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY 538
Cdd:cd14086 138 KGAAVKLADFGLAIEV-QGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPF 203
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
319-538 2.17e-10

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 62.36  E-value: 2.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqvVCAEALGMDSSRPDQTSIVAVKMLkdnasdkdlADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14179  13 KPLGEGSFS--ICRKCLHKKTNQEYAVKIVSKRME---------ANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRPPGpdlspdgprSSEGPLSFPALVScayqvarGMQYLESRKCIHRDLAARNVLVT---EDDVMK 475
Cdd:cd14179  82 ELLKGGELLERIKKKQHFS---------ETEASHIMRKLVS-------AVSHMHDVGVVHRDLKPENLLFTdesDNSEIK 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   476 IADFGLARgvhhidyYKKTSNGRLP-----VKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd14179 146 IIDFGFAR-------LKPPDNQPLKtpcftLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPF 205
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
381-569 2.32e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 62.37  E-value: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   381 IINLLGVCTQEGPLYVIVEYAAKGNLREFLR-ARRPPGPDLspdgprsseGPLSFPALvscayqvaRGMQYL-ESRKCIH 458
Cdd:cd06649  65 IVGFYGAFYSDGEISICMEHMDGGSLDQVLKeAKRIPEEIL---------GKVSIAVL--------RGLAYLrEKHQIMH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   459 RDLAARNVLVTEDDVMKIADFGLARGVhhIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILLWEIfTLGGSPY 538
Cdd:cd06649 128 RDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTR--SYMSPERLQGTHYSVQSDIWSMGLSLVEL-AIGRYPI 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 204138   539 PGIPVEELFSLL---------REGHRME---RPPNCPSELYGL 569
Cdd:cd06649 203 PPPDAKELEAIFgrpvvdgeeGEPHSISprpRPPGRPVSGHGM 245
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
321-559 2.34e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 61.83  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdSSRpdqtsIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14169  11 LGEGAFSEVVLAQERG--SQR-----LVALKCIPKKALRGKEAMVENEIAVLRRI-NHENIVSLEDIYESPTHLYLAMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARrppGPDLSPDGPRssegplsfpalvsCAYQVARGMQYLESRKCIHRDLAARNVLVT---EDDVMKIA 477
Cdd:cd14169  83 VTGGELFDRIIER---GSYTEKDASQ-------------LIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMIS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLArgvhhidyyKKTSNGRLPVK-----WMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPGIPVEELFSL-LR 551
Cdd:cd14169 147 DFGLS---------KIEAQGMLSTAcgtpgYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFNQiLK 216

                ....*...
gi 204138   552 EGHRMERP 559
Cdd:cd14169 217 AEYEFDSP 224
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
349-537 2.78e-10

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 61.60  E-value: 2.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKML-------KDNASDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLrarrppgpdls 421
Cdd:cd14093  32 AVKIIditgeksSENEAEELREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFELCRKGELFDYL----------- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   422 pdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARgvhHIDYYKKTSNGRLPV 501
Cdd:cd14093 101 -----TEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFAT---RLDEGEKLRELCGTP 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 204138   502 KWMAPEAL----FDRV--YTHQSDVWSFGILLWEIftLGGSP 537
Cdd:cd14093 173 GYLAPEVLkcsmYDNApgYGKEVDMWACGVIMYTL--LAGCP 212
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
367-578 2.80e-10

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 61.59  E-value: 2.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   367 SEMEMMKLIG-RHKNIINLLGV----CTQEGPLYVIVEYAAKGNLREFLRArrppgpdlspdgprsseGPLSFPALVSCA 441
Cdd:cd14141  36 NEYEIYSLPGmKHENILQFIGAekrgTNLDVDLWLITAFHEKGSLTDYLKA-----------------NVVSWNELCHIA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESR----------KCIHRDLAARNVLVTEDDVMKIADFGLA----RGVHHIDYYKKTSNGRlpvkWMAPE 507
Cdd:cd14141  99 QTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGLAlkfeAGKSAGDTHGQVGTRR----YMAPE 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   508 AL-----FDRVYTHQSDVWSFGILLWEIF---TLGGSPYPG--IPVEE------LFSLLRE--GHRMERPpncpselygL 569
Cdd:cd14141 175 VLegainFQRDAFLRIDMYAMGLVLWELAsrcTASDGPVDEymLPFEEevgqhpSLEDMQEvvVHKKKRP---------V 245

                ....*....
gi 204138   570 MRECWHAAP 578
Cdd:cd14141 246 LRECWQKHA 254
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
347-541 2.82e-10

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 61.52  E-value: 2.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   347 IVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAaKGNLREFLrARRPPGpdLSPDGPR 426
Cdd:cd07870  27 LVALKVISMKTEEGVPFTAIREASLLKGL-KHANIVLLHDIIHTKETLTFVFEYM-HTDLAQYM-IQHPGG--LHPYNVR 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   427 SSegplsfpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVhhiDYYKKTSNGRLPVKWM-A 505
Cdd:cd07870 102 LF------------MFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAK---SIPSQTYSSEVVTLWYrP 166
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 204138   506 PEALFDRV-YTHQSDVWSFGILLWEIFTlgGSP-YPGI 541
Cdd:cd07870 167 PDVLLGATdYSSALDIWGAGCIFIEMLQ--GQPaFPGV 202
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
321-538 3.01e-10

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 61.52  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaeaLGMDSSRPDQtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNII-------NLLGVCTQEGP 393
Cdd:cd14038   2 LGTGGFGNVL----RWINQETGEQ---VAIKQCRQELSPKNRERWCLEIQIMKRL-NHPNVVaardvpeGLQKLAPNDLP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LyVIVEYAAKGNLREFLrarrppgpDLSPDGPRSSEGPLSfpALVScayQVARGMQYLESRKCIHRDLAARNVLVTEDD- 472
Cdd:cd14038  74 L-LAMEYCQGGDLRKYL--------NQFENCCGLREGAIL--TLLS---DISSALRYLHENRIIHRDLKPENIVLQQGEq 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   473 --VMKIADFGlargvhhidYYKKTSNGRL------PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd14038 140 rlIHKIIDLG---------YAKELDQGSLctsfvgTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
441-589 3.31e-10

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 61.62  E-value: 3.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYL-ESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVhhIDYYKKTSNGRLPVkWMAPEAL----FDRvYT 515
Cdd:cd06618 120 TVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRL--VDSKAKTRSAGCAA-YMAPERIdppdNPK-YD 195
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   516 HQSDVWSFGILLWEIFTlGGSPYPGIPVE-ELFSLLREghrmERPPNCPSE------LYGLMRECWHAAPSQRPTFKQLV 588
Cdd:cd06618 196 IRADVWSLGISLVELAT-GQFPYRNCKTEfEVLTKILN----EEPPSLPPNegfspdFCSFVDLCLTKDHRYRPKYRELL 270

                .
gi 204138   589 E 589
Cdd:cd06618 271 Q 271
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
318-547 3.44e-10

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 61.10  E-value: 3.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGqvVCAEALGMDSSRPdqtsiVAVKMLKDNASDKDL-ADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd14197  14 GRELGRGKFA--VVRKCVEKDSGKE-----FAAKFMRKRRKGQDCrMEIIHEIAVLELAQANPWVINLHEVYETASEMIL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM-- 474
Cdd:cd14197  87 VLEYAAGGEIFNQCVADR--------------EEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgd 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   475 -KIADFGLARGVHHIDYYKKTSNgrLPvKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELF 547
Cdd:cd14197 153 iKIVDFGLSRILKNSEELREIMG--TP-EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDDKQETF 222
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
299-589 3.69e-10

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 61.58  E-value: 3.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   299 SLDLPLDPlwEFPRDRLVLGKPLGEGCFGqVVCAEALgmdssrPDQTSIVAVKMLkDNASDKDLADLISEMEMMKLIgRH 378
Cdd:cd06657   8 ALQMVVDP--GDPRTYLDNFIKIGEGSTG-IVCIATV------KSSGKLVAVKKM-DLRKQQRRELLFNEVVIMRDY-QH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   379 KNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIH 458
Cdd:cd06657  77 ENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTR-----------------MNEEQIAAVCLAVLKALSVLHAQGVIH 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   459 RDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd06657 140 RDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG--TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 204138   539 PGIPVEELFSLLREG--HRMERPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd06657 217 FNEPPLKAMKMIRDNlpPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLK 269
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
99-196 4.00e-10

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 56.87  E-value: 4.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    99 AGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSSLGADGfpyvqvlkttDINSSEVEV--LYLRNVSAEDAGE 176
Cdd:cd20976   5 SSVPKDLEAVEGQDFVAQCSARGKPVPRITWIR----NAQPLQYAA----------DRSTCEAGVgeLHIQDVLPEDHGT 70
                        90       100
                ....*....|....*....|
gi 204138   177 YTCLAGNSIGLSYQSAWLTV 196
Cdd:cd20976  71 YTCLAKNAAGQVSCSAWVTV 90
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
317-548 4.14e-10

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 60.96  E-value: 4.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQV-VCAEalgmdSSRPDQTSIVAVKMLKDNASDKDLA--DLISEMEMMKLIgRHKNIINLLGVCTQEGP 393
Cdd:cd14105   9 IGEELGSGQFAVVkKCRE-----KSTGLEYAAKFIKKRRSKASRRGVSreDIEREVSILRQV-LHPNIITLHDVFENKTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpdlspdgprssegPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14105  83 VVLILELVAGGELFDFLAEKE----------------SLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNV 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   474 ----MKIADFGLArgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPGIPVEELFS 548
Cdd:cd14105 147 piprIKLIDFGLA---HKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLA 221
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
102-196 4.33e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 56.25  E-value: 4.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKHivingsslgaDGfpyvqvlkttDINSSEVEV-----LYLRNVSAEDAGE 176
Cdd:cd05725   4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKE----------DG----------ELPKGRYEIlddhsLKIRKVTAGDMGS 63
                        90       100
                ....*....|....*....|
gi 204138   177 YTCLAGNSIGLSYQSAWLTV 196
Cdd:cd05725  64 YTCVAENMVGKIEASATLTV 83
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
321-554 5.84e-10

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 60.62  E-value: 5.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgMDSSrpdQTSIVAVKMLKDNASDKDL-ADLISEMEMMKLIGRHKNIINLLGV-CTQEGP---LY 395
Cdd:cd07837   9 IGEGTYGKVYKA----RDKN---TGKLVALKKTRLEMEEEGVpSTALREVSLLQMLSQSIYIVRLLDVeHVEENGkplLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKgNLREFLRARRppgpdlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTED-DVM 474
Cdd:cd07837  82 LVFEYLDT-DLKKFIDSYG-----------RGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVhhidyykktsngRLPVK----------WMAPEALFDRV-YTHQSDVWSFGIL----------------- 526
Cdd:cd07837 150 KIADLGLGRAF------------TIPIKsytheivtlwYRAPEVLLGSThYSTPVDMWSVGCIfaemsrkqplfpgdsel 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 204138   527 --LWEIFTLGGSP----YPGIpveelfSLLREGH 554
Cdd:cd07837 218 qqLLHIFRLLGTPneevWPGV------SKLRDWH 245
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
317-525 7.15e-10

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 60.77  E-value: 7.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALGMDSSRpdqtsIVAVK-MLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLY 395
Cdd:cd08216   2 LLYEIGKCFKGGGVVHLAKHKPTNT-----LVAVKkINLESDSKEDLKFLQQEILTSRQL-QHPNILPYVTSFVVDNDLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   396 VIVEYAAKGNLREFLRARRPPGpdlspdgprssegplsFPALVSCA--YQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd08216  76 VVTPLMAYGSCRDLLKTHFPEG----------------LPELAIAFilRDVLNALEYIHSKGYIHRSVKASHILISGDGK 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138   474 MKIADFGLARG-VHH------IDYYKKTSNGRLPvkWMAPEALFD--RVYTHQSDVWSFGI 525
Cdd:cd08216 140 VVLSGLRYAYSmVKHgkrqrvVHDFPKSSEKNLP--WLSPEVLQQnlLGYNEKSDIYSVGI 198
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
312-527 7.18e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 60.08  E-value: 7.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   312 RDRLVLGKPLGEGCFGQVVCAEalgmdssrpDQTS--IVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd14083   2 RDKYEFKEVLGTGAFSEVVLAE---------DKATgkLVAIKCIDKKALKGKEDSLENEIAVLRKI-KHPNIVQLLDIYE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLreFLRARRppgpdlspdgpRSSEGPLSFPALVScayQVARGMQYLESRKCIHRDLAARNVLV- 468
Cdd:cd14083  72 SKSHLYLVMELVTGGEL--FDRIVE-----------KGSYTEKDASHLIR---QVLEAVDYLHSLGIVHRDLKPENLLYy 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 --TEDDVMKIADFGLArgvhhidyyKKTSNGRLPVK-----WMAPEALFDRVYTHQSDVWSFG----ILL 527
Cdd:cd14083 136 spDEDSKIMISDFGLS---------KMEDSGVMSTAcgtpgYVAPEVLAQKPYGKAVDCWSIGvisyILL 196
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
11-87 8.77e-10

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 55.69  E-value: 8.77e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138    11 GNTVKFRCPAAGNPMPTIHWLKNGQAFHGENrigGIRLRHQHWsLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:cd05876  10 GQSLVLECIAEGLPTPTVKWLRPSGPLPPDR---VKYQNHNKT-LQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
447-548 9.31e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 60.11  E-value: 9.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   447 GMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARgvhhIDYYKKTSN---GRLPV--------------KWMAPEAL 509
Cdd:cd05609 112 ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSK----IGLMSLTTNlyeGHIEKdtrefldkqvcgtpEYIAPEVI 187
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 204138   510 FDRVYTHQSDVWSFGILLWEiFTLGGSPYPGIPVEELFS 548
Cdd:cd05609 188 LRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFG 225
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
319-530 9.47e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 60.81  E-value: 9.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGqVVCAE---ALGMDssrpdqtsiVAVKMLKDNASDKDLAD-LISEMEMMKLIGrHKNIINLLGVCTqegPL 394
Cdd:cd07876  27 KPIGSGAQG-IVCAAfdtVLGIN---------VAVKKLSRPFQNQTHAKrAYRELVLLKCVN-HKNIISLLNVFT---PQ 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLREFLRARRPPGPDLSPDGPRSSegplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd07876  93 KSLEEFQDVYLVMELMDANLCQVIHMELDHERMS----------YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTL 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   475 KIADFGLARGV---HHIDYYKKTSNGRlpvkwmAPEALFDRVYTHQSDVWSFGILLWEI 530
Cdd:cd07876 163 KILDFGLARTActnFMMTPYVVTRYYR------APEVILGMGYKENVDIWSVGCIMGEL 215
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
321-540 1.19e-09

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 59.59  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV-VCAEalgMDSSRPDQTSIVAVKMLKDNASDKDLADLISEMEmmkligrHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd14192  12 LGGGRFGQVhKCTE---LSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLN-------HVNLIQLYDAFESKTNLTLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 YAAKGNLREflrarrppgpdlspdgpRSSEGPLSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTED--DVMK 475
Cdd:cd14192  82 YVDGGELFD-----------------RITDESYQLTELDAILFtrQICEGVHYLHQHYILHLDLKPENILCVNStgNQIK 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARgvhhidYYKKTSngRLPVKWMAPEALFDRVYTHQ-----SDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd14192 145 IIDFGLAR------RYKPRE--KLKVNFGTPEFLAPEVVNYDfvsfpTDMWSVGVITYMLLS-GLSPFLG 205
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
437-538 1.41e-09

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 59.07  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   437 LVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKKTSN-GRLpvKWMAPEALFDRVYT 515
Cdd:cd14111 101 VVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRtGTL--EYMAPEMVKGEPVG 178
                        90       100
                ....*....|....*....|...
gi 204138   516 HQSDVWSFGILLWeIFTLGGSPY 538
Cdd:cd14111 179 PPADIWSIGVLTY-IMLSGRSPF 200
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
317-528 1.45e-09

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 59.23  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVvcAEALGMDSSRPdqtsiVAVKMLKDNASDKDLAD--LISEMEMMKLIGrHKNIINLLGVC-TQEGP 393
Cdd:cd14163   4 LGKTIGEGTYSKV--KEAFSKKHQRK-----VAIKIIDKSGGPEEFIQrfLPRELQIVERLD-HKNIIHVYEMLeSADGK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd14163  76 IYLVMELAEDGDVFDCV----------------LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTL 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 mKIADFGLAR--GVHHIDyYKKTSNGRlpVKWMAPEALfdRVYTHQS---DVWSFGILLW 528
Cdd:cd14163 140 -KLTDFGFAKqlPKGGRE-LSQTFCGS--TAYAAPEVL--QGVPHDSrkgDIWSMGVVLY 193
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
321-538 1.59e-09

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 59.08  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgMDSSRPdqtsiVAVKMLKDNASDKDLADliSEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14087   9 IGRGSFSRVVRVEH--RVTRQP-----YAIKMIETKCRGREVCE--SELNVLRRV-RHTNIIQLIEVFETKERVYMVMEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRARrppGPDLSPDGPRSSEgplsfpalvscayQVARGMQYLESRKCIHRDLAARNVLV----TEDDVMkI 476
Cdd:cd14087  79 ATGGELFDRIIAK---GSFTERDATRVLQ-------------MVLDGVKYLHGLGITHRDLKPENLLYyhpgPDSKIM-I 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   477 ADFGLARGVHHIDYYKKTSNGRLPvKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY 538
Cdd:cd14087 142 TDFGLASTRKKGPNCLMKTTCGTP-EYIAPEILLRKPYTQSVDMWAVGVIAY-ILLSGTMPF 201
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
319-550 1.74e-09

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 59.71  E-value: 1.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05593  21 KLLGKGTFGKVILVR-------EKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNT-RHPFLTSLKYSFQTKDRLCF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRPpgpdLSPDGPRSSegplsfpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05593  93 VMEYVNGGELFFHLSRERV----FSEDRTRFY------------GAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKI 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   477 ADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSLL 550
Cdd:cd05593 157 TDFGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 227
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
95-196 2.12e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 54.71  E-value: 2.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    95 PILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLkHiviNGSSLGADGFPYvQVLKTTdinssevevLYLRNVSAEDA 174
Cdd:cd20978   1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWL-H---NGKPLQGPMERA-TVEDGT---------LTIINVQPEDT 66
                        90       100
                ....*....|....*....|..
gi 204138   175 GEYTCLAGNSIGLSYQSAWLTV 196
Cdd:cd20978  67 GYYGCVATNEIGDIYTETLLHV 88
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
8-80 2.20e-09

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 54.87  E-value: 2.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFhgENRIGGIRLRH---QHWSLVMESVVP-----SDRGTYTCLVENSLGSI 79
Cdd:cd07693  12 VSKGDPATLNCKAEGRPTPTIQWLKNGQPL--ETDKDDPRSHRivlPSGSLFFLRVVHgrkgrSDEGVYVCVAHNSLGEA 89

                .
gi 204138    80 R 80
Cdd:cd07693  90 V 90
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
441-538 2.97e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 58.31  E-value: 2.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHidyyKKTSNGRL-PVKWMAPEALFDRV-YTHQS 518
Cdd:cd05577 101 AAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKG----GKKIKGRVgTHGYMAPEVLQKEVaYDFSV 176
                        90       100
                ....*....|....*....|
gi 204138   519 DVWSFGILLWEIFTlGGSPY 538
Cdd:cd05577 177 DWFALGCMLYEMIA-GRSPF 195
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
317-589 4.05e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 57.63  E-value: 4.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVcaEALGMDSSRPdqtsiVAVK-MLKDNASDK----DLADLISEMEMMKLI--GRHKNIINLLGVCT 389
Cdd:cd14005   4 VGDLLGKGGFGTVY--SGVRIRDGLP-----VAVKfVPKSRVTEWaminGPVPVPLEIALLLKAskPGVPGVIRLLDWYE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKG-NLREFLRARRPPGPDLSPDGPRssegplsfpalvscayQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:cd14005  77 RPDGFLLIMERPEPCqDLFDFITERGALSENLARIIFR----------------QVVEAVRHCHQRGVLHRDIKDENLLI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   469 TEDDV-MKIADFGLARGVHHiDYYKKTSNGRLpvkWMAPEALFDRVYtH--QSDVWSFGILLWEIFTlGGSPYpgipVEE 545
Cdd:cd14005 141 NLRTGeVKLIDFGCGALLKD-SVYTDFDGTRV---YSPPEWIRHGRY-HgrPATVWSLGILLYDMLC-GDIPF----END 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 204138   546 LFSLLREGHrmeRPPNCPSELYGLMRECWHAAPSQRPTFKQLVE 589
Cdd:cd14005 211 EQILRGNVL---FRPRLSKECCDLISRCLQFDPSKRPSLEQILS 251
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
434-535 4.52e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 57.97  E-value: 4.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   434 FPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLArgVHHIDYYKKTSNGRLPVKWMAPEALFD 511
Cdd:cd05608 102 FQEPRACFYtaQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA--VELKDGQTKTKGYAGTPGFMAPELLLG 179
                        90       100
                ....*....|....*....|....
gi 204138   512 RVYTHQSDVWSFGILLWEIFTLGG 535
Cdd:cd05608 180 EEYDYSVDYFTLGVTLYEMIAARG 203
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
113-186 4.77e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.10  E-value: 4.77e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   113 VELLCKVYSDAQPHIQWLKhiviNGSSLGADGfpyvqvlKTTDINSSEVEVLYLRNVSAEDAGEYTCLAGNSIG 186
Cdd:cd00096   1 VTLTCSASGNPPPTITWYK----NGKPLPPSS-------RDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
394-587 5.20e-09

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 58.34  E-value: 5.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRPpgpdlspdGPRSSEgplsfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTE--- 470
Cdd:cd13977 110 LWFVMEFCDGGDMNEYLLSRRP--------DRQTNT---------SFMLQLSSALAFLHRNQIVHRDLKPDNILISHkrg 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDVMKIADFGLARGVHhidyyKKTSNGRLPVK--------------WMAPEaLFDRVYTHQSDVWSFGILLWEI-----F 531
Cdd:cd13977 173 EPILKVADFGLSKVCS-----GSGLNPEEPANvnkhflssacgsdfYMAPE-VWEGHYTAKADIFALGIIIWAMveritF 246
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   532 T--------LGGSPYPGIPVEELFSLLREGHRME------RPPNCPSELYGLMRECWHAAPSQRPTFKQL 587
Cdd:cd13977 247 RdgetkkelLGTYIQQGKEIVPLGEALLENPKLElqiplkKKKSMNDDMKQLLRDMLAANPQERPDAFQL 316
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
319-581 5.73e-09

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 58.12  E-value: 5.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAE--ALGmdssrpdqtSIVAVKMLKDNA--SDKDLADLISEMEMMKlIGRHKNIINLLGVCTQEGPL 394
Cdd:cd05594  31 KLLGKGTFGKVILVKekATG---------RYYAMKILKKEVivAKDEVAHTLTENRVLQ-NSRHPFLTALKYSFQTHDRL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLreFLRarrppgpdLSPDGPRSSEGPLSFPAlvscayQVARGMQYLES-RKCIHRDLAARNVLVTEDDV 473
Cdd:cd05594 101 CFVMEYANGGEL--FFH--------LSRERVFSEDRARFYGA------EIVSALDYLHSeKNVVYRDLKLENLMLDKDGH 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   474 MKIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEELFSL-LRE 552
Cdd:cd05594 165 IKITDFGLCKEGIKDGATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELiLME 241
                       250       260       270
                ....*....|....*....|....*....|.
gi 204138   553 GHRMERP--PNCPSELYGLMREcwhaAPSQR 581
Cdd:cd05594 242 EIRFPRTlsPEAKSLLSGLLKK----DPKQR 268
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
457-537 6.68e-09

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 57.71  E-value: 6.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   457 IHRDLAARNVLVTEDDVMKIADFGLARG---VHHIDYYKKTSNGRLPvKWMAPEALFDRVYTHQSDVWSFGILLWEIftL 533
Cdd:cd05598 123 IHRDIKPDNILIDRDGHIKLTDFGLCTGfrwTHDSKYYLAHSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEM--L 199

                ....
gi 204138   534 GGSP 537
Cdd:cd05598 200 VGQP 203
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
8-77 6.96e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 53.51  E-value: 6.96e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHwSLVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd05747  15 VSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKS-TFEISKVQMSDEGNYTVVVENSEG 83
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
321-541 7.09e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 57.78  E-value: 7.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdssrPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd07869  13 LGEGSYATVYKGKS-------KVNGKLVALKVIRLQEEEGTPFTAIREASLLKGL-KHANIVLLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKgNLREFLRaRRPPGpdLSPDGPRSSegplsfpalvscAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFG 480
Cdd:cd07869  85 VHT-DLCQYMD-KHPGG--LHPENVKLF------------LFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   481 LARGVHHIDYykKTSNGRLPVKWMAPEALFDRV-YTHQSDVWSFGILLWEIFTlGGSPYPGI 541
Cdd:cd07869 149 LARAKSVPSH--TYSNEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQ-GVAAFPGM 207
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
321-540 7.83e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 57.73  E-value: 7.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSsrpdqtsIVAVKMLKDNASDKDLADLisEMEMM-KLIGRHKNIINLLGV--CTQEGPLYVI 397
Cdd:cd14229   8 LGRGTFGQVVKCWKRGTNE-------IVAVKILKNHPSYARQGQI--EVGILaRLSNENADEFNFVRAyeCFQHRNHTCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRarrppgpdlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTeDDV---- 473
Cdd:cd14229  79 VFEMLEQNLYDFLK--------------QNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLV-DPVrqpy 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   474 -MKIADFGLARGVHhidyyKKTSNGRLPVKWM-APEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPG 540
Cdd:cd14229 144 rVKVIDFGSASHVS-----KTVCSTYLQSRYYrAPEIILGLPFCEAIDMWSLGCVIAELF-LGWPLYPG 206
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
441-540 8.79e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 57.29  E-value: 8.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHIDYYKktsnGRL-PVKWMAPEALFDRVYTHQSD 519
Cdd:cd05632 110 AAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIR----GRVgTVGYMAPEVLNNQRYTLSPD 185
                        90       100
                ....*....|....*....|.
gi 204138   520 VWSFGILLWEIFTlGGSPYPG 540
Cdd:cd05632 186 YWGLGCLIYEMIE-GQSPFRG 205
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
348-532 8.95e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 57.35  E-value: 8.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   348 VAVKM--LKDNASDKdladliSEMEMMKLIG-RHKNIINLLGV----CTQEGPLYVIVEYAAKGNLREFLRArrppgpdl 420
Cdd:cd14140  21 VAVKIfpIQDKQSWQ------SEREIFSTPGmKHENLLQFIAAekrgSNLEMELWLITAFHDKGSLTDYLKG-------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   421 spdgprsseGPLSFPALVSCAYQVARGMQYL---------ESRK--CIHRDLAARNVLVTEDDVMKIADFGLA----RGV 485
Cdd:cd14140  87 ---------NIVSWNELCHIAETMARGLSYLhedvprckgEGHKpaIAHRDFKSKNVLLKNDLTAVLADFGLAvrfePGK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   486 HHIDYYKKTSNGRlpvkWMAPEAL-----FDRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd14140 158 PPGDTHGQVGTRR----YMAPEVLegainFQRDSFLRIDMYAMGLVLWELVS 205
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
317-548 1.21e-08

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 56.50  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVV-CAE-ALGMDssrpdqtsiVAVKMLK---DNASDKDLA--DLISEMEMMKLIgRHKNIINLLGVCT 389
Cdd:cd14196   9 IGEELGSGQFAIVKkCREkSTGLE---------YAAKFIKkrqSRASRRGVSreEIEREVSILRQV-LHPNIITLHDVYE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   390 QEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgPRSSEGPLSFpalvscAYQVARGMQYLESRKCIHRDLAARNVLVT 469
Cdd:cd14196  79 NRTDVVLILELVSGGELFDFLAQKE----------SLSEEEATSF------IKQILDGVNYLHTKKIAHFDLKPENIMLL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   470 EDDV----MKIADFGLArgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPGIPVEE 545
Cdd:cd14196 143 DKNIpiphIKLIDFGLA---HEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQE 218

                ...
gi 204138   546 LFS 548
Cdd:cd14196 219 TLA 221
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
441-532 1.35e-08

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 56.82  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLEsRKC--IHRDLAARNVLVTEDDV-MKIADFGLARGVHHidYYKKTSNGRlpvKWMAPEALFDRVYTHQ 517
Cdd:cd14136 125 ARQVLQGLDYLH-TKCgiIHTDIKPENVLLCISKIeVKIADLGNACWTDK--HFTEDIQTR---QYRSPEVILGAGYGTP 198
                        90
                ....*....|....*
gi 204138   518 SDVWSFGILLWEIFT 532
Cdd:cd14136 199 ADIWSTACMAFELAT 213
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
442-583 1.43e-08

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 56.08  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   442 YQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHiDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVW 521
Cdd:cd14110 106 WQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQ-GKVLMTDKKGDYVETMAPELLEGQGAGPQTDIW 184
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   522 SFGILLWeIFTLGGSPYPGIPVEELFSLLREGH-RMERppnCPSELYG----LMRECWHAAPSQRPT 583
Cdd:cd14110 185 AIGVTAF-IMLSADYPVSSDLNWERDRNIRKGKvQLSR---CYAGLSGgavnFLKSTLCAKPWGRPT 247
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
321-540 1.45e-08

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 56.08  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQV-VCAE-ALGMdssrpdqtsIVAVKMLKDNaSDKDLADLISEMEMMKLIGrHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14193  12 LGGGRFGQVhKCEEkSSGL---------KLAAKIIKAR-SQKEKEEVKNEIEVMNQLN-HANLIQLYDAFESRNDIVLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV--MKI 476
Cdd:cd14193  81 EYVDGGELFDRII---------------DENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKI 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 204138   477 ADFGLARgvhhidYYKKTSngRLPVKWMAPEALFDRVYTHQ-----SDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd14193 146 IDFGLAR------RYKPRE--KLRVNFGTPEFLAPEVVNYEfvsfpTDMWSLGVIAYMLLS-GLSPFLG 205
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
6-87 1.49e-08

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 52.42  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     6 HAVPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGgirlRHQHWS------LVMESVVPSDRGTYTCLVENSLGSI 79
Cdd:cd20951  10 HTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPG----KYKIESeygvhvLHIRRVTVEDSAVYSAVAKNIHGEA 85

                ....*...
gi 204138    80 RYSYLLDV 87
Cdd:cd20951  86 SSSASVVV 93
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
319-615 1.52e-08

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 56.90  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05603   1 KVIGKGSFGKVLLAK-------RKCDGKFYAVKVLQKKTilKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLreFLRARRppgpdlspdgprssEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05603  74 VLDYVNGGEL--FFHLQR--------------ERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFtLGGSPYPGIPVEELFSLLRegHRM 556
Cdd:cd05603 138 TDFGLCK--EGMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFYSRDVSQMYDNIL--HKP 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   557 ERPPNCPSE-----LYGLMRECWHAAPSQRPTFkqlVEALDKVLLAvSEEYLDL---RLTfGPYSPN 615
Cdd:cd05603 213 LHLPGGKTVaacdlLQGLLHKDQRRRLGAKADF---LEIKNHVFFS-PINWDDLyhkRIT-PPYNPN 274
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
441-538 1.57e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 56.54  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLARGVHHidyyKKTSNGRL-PVKWMAPEALFDRVYTHQSD 519
Cdd:cd05631 108 AAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPE----GETVRGRVgTVGYMAPEVINNEKYTFSPD 183
                        90
                ....*....|....*....
gi 204138   520 VWSFGILLWEIFTlGGSPY 538
Cdd:cd05631 184 WWGLGCLIYEMIQ-GQSPF 201
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
318-540 1.65e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 56.42  E-value: 1.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGqvVCAEALGMDSSRPDQTSIVAVKMLkdnasdkdlADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14180  11 EPALGEGSFS--VCRKCRHRQSGQEYAVKIISRRME---------ANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLREFLRARRppgpdlspdgpRSSEGPLS--FPALVScayqvarGMQYLESRKCIHRDLAARNVLV---TEDD 472
Cdd:cd14180  80 MELLRGGELLDRIKKKA-----------RFSESEASqlMRSLVS-------AVSFMHEAGVVHRDLKPENILYadeSDGA 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   473 VMKIADFGLARgvhhidyyKKTSNGR------LPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPG 540
Cdd:cd14180 142 VLKVIDFGFAR--------LRPQGSRplqtpcFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLS-GQVPFQS 206
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
368-539 1.65e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 56.16  E-value: 1.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   368 EMEMMKLIgRHKNIINLLGV--CTQEGPLYVIV--EYAAKGNLREFLRARRPPGPDLspdgprssegplsfpaLVSCAYQ 443
Cdd:cd14033  50 EVEMLKGL-QHPNIVRFYDSwkSTVRGHKCIILvtELMTSGTLKTYLKRFREMKLKL----------------LQRWSRQ 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   444 VARGMQYLESR--KCIHRDLAARNVLVT-EDDVMKIADFGLARgvhhidyYKKTSNGRLPV---KWMAPEaLFDRVYTHQ 517
Cdd:cd14033 113 ILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGLAT-------LKRASFAKSVIgtpEFMAPE-MYEEKYDEA 184
                       170       180
                ....*....|....*....|..
gi 204138   518 SDVWSFGILLWEIFTlggSPYP 539
Cdd:cd14033 185 VDVYAFGMCILEMAT---SEYP 203
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
321-532 1.91e-08

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 55.69  E-value: 1.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGMDSSRPDQTSIVAVKMLKDNASDKDLADlisEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14019   9 IGEGTFSSVYKAEDKLHDLYDRNKGRLVALKHIYPTSSPSRILN---ELECLERLGGSNNVSGLITAFRNEDQVVAVLPY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLRArrppgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT-EDDVMKIADF 479
Cdd:cd14019  86 IEHDDFRDFYRK-------------------MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDF 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   480 GLARGVHhidyYKK--------TSNGRlpvkwmAPEALFDrvYTHQS---DVWSFGILLWEIFT 532
Cdd:cd14019 147 GLAQREE----DRPeqrapragTRGFR------APEVLFK--CPHQTtaiDIWSAGVILLSILS 198
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
368-540 2.65e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 55.80  E-value: 2.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   368 EMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSFpalvsCAYQVARG 447
Cdd:cd14173  49 EVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSILSHIHRRR-----------HFNELEASV-----VVQDIASA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   448 MQYLESRKCIHRDLAARNVLVTEDDVM---KIADFGLARGVHHIDYYKKTSNGRL-----PVKWMAPEAL--FDR---VY 514
Cdd:cd14173 113 LDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSGIKLNSDCSPISTPELltpcgSAEYMAPEVVeaFNEeasIY 192
                       170       180
                ....*....|....*....|....*.
gi 204138   515 THQSDVWSFGILLWeIFTLGGSPYPG 540
Cdd:cd14173 193 DKRCDLWSLGVILY-IMLSGYPPFVG 217
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
450-581 2.82e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 55.83  E-value: 2.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   450 YLESRKCIHRDLAARNVLVTEDDVMKIADFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWE 529
Cdd:cd05571 110 YLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCK--EEISYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 187
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 204138   530 IFTlGGSPYPGIPVEELFSL-LREGHRMerPPNCPSELYGLMRECWHAAPSQR 581
Cdd:cd05571 188 MMC-GRLPFYNRDHEVLFELiLMEEVRF--PSTLSPEAKSLLAGLLKKDPKKR 237
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
319-531 2.84e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 56.18  E-value: 2.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEalgmdsSRPDQTsIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05602  13 KVIGKGSFGKVLLAR------HKSDEK-FYAVKVLQKKAilKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRPpgpdlspdgprssegpLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05602  86 VLDYINGGELFYHLQRERC----------------FLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 204138   477 ADFGLARgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIF 531
Cdd:cd05602 150 TDFGLCK--ENIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEML 202
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
317-538 2.86e-08

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 56.08  E-value: 2.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   317 LGKPLGEGCFGQVVCAEALgmdsSRPDQTSIVAVKMLKDNA---SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGP 393
Cdd:cd05614   4 LLKVLGTGAYGKVFLVRKV----SGHDANKLYAMKVLRKAAlvqKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   394 LYVIVEYAAKGNLREFLRARRppgpDLSPDGPRSSEGplsfpalvscayQVARGMQYLESRKCIHRDLAARNVLVTEDDV 473
Cdd:cd05614  80 LHLILDYVSGGELFTHLYQRD----HFSEDEVRFYSG------------EIILALEHLHKLGIVYRDIKLENILLDSEGH 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   474 MKIADFGLARGVHHIDyYKKTSNGRLPVKWMAPEALFDRV-YTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd05614 144 VVLTDFGLSKEFLTEE-KERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLT-GASPF 207
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
321-559 2.91e-08

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 56.19  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNASDK--DLADLISEMEMMkLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05600  19 VGQGGYGSVFLAR-------KKDTGEICALKIMKKKVLFKlnEVNHVLTERDIL-TTTNSPWLVKLLYAFQDPENVYLAM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRPpgpdLSPDGPR--SSEGPLSFPALVSCAYqvargmqylesrkcIHRDLAARNVLVTEDDVMKI 476
Cdd:cd05600  91 EYVPGGDFRTLLNNSGI----LSEEHARfyIAEMFAAISSLHQLGY--------------IHRDLKPENFLIDSSGHIKL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   477 ADFGLARG----------------------VHHIDYYK----KTSNGRLPVK---------WMAPEALFDRVYTHQSDVW 521
Cdd:cd05600 153 TDFGLASGtlspkkiesmkirleevkntafLELTAKERrniyRAMRKEDQNYansvvgspdYMAPEVLRGEGYDLTVDYW 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 204138   522 SFGILLWEiFTLGGSPYPGIPVEELFS-LLREGHRMERP 559
Cdd:cd05600 233 SLGCILFE-CLVGFPPFSGSTPNETWAnLYHWKKTLQRP 270
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
8-74 3.08e-08

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549  Cd Length: 88  Bit Score: 51.38  E-value: 3.08e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRhqhwSLVMESVVPSDRGTYTCLVEN 74
Cdd:cd20957  13 VDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED----VLVIPSVKREDKGMYQCFVRN 75
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
321-540 3.14e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 55.42  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAL--GMDssrpdqtsiVAVKMLKDNASDKDlADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd14174  10 LGEGAYAKVQGCVSLqnGKE---------YAVKIIEKNAGHSR-SRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSfpalvSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV---MK 475
Cdd:cd14174  80 EKLRGGSILAHIQKRK-----------HFNEREAS-----RVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   476 IADFGLARGVhhidyykKTSNGRLPV------------KWMAPEALfdRVYTHQS-------DVWSFGILLWeIFTLGGS 536
Cdd:cd14174 144 ICDFDLGSGV-------KLNSACTPIttpelttpcgsaEYMAPEVV--EVFTDEAtfydkrcDLWSLGVILY-IMLSGYP 213

                ....
gi 204138   537 PYPG 540
Cdd:cd14174 214 PFVG 217
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
3-87 3.49e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 3.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     3 KKLHAVpAGNTVKFRCPAAGNPMPTIHWLKNGQA-------FHGENRIGGIRLRhqhwslvmeSVVPSDRGTYTCLVENS 75
Cdd:cd20976   9 KDLEAV-EGQDFVAQCSARGKPVPRITWIRNAQPlqyaadrSTCEAGVGELHIQ---------DVLPEDHGTYTCLAKNA 78
                        90
                ....*....|..
gi 204138    76 LGSIRYSYLLDV 87
Cdd:cd20976  79 AGQVSCSAWVTV 90
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
327-532 3.53e-08

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 55.33  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   327 GQVVCAEALGMDSSRPDQTSIVAVKMLK-DNASDKDLAD--LISEMEMMKLIGRHKNIINLLGVCTQEGPLYViveyAAK 403
Cdd:cd14020   9 GQGSSASVYRVSSGRGADQPTSALKEFQlDHQGSQESGDygFAKERAALEQLQGHRNIVTLYGVFTNHYSANV----PSR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   404 GNLREFLRArrppgpDLSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT-EDDVMKIADFGLA 482
Cdd:cd14020  85 CLLLELLDV------SVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaEDECFKLIDFGLS 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   483 RGVHHIDY-YKKTSNGRlpvkwmAPEALF-----------DRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd14020 159 FKEGNQDVkYIQTDGYR------APEAELqnclaqaglqsETECTSAVDLWSLGIVLLEMFS 214
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
377-538 3.99e-08

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 54.61  E-value: 3.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   377 RHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFL-RARRppgpdLSPDgprssEGPLSFPALVScayqvarGMQYLESRK 455
Cdd:cd14665  54 RHPNIVRFKEVILTPTHLAIVMEYAAGGELFERIcNAGR-----FSED-----EARFFFQQLIS-------GVSYCHSMQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   456 CIHRDLAARNVLVTEDDV--MKIADFGLARGvhHIDYYKKTSNGRLPVkWMAPEALFDRVYTHQ-SDVWSFGILLWeIFT 532
Cdd:cd14665 117 ICHRDLKLENTLLDGSPAprLKICDFGYSKS--SVLHSQPKSTVGTPA-YIAPEVLLKKEYDGKiADVWSCGVTLY-VML 192

                ....*.
gi 204138   533 LGGSPY 538
Cdd:cd14665 193 VGAYPF 198
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
368-548 4.28e-08

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 55.01  E-value: 4.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   368 EMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdlspdgprssegPLSFPALVSCAYQVARG 447
Cdd:cd14195  58 EVNILREI-QHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKE----------------SLTEEEATQFLKQILDG 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   448 MQYLESRKCIHRDLAARNVLVTEDDV----MKIADFGLArgvHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSF 523
Cdd:cd14195 121 VHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIA---HKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSI 197
                       170       180
                ....*....|....*....|....*
gi 204138   524 GILLWeIFTLGGSPYPGIPVEELFS 548
Cdd:cd14195 198 GVITY-ILLSGASPFLGETKQETLT 221
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
318-540 4.37e-08

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 55.11  E-value: 4.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   318 GKPLGEGCFGQVvcaealgmdssrpdQTSI-------VAVKMLKDNASDKDlADLISEMEMMKLIGRHKNIINLLGVCTQ 390
Cdd:cd14090   7 GELLGEGAYASV--------------QTCInlytgkeYAVKIIEKHPGHSR-SRVFREVETLHQCQGHPNILQLIEYFED 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFLRARRppgpdlspdgpRSSEGPLSfpaLVscAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd14090  72 DERFYLVFEKMRGGPLLSHIEKRV-----------HFTEQEAS---LV--VRDIASALDFLHDKGIAHRDLKPENILCES 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 DDV---MKIADFGLARGVHHIDYYK---KTSNGRLPV---KWMAPE---ALFDR--VYTHQSDVWSFGILLWeIFTLGGS 536
Cdd:cd14090 136 MDKvspVKICDFDLGSGIKLSSTSMtpvTTPELLTPVgsaEYMAPEvvdAFVGEalSYDKRCDLWSLGVILY-IMLCGYP 214

                ....
gi 204138   537 PYPG 540
Cdd:cd14090 215 PFYG 218
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
321-537 4.87e-08

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 54.75  E-value: 4.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAealgmdSSRPDQTSIVAVKMLK------DNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPL 394
Cdd:cd14096   9 IGEGAFSNVYKA------VPLRNTGKPVAIKVVRkadlssDNLKGSSRANILKEVQIMKRL-SHPNIVKLLDFQESDEYY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKGNLreflrarrppgpdlspdgprssegplsFPALVSCAY-----------QVARGMQYLESRKCIHRDLAA 463
Cdd:cd14096  82 YIVLELADGGEI---------------------------FHQIVRLTYfsedlsrhvitQVASAVKYLHEIGVVHRDIKP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   464 RNVLV--------------TEDD-------------------VMKIADFGLARGVhhidyykKTSNGRLP---VKWMAPE 507
Cdd:cd14096 135 ENLLFepipfipsivklrkADDDetkvdegefipgvggggigIVKLADFGLSKQV-------WDSNTKTPcgtVGYTAPE 207
                       250       260       270
                ....*....|....*....|....*....|
gi 204138   508 ALFDRVYTHQSDVWSFGILLWEIftLGGSP 537
Cdd:cd14096 208 VVKDERYSKKVDMWALGCVLYTL--LCGFP 235
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
441-538 5.15e-08

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 54.67  E-value: 5.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   441 AYQVARGMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLArgVHHIDyyKKTSNGRL-PVKWMAPEALFDRVYTHQSD 519
Cdd:cd05605 108 AAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLA--VEIPE--GETIRGRVgTVGYMAPEVVKNERYTFSPD 183
                        90
                ....*....|....*....
gi 204138   520 VWSFGILLWEIFTlGGSPY 538
Cdd:cd05605 184 WWGLGCLIYEMIE-GQAPF 201
pknD PRK13184
serine/threonine-protein kinase PknD;
321-538 5.43e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 56.32  E-value: 5.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    321 LGEGCFGQVVcaeaLGMDssrPDQTSIVAVKMLKDNASDKDL------------ADLIsememmkligrHKNIINLLGVC 388
Cdd:PRK13184  10 IGKGGMGEVY----LAYD---PVCSRRVALKKIREDLSENPLlkkrflreakiaADLI-----------HPGIVPVYSIC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    389 TQEGPLYVIVEYAAKGNLREFLRARRPpgpdlSPDGPRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV 468
Cdd:PRK13184  72 SDGDPVYYTMPYIEGYTLKSLLKSVWQ-----KESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    469 TEDDVMKIADFGLAR--------------GVHHIDYYKKTSNGRL--PVKWMAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:PRK13184 147 GLFGEVVILDWGAAIfkkleeedlldidvDERNICYSSMTIPGKIvgTPDYMAPERLLGVPASESTDIYALGVILYQMLT 226

                 ....*.
gi 204138    533 LgGSPY 538
Cdd:PRK13184 227 L-SFPY 231
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
8-77 5.75e-08

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.65  E-value: 5.75e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd20973   9 VVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLG 78
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
95-196 6.09e-08

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 50.62  E-value: 6.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    95 PILQAGLPANTTAVVGSNVELLCKVYSDAQPHIQWLKhivingsslgADGFPYVQVLKTTdinsSEvEVLYLRNVSAEDA 174
Cdd:cd04968   1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRK----------VDGSPSSQWEITT----SE-PVLEIPNVQFEDE 65
                        90       100
                ....*....|....*....|..
gi 204138   175 GEYTCLAGNSIGLSYQSAWLTV 196
Cdd:cd04968  66 GTYECEAENSRGKDTVQGRIIV 87
IgI_3_hemolin-like cd20977
Third immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
8-77 6.97e-08

Third immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The third Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM).


Pssm-ID: 409569  Cd Length: 93  Bit Score: 50.47  E-value: 6.97e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAF--HGENRIGgirlRHQHWS---LVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd20977  12 AKAGDVTMIYCMYGSNPTAHPNYFKNGKDVngNPEDRIT----RHNRTSgkrLLFKTTLPEDEGVYTCEVDNGVG 82
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
313-559 8.90e-08

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 53.88  E-value: 8.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGqvVCAEALGMDSSRPdqtsiVAVKMLkDNASDKDLADLI-SEMEMMKLIgRHKNIINLLGVCTQE 391
Cdd:cd14184   1 EKYKIGKVIGDGNFA--VVKECVERSTGKE-----FALKII-DKAKCCGKEHLIeNEVSILRRV-KHPNIIMLIEEMDTP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   392 GPLYVIVEYAAKGNLReflrarrppgpDLSPDGPRSSEGPLSfpALVscaYQVARGMQYLESRKCIHRDLAARNVLVTE- 470
Cdd:cd14184  72 AELYLVMELVKGGDLF-----------DAITSSTKYTERDAS--AMV---YNLASALKYLHGLCIVHRDIKPENLLVCEy 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   471 ---DDVMKIADFGLARGVHHIDYykkTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY--PGIPVEE 545
Cdd:cd14184 136 pdgTKSLKLGDFGLATVVEGPLY---TVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFrsENNLQED 209
                       250
                ....*....|....
gi 204138   546 LFSLLREGHrMERP 559
Cdd:cd14184 210 LFDQILLGK-LEFP 222
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
313-540 9.53e-08

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 53.85  E-value: 9.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   313 DRLVLGKPLGEGCFGqvVCAEALGMDSSRPdqtsiVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEG 392
Cdd:cd14183   6 ERYKVGRTIGDGNFA--VVKECVERSTGRE-----YALKIINKSKCRGKEHMIQNEVSILRRV-KHPNIVLLIEEMDMPT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   393 PLYVIVEYAAKGNLREFLRARrppgpdlSPDGPRSSEGPLsfpalvscaYQVARGMQYLESRKCIHRDLAARNVLVTE-- 470
Cdd:cd14183  78 ELYLVMELVKGGDLFDAITST-------NKYTERDASGML---------YNLASAIKYLHSLNIVHRDIKPENLLVYEhq 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 204138   471 --DDVMKIADFGLARGVHHIDYykkTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPG 540
Cdd:cd14183 142 dgSKSLKLGDFGLATVVDGPLY---TVCGT-PT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRG 207
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
317-539 1.09e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 54.66  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    317 LGKPLGEGCFGqvVCAEALGMDSSRPdqtsiVAVKMLKDNASDKDladliSEMEMMKLIGrHKNIINLLGV----CTQEG 392
Cdd:PTZ00036  70 LGNIIGNGSFG--VVYEAICIDTSEK-----VAIKKVLQDPQYKN-----RELLIMKNLN-HINIIFLKDYyyteCFKKN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    393 P----LYVIVEYAAKgNLREFLRARrppgpdlspdgPRSSEG-PLSFPALVScaYQVARGMQYLESRKCIHRDLAARNVL 467
Cdd:PTZ00036 137 EknifLNVVMEFIPQ-TVHKYMKHY-----------ARNNHAlPLFLVKLYS--YQLCRALAYIHSKFICHRDLKPQNLL 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    468 VTEDD-VMKIADFGLA-------RGVHHI--DYYKktsngrlpvkwmAPEALFDRV-YTHQSDVWSFGILLWEIFtLGgs 536
Cdd:PTZ00036 203 IDPNThTLKLCDFGSAknllagqRSVSYIcsRFYR------------APELMLGATnYTTHIDLWSLGCIIAEMI-LG-- 267

                 ...
gi 204138    537 pYP 539
Cdd:PTZ00036 268 -YP 269
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
8-78 1.33e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.50  E-value: 1.33e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIGgIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGS 78
Cdd:cd20972  13 VAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQ-IHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGS 82
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
377-538 1.64e-07

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 52.85  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   377 RHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFL-RARRppgpdLSPDgprssEGPLSFPALVScayqvarGMQYLESRK 455
Cdd:cd14662  54 RHPNIIRFKEVVLTPTHLAIVMEYAAGGELFERIcNAGR-----FSED-----EARYFFQQLIS-------GVSYCHSMQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   456 CIHRDLAARNVLV--TEDDVMKIADFGLAR-GVHHIDyyKKTSNGRlPVkWMAPEALFDRVYTHQ-SDVWSFGILLWeIF 531
Cdd:cd14662 117 ICHRDLKLENTLLdgSPAPRLKICDFGYSKsSVLHSQ--PKSTVGT-PA-YIAPEVLSRKEYDGKvADVWSCGVTLY-VM 191

                ....*..
gi 204138   532 TLGGSPY 538
Cdd:cd14662 192 LVGAYPF 198
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
11-87 1.72e-07

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 49.48  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    11 GNTVKFRCPAAGNPMPTIHWLKNGQAFHgEN---RIGGIRLRHQHwslVME-----SVVPSDRGTYTCLVENSLGSIRYS 82
Cdd:cd20956  16 GPSVSLKCVASGNPLPQITWTLDGFPIP-ESprfRVGDYVTSDGD---VVSyvnisSVRVEDGGEYTCTATNDVGSVSHS 91

                ....*
gi 204138    83 YLLDV 87
Cdd:cd20956  92 ARINV 96
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
321-592 1.73e-07

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 52.96  E-value: 1.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdssrpdQTSIVAVKMLK-DNASD--KDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVI 397
Cdd:cd14160   1 IGEGEIFEVYRVRI---------GNRSYAVKLFKqEKKMQwkKHWKRFLSELEVLLLF-QHPNILELAAYFTETEKFCLV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   398 VEYAAKGNLreFLRARRPPGpdlspdgprssEGPLSFPALVSCAYQVARGMQYLE-SRKC--IHRDLAARNVLVTEDDVM 474
Cdd:cd14160  71 YPYMQNGTL--FDRLQCHGV-----------TKPLSWHERINILIGIAKAIHYLHnSQPCtvICGNISSANILLDDQMQP 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHHIDYYKKTSN----GRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlggspypGIPVE------ 544
Cdd:cd14160 138 KLTDFALAHFRPHLEDQSCTINmttaLHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT-------GCKVVlddpkh 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138   545 -ELFSLLREghRMER-----------------PPNCPSELYGLMRECWHAAPSQRPTFKQLVEALD 592
Cdd:cd14160 211 lQLRDLLHE--LMEKrgldsclsfldlkfppcPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLE 274
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
368-528 1.73e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 53.46  E-value: 1.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   368 EMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgPRSSEGPLS--FPALVScayqva 445
Cdd:cd14092  48 EVQLLRLCQGHPNIVKLHEVFQDELHTYLVMELLRGGELLERIRKK-----------KRFTESEASriMRQLVS------ 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   446 rGMQYLESRKCIHRDLAARNVLVTEDD---VMKIADFGLARgvhhidyyKKTSNGRL--P---VKWMAPEALFDRV---- 513
Cdd:cd14092 111 -AVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFAR--------LKPENQPLktPcftLPYAAPEVLKQALstqg 181
                       170
                ....*....|....*
gi 204138   514 YTHQSDVWSFGILLW 528
Cdd:cd14092 182 YDESCDLWSLGVILY 196
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
374-546 2.05e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 52.55  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    374 LIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRarrppgpdlspdgprsSEGPLSFPALVSCAYQVARGMQYLES 453
Cdd:PHA03390  64 LMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLK----------------KEGKLSEAEVKKIIRQLVEALNDLHK 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    454 RKCIHRDLAARNVLVTE-DDVMKIADFGLARGVHHIDYYKKTsngrlpVKWMAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:PHA03390 128 HNIIHNDIKLENVLYDRaKDRIYLCDYGLCKIIGTPSCYDGT------LDYFSPEKIKGHNYDVSFDWWAVGVLTYELLT 201
                        170
                 ....*....|....
gi 204138    533 lGGSPYPGIPVEEL 546
Cdd:PHA03390 202 -GKHPFKEDEDEEL 214
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
321-566 2.08e-07

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 53.49  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEAlgmdsSRPDQTsiVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIV 398
Cdd:cd05617  23 IGRGSYAKVLLVRL-----KKNDQI--YAMKVVKKELvhDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   399 EYAAKGNLR-EFLRARRPPgpdlspdgprssEGPLSFPALVSCAyqvarGMQYLESRKCIHRDLAARNVLVTEDDVMKIA 477
Cdd:cd05617  96 EYVNGGDLMfHMQRQRKLP------------EEHARFYAAEICI-----ALNFLHERGIIYRDLKLDNVLLDADGHIKLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLAR-GVHHIDyykKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY------PGIPVEE-LFSL 549
Cdd:cd05617 159 DYGMCKeGLGPGD---TTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMA-GRSPFdiitdnPDMNTEDyLFQV 234
                       250
                ....*....|....*..
gi 204138   550 LreghrMERPPNCPSEL 566
Cdd:cd05617 235 I-----LEKPIRIPRFL 246
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
365-553 2.13e-07

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 52.51  E-value: 2.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   365 LISEMEMMKLIGrHKNIINLLGVCTQEG-PLYVIVEYAAKGnlrEFLRARRPPGPDLSPDgprssegplsfPALVSCAYQ 443
Cdd:cd14109  43 LMREVDIHNSLD-HPNIVQMHDAYDDEKlAVTVIDNLASTI---ELVRDNLLPGKDYYTE-----------RQVAVFVRQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   444 VARGMQYLESRKCIHRDLAARNVLVtEDDVMKIADFGLARgvhHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSF 523
Cdd:cd14109 108 LLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSR---RLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSV 183
                       170       180       190
                ....*....|....*....|....*....|
gi 204138   524 GILLWEIFTlGGSPYPGIPVEELFSLLREG 553
Cdd:cd14109 184 GVLTYVLLG-GISPFLGDNDRETLTNVRSG 212
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
3-77 2.31e-07

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 48.72  E-value: 2.31e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138     3 KKLHAVpAGNTVKFRCPAAGNPMPTIHWLKNGQAFhGENRiggiRLR-HQHWSLVMESVVP-SDRGTYTCLVENSLG 77
Cdd:cd20958   8 GNLTAV-AGQTLRLHCPVAGYPISSITWEKDGRRL-PLNH----RQRvFPNGTLVIENVQRsSDEGEYTCTARNQQG 78
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
321-553 2.32e-07

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 52.96  E-value: 2.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKML--KDNASDKDLADLISEMEMM--KLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05586   1 IGKGTFGQVYQVR-------KKDTRRIYAMKVLskKVIVAKKEVAHTIGERNILvrTALDESPFIVGLKFSFQTPTDLYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLreFLRarrppgpdLSPDGpRSSEGPLSFpalvscaY--QVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd05586  74 VTDYMSGGEL--FWH--------LQKEG-RFSEDRAKF-------YiaELVLALEHLHKNDIVYRDLKPENILLDANGHI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   475 KIADFGLARGVHHIDYYKKTSNGrlPVKWMAPEALFDRV-YTHQSDVWSFGILLWEIfTLGGSPYPGIPVEELFSLLREG 553
Cdd:cd05586 136 ALCDFGLSKADLTDNKTTNTFCG--TTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEM-CCGWSPFYAEDTQQMYRNIAFG 212
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
7-88 2.48e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.77  E-value: 2.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     7 AVPAGNTVKFRCPAAGNPMPTIHWLKNGQafhgeNRIGGIRLRHQHwslVM--------ESVVPSDRGTYTCLVENSLGS 78
Cdd:cd05763  10 TIRAGSTARLECAATGHPTPQIAWQKDGG-----TDFPAARERRMH---VMpeddvffiVDVKIEDTGVYSCTAQNSAGS 81
                        90
                ....*....|
gi 204138    79 IRYSYLLDVL 88
Cdd:cd05763  82 ISANATLTVL 91
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
349-538 2.78e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 52.52  E-value: 2.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   349 AVKMLKDNASDKDLADLISEMEMMKligrHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppgpdlspdgprss 428
Cdd:cd14085  32 AVKKLKKTVDKKIVRTEIGVLLRLS----HPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEK--------------- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   429 eGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVT---EDDVMKIADFGLARGVHHiDYYKKTSNGRlPvKWMA 505
Cdd:cd14085  93 -GYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYAtpaPDAPLKIADFGLSKIVDQ-QVTMKTVCGT-P-GYCA 168
                       170       180       190
                ....*....|....*....|....*....|...
gi 204138   506 PEALFDRVYTHQSDVWSFGILLWeIFTLGGSPY 538
Cdd:cd14085 169 PEILRGCAYGPEVDMWSVGVITY-ILLCGFEPF 200
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
7-87 2.90e-07

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 48.70  E-value: 2.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     7 AVPAGNTVKFRCPAAGNPMPTIHWLKngQAFHGENRIggIRLRHQHWSLVMESVV--------PSDRGTYTCLVENSLGS 78
Cdd:cd05765  11 TVKVGETASFHCDVTGRPQPEITWEK--QVPGKENLI--MRPNHVRGNVVVTNIGqlviynaqPQDAGLYTCTARNSGGL 86

                ....*....
gi 204138    79 IRYSYLLDV 87
Cdd:cd05765  87 LRANFPLSV 95
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
321-528 2.99e-07

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 52.03  E-value: 2.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVcaEALGMDSSRPdqtsiVAVKML-KDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVE 399
Cdd:cd14082  11 LGSGQFGIVY--GGKHRKTGRD-----VAIKVIdKLRFPTKQESQLRNEVAILQQL-SHPGVVNLECMFETPERVFVVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   400 yAAKGNLREFLrarrppgpdLSPDGPRSSEGPLSFpaLVScayQVARGMQYLESRKCIHRDLAARNVLVTEDD---VMKI 476
Cdd:cd14082  83 -KLHGDMLEMI---------LSSEKGRLPERITKF--LVT---QILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKL 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 204138   477 ADFGLARGVHHiDYYKKTSNGRlPVkWMAPEALFDRVYTHQSDVWSFGILLW 528
Cdd:cd14082 148 CDFGFARIIGE-KSFRRSVVGT-PA-YLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
368-539 3.15e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 52.42  E-value: 3.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   368 EMEMMKLIgRHKNIINLL----GVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDLspdgprssegplsfpaLVSCAYQ 443
Cdd:cd14031  59 EAEMLKGL-QHPNIVRFYdsweSVLKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKV----------------LRSWCRQ 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   444 VARGMQYLESRK--CIHRDLAARNVLVT-EDDVMKIADFGLARgvhhidyYKKTSNGRLPV---KWMAPEaLFDRVYTHQ 517
Cdd:cd14031 122 ILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT-------LMRTSFAKSVIgtpEFMAPE-MYEEHYDES 193
                       170       180
                ....*....|....*....|..
gi 204138   518 SDVWSFGILLWEIFTlggSPYP 539
Cdd:cd14031 194 VDVYAFGMCMLEMAT---SEYP 212
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
456-538 3.55e-07

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 52.67  E-value: 3.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   456 CIHRDLAARNVLVTEDDVMKIADFGLARGVH--HIDYYKKT----SNGRLPVK---------------------WMAPEA 508
Cdd:cd05573 122 FIHRDIKPDNILLDADGHIKLADFGLCTKMNksGDRESYLNdsvnTLFQDNVLarrrphkqrrvraysavgtpdYIAPEV 201
                        90       100       110
                ....*....|....*....|....*....|
gi 204138   509 LFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd05573 202 LRGTGYGPECDWWSLGVILYEMLY-GFPPF 230
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
22-87 4.89e-07

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 48.26  E-value: 4.89e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 204138    22 GNPMPTIHWLKNGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:cd20959  29 GDLPLNIRWTLDGQPISDDLGITVSRLGRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
311-545 5.51e-07

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 51.38  E-value: 5.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   311 PRDRLVLGKPLGEGCFGQVVcaeaLGMDSSRPDQTsIVAVKMLKdnASDkDLADLISEMEMMKlIGRHKNIINLLGVCTQ 390
Cdd:cd14112   1 PTGRFSFGSEIFRGRFSVIV----KAVDSTTETDA-HCAVKIFE--VSD-EASEAVREFESLR-TLQHENVQRLIAAFKP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   391 EGPLYVIVEYAAKGNLREFlrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTE 470
Cdd:cd14112  72 SNFAYLVMEKLQEDVFTRF-----------------SSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQS 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   471 DD--VMKIADFGLARGVHHIDyyKKTSNGRlpVKWMAPEALFDRVY-THQSDVWSFGILLWeIFTLGGSPYPGIPVEE 545
Cdd:cd14112 135 VRswQVKLVDFGRAQKVSKLG--KVPVDGD--TDWASPEFHNPETPiTVQSDIWGLGVLTF-CLLSGFHPFTSEYDDE 207
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
321-586 6.55e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 51.59  E-value: 6.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNASDKDLADLISEMEMMKLIgRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14168  18 LGTGAFSEVVLAE-------ERATGKLFAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVL-VTEDDVMKI--A 477
Cdd:cd14168  90 VSGGELFDRI----------------VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyFSQDEESKImiS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   478 DFGLARGVHHIDYYKkTSNGrlPVKWMAPEALFDRVYTHQSDVWSFGILLWeIFTLGGSPYPGIPVEELF-SLLREGHRM 556
Cdd:cd14168 154 DFGLSKMEGKGDVMS-TACG--TPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKADYEF 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 204138   557 ERP--PNCPSELYGLMRECWHAAPSQRPTFKQ 586
Cdd:cd14168 230 DSPywDDISDSAKDFIRNLMEKDPNKRYTCEQ 261
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
319-537 6.59e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 51.50  E-value: 6.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   319 KPLGEGCFGQVVCAEalgmdssRPDQTSIVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYV 396
Cdd:cd05604   2 KVIGKGSFGKVLLAK-------RKRDGKYYAVKVLQKKVilNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   397 IVEYAAKGNLREFLRARRppgpdlspdgprssegplSFPALVSCAY--QVARGMQYLESRKCIHRDLAARNVLVTEDDVM 474
Cdd:cd05604  75 VLDFVNGGELFFHLQRER------------------SFPEPRARFYaaEIASALGYLHSINIVYRDLKPENILLDSQGHI 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 204138   475 KIADFGLAR-GVHHIDyyKKTSNGRLPvKWMAPEALFDRVYTHQSDVWSFGILLWEIftLGGSP 537
Cdd:cd05604 137 VLTDFGLCKeGISNSD--TTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEM--LYGLP 195
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
102-197 7.32e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 47.61  E-value: 7.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKHivingsslGADGFPYVQV----LKTTDinssevEVLYLRNVSAEDAGEY 177
Cdd:cd05763   6 PHDITIRAGSTARLECAATGHPTPQIAWQKD--------GGTDFPAARErrmhVMPED------DVFFIVDVKIEDTGVY 71
                        90       100
                ....*....|....*....|
gi 204138   178 TCLAGNSIGLSYQSAWLTVL 197
Cdd:cd05763  72 SCTAQNSAGSISANATLTVL 91
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
8-78 7.41e-07

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 47.20  E-value: 7.41e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 204138     8 VPAGNTVKFRCPAAGNPMPTIHWLKNGQAFHGENRIgGIRLRHQHWSLVMESVVPSDRGTYTCLVENSLGS 78
Cdd:cd05748   4 VRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRV-QIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGE 73
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
1-82 8.07e-07

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 47.31  E-value: 8.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     1 MEKKLHAVPAGNTVKFRCPAAGNPMPTIHWLKNG---QAFHGENRIGGIRlrhqHWSLVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd05738   4 MGPQLKVVEKARTATMLCAASGNPDPEISWFKDFlpvDTATSNGRIKQLR----SGALQIENSEESDQGKYECVATNSAG 79

                ....*
gi 204138    78 SiRYS 82
Cdd:cd05738  80 T-RYS 83
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
321-532 9.13e-07

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 51.16  E-value: 9.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVV-CaealgMDSSRPDqtSIVAVKMLKDNASDKDLADLisEMEMMKLIGRHKNIINLLGVCTQE-----GPL 394
Cdd:cd14214  21 LGEGTFGKVVeC-----LDHARGK--SQVALKIIRNVGKYREAARL--EINVLKKIKEKDKENKFLCVLMSDwfnfhGHM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   395 YVIVEYAAKgNLREFLRarrppgpdlspdgpRSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDDV- 473
Cdd:cd14214  92 CIAFELLGK-NTFEFLK--------------ENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEFd 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 204138   474 ------------------MKIADFGLARGVHhiDYYKKTSNGRlpvKWMAPEALFDRVYTHQSDVWSFGILLWEIFT 532
Cdd:cd14214 157 tlynesksceeksvkntsIRVADFGSATFDH--EHHTTIVATR---HYRPPEVILELGWAQPCDVWSLGCILFEYYR 228
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
11-87 9.28e-07

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 46.86  E-value: 9.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    11 GNTVKFRCPAAGNPMPTIHWLKNGQAFhgenrigGIRLRHQHWS---LVMESVVPSDRGTYTCLVENSLGSIRYSYLLDV 87
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTKGGSQL-------SVDRRHLVLSsgtLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
11-77 9.37e-07

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 47.01  E-value: 9.37e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138    11 GNTVKFRC-PAAGNPMPTIHWLKNGQAFHGENRigGIRLRHQHwSLVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd05724  12 GEMAVLECsPPRGHPEPTVSWRKDGQPLNLDNE--RVRIVDDG-NLLIAEARKSDEGTYKCVATNMVG 76
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
347-538 1.29e-06

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 50.80  E-value: 1.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   347 IVAVKMLKDNA--SDKDLADLISEMEMMKLIGRHKNIINLLGVCTQEGPLYVIVEYAAKGNLR-EFLRARRPPgpdlspd 423
Cdd:cd05618  47 IYAMKVVKKELvnDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMfHMQRQRKLP------- 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   424 gprsSEGPLSFPALVSCAyqvargMQYLESRKCIHRDLAARNVLVTEDDVMKIADFGLAR-GVHHIDyykKTSNGRLPVK 502
Cdd:cd05618 120 ----EEHARFYSAEISLA------LNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKeGLRPGD---TTSTFCGTPN 186
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 204138   503 WMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPY 538
Cdd:cd05618 187 YIAPEILRGEDYGFSVDWWALGVLMFEMMA-GRSPF 221
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
321-545 1.38e-06

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 50.36  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   321 LGEGCFGQVVCAEALGmdSSRPDQTSIVAVKMLKDNASDKDLADLISEmemmkligRHKNIINLLGVCTQEGPLYVIVEY 400
Cdd:cd14113  15 LGRGRFSVVKKCDQRG--TKRAVATKFVNKKLMKRDQVTHELGVLQSL--------QHPQLVGLLDTFETPTSYILVLEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   401 AAKGNLREFLrarrppgpdlspdgprSSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLVTED---DVMKIA 477
Cdd:cd14113  85 ADQGRLLDYV----------------VRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSlskPTIKLA 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   478 DFGLARGVhHIDYYKKTSNGRlpVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTlGGSPYPGIPVEE 545
Cdd:cd14113 149 DFGDAVQL-NTTYYIHQLLGS--PEFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPFLDESVEE 212
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
427-589 1.48e-06

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 49.95  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   427 SSEGPLSFPALVSCAYQVARGMQYLESRKCIHRDLAARNVLV-TEDDVMKIADFG---LARGVHHIDYykKTSNGRLPVK 502
Cdd:cd14102  97 TEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFGsgaLLKDTVYTDF--DGTRVYSPPE 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   503 WMApealFDRVYTHQSDVWSFGILLWEIFtlggspYPGIPVEELFSLLREGHRMER--PPNCPSelygLMRECWHAAPSQ 580
Cdd:cd14102 175 WIR----YHRYHGRSATVWSLGVLLYDMV------CGDIPFEQDEEILRGRLYFRRrvSPECQQ----LIKWCLSLRPSD 240

                ....*....
gi 204138   581 RPTFKQLVE 589
Cdd:cd14102 241 RPTLEQIFD 249
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
102-196 2.51e-06

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205  Cd Length: 85  Bit Score: 45.67  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSSLGADGFPYVqvlkttdinssEVEVLYLRNVSAEDAGEYTCLA 181
Cdd:cd05728   6 ISDTEADIGSSLRWECKASGNPRPAYRWLK----NGQPLASENRIEV-----------EAGDLRITKLSLSDSGMYQCVA 70
                        90
                ....*....|....*
gi 204138   182 GNSIGLSYQSAWLTV 196
Cdd:cd05728  71 ENKHGTIYASAELAV 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
104-196 2.25e-05

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 43.33  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   104 NTTAVVGSNVELLCKVYSDAQPHIQWLKhivingsslgaDGFPYVQVLK-TTDINSSEVEVLYLRNVSAEDAGEYTCLAG 182
Cdd:cd20973   6 DKEVVEGSAARFDCKVEGYPDPEVKWMK-----------DDNPIVESRRfQIDQDEDGLCSLIISDVCGDDSGKYTCKAV 74
                        90
                ....*....|....
gi 204138   183 NSIGLSYQSAWLTV 196
Cdd:cd20973  75 NSLGEATCSAELTV 88
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
11-77 5.98e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 42.15  E-value: 5.98e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138    11 GNTVKFRCPAAGNPMPTIHWLK-NGQAFHGENRiggirlRHQHWSLVMESVVPSDRGTYTCLVENSLG 77
Cdd:cd04968  16 GQTVTLECFALGNPVPQIKWRKvDGSPSSQWEI------TTSEPVLEIPNVQFEDEGTYECEAENSRG 77
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
102-188 1.04e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 41.41  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     102 PANTTAVVGSNVELLCKV-YSDAQPHIQWLKhivingsslgADGFPYVQVLKTTDINSSEVEVLYLRNVSAEDAGEYTCL 180
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSK----------EGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCV 72

                  ....*...
gi 204138     181 AGNSIGLS 188
Cdd:pfam00047  73 VNNPGGSA 80
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
7-88 1.56e-04

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 41.48  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138     7 AVPAGNTVKFRCPAAGNPMPTIHWLK----NGQAFHGEN-------RIGGIRLRHQHWS-LVMESVVPSDRGTYTCLVEN 74
Cdd:cd05858  12 SVVVGTDAEFVCKVYSDAQPHIQWLKhvekNGSKYGPDGlpyvevlKTAGVNTTDKEIEvLYLRNVTFEDAGEYTCLAGN 91
                        90
                ....*....|....
gi 204138    75 SLGSIRYSYLLDVL 88
Cdd:cd05858  92 SIGISHHSAWLTVL 105
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
110-196 2.63e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 40.26  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   110 GSNVELLCKVYSDAQPHIQWLKhiviNGSSLgaDGFPYVQVLKTTDINSsevevLYLRNVSAEDAGEYTCLAGNSIGLSY 189
Cdd:cd20972  16 GSKVRLECRVTGNPTPVVRWFC----EGKEL--QNSPDIQIHQEGDLHS-----LIIAEAFEEDTGRYSCLATNSVGSDT 84

                ....*..
gi 204138   190 QSAWLTV 196
Cdd:cd20972  85 TSAEIFV 91
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
109-186 3.35e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 39.84  E-value: 3.35e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 204138   109 VGSNVELLCKVYSDAQPHIQWLKhivingsslgaDGFPYVQvlKTTDINSSEVEVLYLRNVSAEDAGEYTCLAGNSIG 186
Cdd:cd05856  18 VGSSVRLKCVASGNPRPDITWLK-----------DNKPLTP--PEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAG 82
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
110-196 5.40e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 39.33  E-value: 5.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   110 GSNVELLCKVYSDAQPHIQWLKHIV-INGSSLGAdgfpyvqvlKTTDINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLS 188
Cdd:cd20951  15 KSDAKLRVEVQGKPDPEVKWYKNGVpIDPSSIPG---------KYKIESEYGVHVLHIRRVTVEDSAVYSAVAKNIHGEA 85

                ....*...
gi 204138   189 YQSAWLTV 196
Cdd:cd20951  86 SSSASVVV 93
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
97-183 3.46e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549  Cd Length: 88  Bit Score: 37.13  E-value: 3.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138    97 LQAGL-PANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSSLGADGfpyvqvlkttDINSSEVEVLYLRNVSAEDAG 175
Cdd:cd20957   2 LSATIdPPVQTVDFGRTAVFNCSVTGNPIHTVLWMK----DGKPLGHSS----------RVQILSEDVLVIPSVKREDKG 67

                ....*...
gi 204138   176 EYTCLAGN 183
Cdd:cd20957  68 MYQCFVRN 75
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
102-189 3.61e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 37.15  E-value: 3.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   102 PANTTAVVGSNVELLCKVYSDAQPHIQWLKhiviNGSSLGADgfpyvqvlkTTDINSSEV-----EVLYLRNV----SAE 172
Cdd:cd07693   7 PSDLIVSKGDPATLNCKAEGRPTPTIQWLK----NGQPLETD---------KDDPRSHRIvlpsgSLFFLRVVhgrkGRS 73
                        90
                ....*....|....*..
gi 204138   173 DAGEYTCLAGNSIGLSY 189
Cdd:cd07693  74 DEGVYVCVAHNSLGEAV 90
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
110-196 3.88e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 36.45  E-value: 3.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 204138   110 GSNVELLCKVYSDAQPHIQWLKhiviNGSSLGADgfPYVQVLKTTdinsseveVLYLRNVSAEDAGEYTCLAGNSIGLSY 189
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTK----GGSQLSVD--RRHLVLSSG--------TLRISRVALHDQGQYECQAVNIVGSQR 67

                ....*..
gi 204138   190 QSAWLTV 196
Cdd:cd05745  68 TVAQLTV 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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