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Conserved domains on  [gi|1958782016|ref|XP_038967755|]
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protein kinase C epsilon type isoform X1 [Rattus norvegicus]

Protein Classification

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 ...
412-689 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 cd05591:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 321  Bit Score: 635.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05591   161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05591   241 CVASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKI 278
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
3-135 3.89e-81

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


:

Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 253.35  E-value: 3.89e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016   3 VFNGLLKIKICEAVSLKPTAWSLRHAVgPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELA 82
Cdd:cd04014     1 MFTGTLKIKICEAVDLKPTDWSTRHAV-PKKGSQLLDPYVSIDVDDTHIGKTSTKPKTNSPVWNEEFTTEVHNGRNLELT 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016  83 VFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSS 135
Cdd:cd04014    80 VFHDAAIGPDDFVANCTISFEDLIQRGSGSFDLWVDLEPQGKLHVKIELKGSA 132
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
161-224 2.58e-48

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410385  Cd Length: 64  Bit Score: 163.79  E-value: 2.58e-48
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 161 RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLK 224
Cdd:cd20835     1 RRRVHQVNGHKFMATYLRQPTYCSHCKDFIWGVIGKQGYQCQVCTCVVHKRCHQLVVTKCPGNK 64
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
241-295 2.91e-37

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; 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. 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410388  Cd Length: 55  Bit Score: 132.78  E-value: 2.91e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 241 MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:cd20838     1 VPHRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNCGVN 55
 
Name Accession Description Interval E-value
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
412-689 0e+00

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: 635.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05591   161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05591   241 CVASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKI 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
408-668 4.76e-100

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 307.15  E-value: 4.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVIlqDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTF 567
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD-LFESILHDDVLYPVW---LSKEAVSILKAFMT 643
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLeLFKKIGKPKPPFPPPewdISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|....*
gi 1958782016  644 KNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:smart00220 237 KDPEKRLTA-------EEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
405-689 1.64e-84

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 269.77  E-value: 1.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILaLARKHPYLTQLYCCFQTKDRLFF 484
Cdd:PTZ00263   17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSIL-MELSHPFIVNMMCSFQDENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilngVT- 563
Cdd:PTZ00263   96 LLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VPd 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 -TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFM 642
Cdd:PTZ00263  171 rTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 643 TKNPHKRLGCVaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:PTZ00263  251 QTDHTKRLGTL--KGGVADVKNHPYFHGANWDKLYARYYPAPIPVRV 295
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
3-135 3.89e-81

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 253.35  E-value: 3.89e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016   3 VFNGLLKIKICEAVSLKPTAWSLRHAVgPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELA 82
Cdd:cd04014     1 MFTGTLKIKICEAVDLKPTDWSTRHAV-PKKGSQLLDPYVSIDVDDTHIGKTSTKPKTNSPVWNEEFTTEVHNGRNLELT 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016  83 VFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSS 135
Cdd:cd04014    80 VFHDAAIGPDDFVANCTISFEDLIQRGSGSFDLWVDLEPQGKLHVKIELKGSA 132
Pkinase pfam00069
Protein kinase domain;
408-668 4.37e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 203.63  E-value: 4.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVME 487
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLN-HPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEvtsalmflhqhgviyrdlkldnILldaeghckladfgmckEGILNGVTTTTF 567
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQ----------------------IL----------------EGLESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVW---LSKEAVSILKAFMTK 644
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|....
gi 1958782016 645 NPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:pfam00069 201 DPSKRLTA-------TQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
411-649 6.49e-59

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 206.40  E-value: 6.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:COG0515    12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDGRPYLVMEYVE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT-TTTFCG 569
Cdd:COG0515    91 GESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTqTGTVVG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL--------YPVWLskEAVsILKAf 641
Cdd:COG0515   171 TPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPppselrpdLPPAL--DAI-VLRA- 246

                  ....*...
gi 1958782016 642 MTKNPHKR 649
Cdd:COG0515   247 LAKDPEER 254
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
161-224 2.58e-48

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 163.79  E-value: 2.58e-48
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 161 RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLK 224
Cdd:cd20835     1 RRRVHQVNGHKFMATYLRQPTYCSHCKDFIWGVIGKQGYQCQVCTCVVHKRCHQLVVTKCPGNK 64
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
241-295 2.91e-37

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; 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. 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 132.78  E-value: 2.91e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 241 MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:cd20838     1 VPHRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNCGVN 55
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
411-649 6.34e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 100.25  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAE---LkgkDEVYAVKVLKKDviLQDDDvdcTMTEKRI---LALAR-KHPYLTQLYCCFQTKDRLF 483
Cdd:NF033483   12 GERIGRGGMAEVYLAKdtrL---DRDVAVKVLRPD--LARDP---EFVARFRreaQSAASlSHPNIVSVYDVGEDGGIPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFgmckeGI---LN 560
Cdd:NF033483   84 IVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF-----GIaraLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTT---TFCGTPDYIAPEilQ-ELEY-GPSVDWWALGVLMYEMMAGQPPFEAD----------NED-----DLFESIl 620
Cdd:NF033483  159 STTMTqtnSVLGTVHYLSPE--QaRGGTvDARSDIYSLGIVLYEMLTGRPPFDGDspvsvaykhvQEDppppsELNPGI- 235
                         250       260
                  ....*....|....*....|....*....
gi 1958782016 621 hddvlyPVWLskEAVsILKAfMTKNPHKR 649
Cdd:NF033483  236 ------PQSL--DAV-VLKA-TAKDPDDR 254
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
243-295 3.08e-20

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 84.42  E-value: 3.08e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
170-220 5.78e-18

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 77.87  E-value: 5.78e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWG-LGKQGLKCSWCKLNVHKRCHEKVPPEC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
243-292 1.83e-15

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 70.57  E-value: 1.83e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958782016  243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
170-220 1.01e-13

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 65.95  E-value: 1.01e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016  170 HKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWG-SFKQGLRCSECKVKCHKKCADKVPKAC 50
C2 pfam00168
C2 domain;
6-119 6.28e-12

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 62.34  E-value: 6.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016   6 GLLKIKICEAVSLKPtawslrhavgpRPQTFLLDPYIALNVDDS-RIGQTATKQKTNSPAWHDEFVTDV--CNGRKIELA 82
Cdd:pfam00168   1 GRLTVTVIEAKNLPP-----------KDGNGTSDPYVKVYLLDGkQKKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIE 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958782016  83 VFHDAPIGYDDFVANCTIQFEELLQngSRHFEDWIDL 119
Cdd:pfam00168  70 VYDYDRFGRDDFIGEVRIPLSELDS--GEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
7-111 1.85e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 60.96  E-value: 1.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016    7 LLKIKICEAVSLKPtawslrhavgpRPQTFLLDPYIALNVD--DSRIGQTATKQKTNSPAWHDEFVTDVCN--GRKIELA 82
Cdd:smart00239   1 TLTVKIISARNLPP-----------KDKGGKSDPYVKVSLDgdPKEKKKTKVVKNTLNPVWNETFEFEVPPpeLAELEIE 69
                           90       100
                   ....*....|....*....|....*....
gi 1958782016   83 VFHDAPIGYDDFVANCTIQFEELLQNGSR 111
Cdd:smart00239  70 VYDKDRFGRDDFIGQVTIPLSDLLLGGRH 98
 
Name Accession Description Interval E-value
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
412-689 0e+00

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: 635.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05591    81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05591   161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05591   241 CVASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKI 278
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
412-689 0e+00

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: 599.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05570     1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05570    81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05570   161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVAaqNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05570   241 CGP--KGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKV 276
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
412-689 0e+00

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: 529.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05590    81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05590   161 DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05590   241 SL-TLGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRI 277
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
411-689 7.51e-173

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: 496.53  E-value: 7.51e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd05587     1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGT 570
Cdd:cd05587    81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRL 650
Cdd:cd05587   161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958782016 651 GCVAaqNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05587   241 GCGP--TGERDIKEHPFFRRIDWEKLERREIQPPFKPKI 277
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
412-689 1.09e-168

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: 485.74  E-value: 1.09e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05592     1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05592    81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05592   161 DYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVAAQNGEdaIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05592   241 VPECPAGD--IRDHPFFKTIDWDKLERREIDPPFKPKV 276
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
407-688 3.63e-157

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: 456.77  E-value: 3.63e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05616     1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTT 566
Cdd:cd05616    81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNP 646
Cdd:cd05616   161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 647 HKRLGCvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPR 688
Cdd:cd05616   241 GKRLGC--GPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPK 280
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
402-689 1.42e-148

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: 435.19  E-value: 1.42e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDR 481
Cdd:cd05615     6 RVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd05615    86 LYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAF 641
Cdd:cd05615   166 VTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGL 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 642 MTKNPHKRLGCvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05615   246 MTKHPAKRLGC--GPEGERDIREHAFFRRIDWDKLENREIQPPFKPKV 291
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
402-689 1.04e-139

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: 412.39  E-value: 1.04e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDR 481
Cdd:cd05619     1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd05619    81 LFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAF 641
Cdd:cd05619   161 AKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 642 MTKNPHKRLGCvaaqngEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05619   241 FVREPERRLGV------RGDIRQHPFFREINWEALEEREIEPPFKPKV 282
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
412-689 2.44e-138

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: 408.28  E-value: 2.44e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTR-HPFLTSLKYSFQTNDRLCFVMEYVNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05571    80 GELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05571   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLG 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 cvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05571   240 --GGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQV 275
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
412-689 4.09e-138

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: 407.79  E-value: 4.09e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05620    81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05620   161 DYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 CVAaqngedAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05620   241 VVG------NIRGHPFFKTINWTALEKRELDPPFKPKV 272
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
408-689 2.07e-137

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: 406.30  E-value: 2.07e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNsaRHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQrSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd05589    81 MEYAAGGDLMMHIH-EDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd05589   160 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKN 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 646 PHKRLGCvAAQNGEDaIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05589   240 PERRLGA-SERDAED-VKKQPFFRNIDWEALLARKIKPPFVPTI 281
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
414-668 5.32e-134

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: 394.19  E-value: 5.32e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDY 573
Cdd:cd05123    80 LFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 574 IAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCv 653
Cdd:cd05123   160 LAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGS- 238
                         250
                  ....*....|....*
gi 1958782016 654 aaqNGEDAIKQHPFF 668
Cdd:cd05123   239 ---GGAEEIKAHPFF 250
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
412-689 5.41e-128

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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 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: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 382.15  E-value: 5.41e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05588     1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05588    81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE----ADN-----EDDLFESILHDDVLYPVWLSKEAVSILKAFM 642
Cdd:cd05588   161 NYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDivgsSDNpdqntEDYLFQVILEKPIRIPRSLSVKAASVLKGFL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 643 TKNPHKRLGCvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05588   241 NKNPAERLGC-HPQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRI 286
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
412-689 1.36e-124

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 373.19  E-value: 1.36e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05575     1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05575    81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05575   161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 652 cvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05575   241 ---SGNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNV 275
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
403-689 1.08e-118

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: 359.33  E-value: 1.08e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 403 LGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRL 482
Cdd:cd05617    12 LGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd05617    92 FLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE--ADN-----EDDLFESILHDDVLYPVWLSKEAV 635
Cdd:cd05617   172 TTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDiiTDNpdmntEDYLFQVILEKPIRIPRFLSVKAS 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 636 SILKAFMTKNPHKRLGCvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05617   252 HVLKGFLNKDPKERLGC-QPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQI 304
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
403-689 1.24e-117

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: 357.04  E-value: 1.24e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 403 LGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRL 482
Cdd:cd05618    17 LGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd05618    97 FFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGD 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE----ADN-----EDDLFESILHDDVLYPVWLSKE 633
Cdd:cd05618   177 TTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDivgsSDNpdqntEDYLFQVILEKQIRIPRSLSVK 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 634 AVSILKAFMTKNPHKRLGCVaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05618   257 AASVLKSFLNKDPKERLGCH-PQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNI 311
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
406-689 2.07e-111

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: 338.01  E-value: 2.07e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05580     1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVR-HPFIVNLLGSFQDDRNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVTTT 565
Cdd:cd05580    80 MEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAK--RVKDRTYT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd05580   158 L-CGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVD 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 646 PHKRLGCVAaqNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05580   237 LTKRLGNLK--NGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKV 278
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
412-693 1.19e-110

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: 337.36  E-value: 1.19e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTR-HPFLTALKYAFQTHDRLCFVMEYANG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05595    80 GELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05595   160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLG 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 652 cvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIFASV 693
Cdd:cd05595   240 --GGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEV 279
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
401-689 1.24e-105

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: 325.11  E-value: 1.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 401 KRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKD 480
Cdd:cd05593    10 KRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTR-HPFLTSLKYSFQTKD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN 560
Cdd:cd05593    89 RLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA 640
Cdd:cd05593   169 AATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 641 FMTKNPHKRLGcvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05593   249 LLIKDPNKRLG--GGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQV 295
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
411-689 4.02e-105

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: 323.07  E-value: 4.02e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGT 570
Cdd:cd05604    81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRL 650
Cdd:cd05604   161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRL 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958782016 651 GcvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05604   241 G---AKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNV 276
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
388-689 4.29e-105

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: 324.29  E-value: 4.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 388 SPGENG-----EVRQGQAK-RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILA 461
Cdd:cd05594     1 SPSDNSgaeemEVSLTKPKhKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 462 LARkHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLH-QHGVIYRDLKLDNILL 540
Cdd:cd05594    81 NSR-HPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 541 DAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd05594   160 DKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 621 HDDVLYPVWLSKEAVSILKAFMTKNPHKRLGcvaaQNGEDA--IKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05594   240 MEEIRFPRTLSPEAKSLLSGLLKKDPKQRLG----GGPDDAkeIMQHKFFAGIVWQDVYEKKLVPPFKPQV 306
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
412-689 1.14e-100

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: 311.52  E-value: 1.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05603    81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd05603   161 EYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958782016 652 CVAaqngeD--AIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05603   241 AKA-----DflEIKNHVFFSPINWDDLYHKRITPPYNPNV 275
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
408-668 4.76e-100

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 307.15  E-value: 4.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVIlqDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTF 567
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD-LFESILHDDVLYPVW---LSKEAVSILKAFMT 643
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLeLFKKIGKPKPPFPPPewdISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|....*
gi 1958782016  644 KNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:smart00220 237 KDPEKRLTA-------EEALQHPFF 254
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
411-690 6.74e-100

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: 309.33  E-value: 6.74e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAE-LKGKDE--VYAVKVLKKDVILQDD-DVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05584     1 LKVLGKGGYGKVFQVRkTTGSDKgkIFAMKVLKKASIVRNQkDTAHTKAERNILE-AVKHPFIVDLHYAFQTGGKLYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTT 566
Cdd:cd05584    80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNP 646
Cdd:cd05584   160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 647 HKRLGcvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIF 690
Cdd:cd05584   240 SSRLG--SGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQ 281
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
407-689 1.83e-96

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: 301.17  E-value: 1.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05602     8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTT 566
Cdd:cd05602    88 DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTST 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNP 646
Cdd:cd05602   168 FCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDR 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 647 HKRLGcvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05602   248 TKRLG---AKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNV 287
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
416-673 2.95e-91

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: 284.88  E-value: 2.95e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 416 KGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGDLM 495
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQ-NPFVVKLYYSFQGKKNLYLVMEYLPGGDLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 496 FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT------------ 563
Cdd:cd05579    82 SLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIklsiqkksngap 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 ---TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP--VWLSKEAVSIL 638
Cdd:cd05579   162 ekeDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPedPEVSDEAKDLI 241
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 639 KAFMTKNPHKRLGCvaaqNGEDAIKQHPFFKEIDW 673
Cdd:cd05579   242 SKLLTPDPEKRLGA----KGIEEIKNHPFFKGIDW 272
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
413-693 3.56e-91

Catalytic domain of Yeast Protein Kinase 1-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 proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-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: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 286.39  E-value: 3.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQV-DCPFIVPLKFSFQSPEKLYLVLAFINGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPD 572
Cdd:cd05585    80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 573 YIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGc 652
Cdd:cd05585   160 YLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLG- 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 653 vaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIFASV 693
Cdd:cd05585   239 ---YNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAI 276
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
406-689 1.28e-90

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: 286.10  E-value: 1.28e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADS-PWIVRLHYAFQDEDHLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG---- 561
Cdd:cd05573    80 MEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGdres 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 -------------------------VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLF 616
Cdd:cd05573   160 ylndsvntlfqdnvlarrrphkqrrVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETY 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 617 ESILH--DDVLYP--VWLSKEAVSILKAFMTkNPHKRLGCVaaqngeDAIKQHPFFKEIDWV-LLEQkkiKPPFKPRI 689
Cdd:cd05573   240 SKIMNwkESLVFPddPDVSPEAIDLIRRLLC-DPEDRLGSA------EEIKAHPFFKGIDWEnLRES---PPPFVPEL 307
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
412-687 3.63e-90

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: 283.91  E-value: 3.63e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLA-ELKGKD--EVYAVKVLKKDVILQDDDVDCTMtEKRILALARkHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd05582     1 KVLGQGSFGKVFLVrKITGPDagTLYAMKVLKKATLKVRDRVRTKM-ERDILADVN-HPFIVKLHYAFQTEGKLYLILDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd05582    79 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHK 648
Cdd:cd05582   159 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPAN 238
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958782016 649 RLGcvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05582   239 RLG--AGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKP 275
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
406-689 4.00e-90

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: 282.76  E-value: 4.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILaLARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRIL-QAINFPFLVKLEYSFKDNSNLYMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGvTTT 565
Cdd:cd14209    80 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKR--VKG-RTW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd14209   157 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVD 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 646 PHKRLGCVaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd14209   237 LTKRFGNL--KNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKL 278
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
406-688 6.08e-90

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-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: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 283.36  E-value: 6.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05574     1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATL-DHPFLPTLYASFQTSTHLCFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDL--MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG------ 557
Cdd:cd05574    80 MDYCPGGELfrLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSsvtppp 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ---ILNGVT--------------------TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd05574   160 vrkSLRKGSrrssvksieketfvaepsarSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDE 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 615 LFESILHDDVLYP--VWLSKEAVSILKAFMTKNPHKRLGCvaaQNGEDAIKQHPFFKEIDWVLLeqKKIKPPFKPR 688
Cdd:cd05574   240 TFSNILKKELTFPesPPVSSEAKDLIRKLLVKDPSKRLGS---KRGASEIKRHPFFRGVNWALI--RNMTPPIIPR 310
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
406-668 5.06e-85

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: 269.08  E-value: 5.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRL-AHPGIVKLYYTFQDESKLYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK---------- 555
Cdd:cd05581    80 LEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdsspes 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 -------EGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV 628
Cdd:cd05581   160 tkgdadsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958782016 629 WLSKEAVSILKAFMTKNPHKRLGCVaAQNGEDAIKQHPFF 668
Cdd:cd05581   240 NFPPDAKDLIQKLLVLDPSKRLGVN-ENGGYDELKAHPFF 278
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
405-689 1.64e-84

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 269.77  E-value: 1.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILaLARKHPYLTQLYCCFQTKDRLFF 484
Cdd:PTZ00263   17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSIL-MELSHPFIVNMMCSFQDENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilngVT- 563
Cdd:PTZ00263   96 LLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VPd 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 -TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFM 642
Cdd:PTZ00263  171 rTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 643 TKNPHKRLGCVaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:PTZ00263  251 QTDHTKRLGTL--KGGVADVKNHPYFHGANWDKLYARYYPAPIPVRV 295
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
414-673 4.79e-83

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: 263.32  E-value: 4.79e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECN-SPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTFCGTPDY 573
Cdd:cd05572    80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTPEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 574 IAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDL--FESILH--DDVLYPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd05572   159 VAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMkiYNIILKgiDKIEFPKYIDKNAKNLIKQLLRRNPEER 238
                         250       260
                  ....*....|....*....|....
gi 1958782016 650 LGCVaaQNGEDAIKQHPFFKEIDW 673
Cdd:cd05572   239 LGYL--KGGIRDIKKHKWFEGFDW 260
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
407-689 1.55e-81

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: 261.78  E-value: 1.55e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLA-ELKGKD--EVYAVKVLKKDVILQDDD-VDCTMTEKRILALARKHPYLTQLYCCFQTKDRL 482
Cdd:cd05614     1 NFELLKVLGTGAYGKVFLVrKVSGHDanKLYAMKVLRKAALVQKAKtVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd05614    81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTT-TFCGTPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPF----EADNEDDLFESILHDDVLYPVWLSKEAVS 636
Cdd:cd05614   161 ERTySFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 637 ILKAFMTKNPHKRLGcvAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05614   241 LLQKLLCKDPKKRLG--AGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSI 291
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
406-689 2.97e-81

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR 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: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 261.01  E-value: 2.97e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05599     1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEA-DNPWVVKLYYSFQDEENLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKeGILNGVTTT 565
Cdd:cd05599    80 MEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHLAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH--DDVLYP--VWLSKEAVSILKAF 641
Cdd:cd05599   159 STVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNwrETLVFPpeVPISPEAKDLIERL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 642 MTkNPHKRLGcvaaQNGEDAIKQHPFFKEIDWVLLEQKkiKPPFKPRI 689
Cdd:cd05599   239 LC-DAEHRLG----ANGVEEIKSHPFFKGVDWDHIRER--PAPILPEV 279
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
3-135 3.89e-81

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 253.35  E-value: 3.89e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016   3 VFNGLLKIKICEAVSLKPTAWSLRHAVgPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELA 82
Cdd:cd04014     1 MFTGTLKIKICEAVDLKPTDWSTRHAV-PKKGSQLLDPYVSIDVDDTHIGKTSTKPKTNSPVWNEEFTTEVHNGRNLELT 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016  83 VFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSS 135
Cdd:cd04014    80 VFHDAAIGPDDFVANCTISFEDLIQRGSGSFDLWVDLEPQGKLHVKIELKGSA 132
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
413-671 4.34e-81

N-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: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 258.48  E-value: 4.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLA-ELKGKD--EVYAVKVLKKDVILQDDDV-DCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd05583     1 VLGTGAYGKVFLVrKVGGHDagKLYAMKVLKKATIVQKAKTaEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVT--TTT 566
Cdd:cd05583    81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKE-FLPGENdrAYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQ--ELEYGPSVDWWALGVLMYEMMAGQPPFEADNED----DLFESILHDDVLYPVWLSKEAVSILKA 640
Cdd:cd05583   160 FCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERnsqsEISKRILKSHPPIPKTFSAEAKDFILK 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 641 FMTKNPHKRLGCvaAQNGEDAIKQHPFFKEI 671
Cdd:cd05583   240 LLEKDPKKRLGA--GPRGAHEIKEHPFFKGL 268
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
407-669 1.39e-79

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: 253.94  E-value: 1.39e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14007     1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLR-HPNILRLYGYFEDKKRIYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGVTTTT 566
Cdd:cd14007    80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH--APSNRRKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNP 646
Cdd:cd14007   158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDP 237
                         250       260
                  ....*....|....*....|...
gi 1958782016 647 HKRLGCvaaqngeDAIKQHPFFK 669
Cdd:cd14007   238 SKRLSL-------EQVLNHPWIK 253
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
408-687 2.12e-79

N-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: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 254.93  E-value: 2.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLA-ELKGKD--EVYAVKVLKKDVILQD-DDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLF 483
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVrKVSGHDagKLYAMKVLKKATIVQKaKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TT-TFCGTPDYIAPEILQELEYG--PSVDWWALGVLMYEMMAGQPPFEADNED----DLFESILHDDVLYPVWLSKEAVS 636
Cdd:cd05613   162 RAySFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALAKD 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 637 ILKAFMTKNPHKRLGCvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05613   242 IIQRLLMKDPKKRLGC--GPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
406-689 9.47e-79

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: 253.13  E-value: 9.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILaLARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVL-KEVSHPFIIRLFWTEHDQRFLYML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNgvtTT 565
Cdd:cd05612    80 MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDR---TW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd05612   157 TLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVD 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 646 PHKRLGCVaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05612   237 RTRRLGNM--KNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKV 278
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
414-689 1.15e-78

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: 254.42  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRIL--ALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05586    81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV-WLSKEAVSILKAFMTKNPHKR 649
Cdd:cd05586   161 EYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958782016 650 LGCVAaqnGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05586   241 LGAHD---DAVELKEHPFFADIDWDLLSKKKITPPFKPIV 277
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
406-689 2.29e-77

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: 251.08  E-value: 2.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEA-DNEWVVKLYYSFQDKENLYFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCkegilngvttT 565
Cdd:cd05598    80 MDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC----------T 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TF--------------CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL---YP 627
Cdd:cd05598   150 GFrwthdskyylahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInWRTTLkipHE 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 628 VWLSKEAVSILKAFMTkNPHKRLGCvaaqNGEDAIKQHPFFKEIDWVLLEQKkiKPPFKPRI 689
Cdd:cd05598   230 ANLSPEAKDLILRLCC-DAEDRLGR----NGADEIKAHPFFAGIDWEKLRKQ--KAPYIPTI 284
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
410-667 4.23e-77

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: 247.43  E-value: 4.23e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCtMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd14003     4 LGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKI-KREIEIMKLLN-HPNIIKLYEVIETENKIYLVMEYA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTFCG 569
Cdd:cd14003    82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-FRGGSLLKTFCG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHK 648
Cdd:cd14003   161 TPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSK 240
                         250
                  ....*....|....*....
gi 1958782016 649 RLGCvaaqngeDAIKQHPF 667
Cdd:cd14003   241 RITI-------EEILNHPW 252
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
406-689 1.36e-76

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK 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: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 248.76  E-value: 1.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05601     1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKA-NSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQR-SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG-MCKEGILNGVT 563
Cdd:cd05601    80 MEYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGsAAKLSSDKTVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELE------YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL-YP--VWLSKE 633
Cdd:cd05601   160 SKMPVGTPDYIAPEVLTSMNggskgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnFKKFLkFPedPKVSES 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 634 AVSILKAFMTkNPHKRLgcvaaqnGEDAIKQHPFFKEIDWVLLEQKkiKPPFKPRI 689
Cdd:cd05601   240 AVDLIKGLLT-DAKERL-------GYEGLCCHPFFSGIDWNNLRQT--VPPFVPTL 285
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
408-668 2.98e-75

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: 242.55  E-value: 2.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILaLARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEIL-QELEHPFLVNLWYSFQDEEDMYMVVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG---MCKEGILngvtT 564
Cdd:cd05578    81 LLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNiatKLTDGTL----A 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEA---DNEDDLFESILHDDVLYPVWLSKEAVSILKAF 641
Cdd:cd05578   157 TSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIhsrTSIEEIRAKFETASVLYPAGWSEEAIDLINKL 236
                         250       260
                  ....*....|....*....|....*..
gi 1958782016 642 MTKNPHKRLGCVaaqngeDAIKQHPFF 668
Cdd:cd05578   237 LERDPQKRLGDL------SDLKNHPYF 257
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
411-673 4.68e-74

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: 239.69  E-value: 4.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGvTTTTFCGT 570
Cdd:cd05611    81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKR-HNKKFVGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAFMTKNP 646
Cdd:cd05611   160 PDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRLLCMDP 239
                         250       260
                  ....*....|....*....|....*..
gi 1958782016 647 HKRLGCvaaqNGEDAIKQHPFFKEIDW 673
Cdd:cd05611   240 AKRLGA----NGYQEIKSHPFFKSINW 262
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
408-667 6.65e-74

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: 238.92  E-value: 6.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE-EMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEgILNGVTT 564
Cdd:cd05117    80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEGEKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSILKA 640
Cdd:cd05117   159 KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFdsPEWknVSEEAKDLIKR 238
                         250       260
                  ....*....|....*....|....*..
gi 1958782016 641 FMTKNPHKRLgcVAAQngedaIKQHPF 667
Cdd:cd05117   239 LLVVDPKKRL--TAAE-----ALNHPW 258
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
406-689 6.55e-73

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-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: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 239.17  E-value: 6.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05597     1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDR-RWITKLHYAFQDENYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQrsrKFD----EPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd05597    80 MDYYCGGDLLTLLS---KFEdrlpEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 -VTTTTFCGTPDYIAPEILQELE-----YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVLYPVWL 630
Cdd:cd05597   157 tVQSSVAVGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNhkehfSFPDDEDDV 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 631 SKEAVSILKAFMTkNPHKRLGcvaaQNGEDAIKQHPFFKEIDWVLLeqKKIKPPFKPRI 689
Cdd:cd05597   237 SEEAKDLIRRLIC-SRERRLG----QNGIDDFKKHPFFEGIDWDNI--RDSTPPYIPEV 288
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
414-687 8.63e-73

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: 237.04  E-value: 8.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSS-PFIVSLAYAFETKDKLCLVLTLMNGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTFCGTP 571
Cdd:cd05577    80 LKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVGTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPFEADNE----DDLFESILHDDVLYPVWLSKEAVSILKAFMTKNP 646
Cdd:cd05577   159 GYMAPEVLQkEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEkvdkEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 647 HKRLGCVaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05577   239 ERRLGCR--GGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
392-689 1.96e-72

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK 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: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 238.43  E-value: 1.96e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 392 NGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQ 471
Cdd:cd05596    12 EKPVNEITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANS-EWIVQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 472 LYCCFQTKDRLFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADF 551
Cdd:cd05596    91 LHYAFQDDKYLYMVMDYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 552 GMCKEGILNG-VTTTTFCGTPDYIAPEILQ----ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL 625
Cdd:cd05596   170 GTCMKMDKDGlVRSDTAVGTPDYISPEVLKsqggDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnHKNSL 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 626 -YP--VWLSKEAVSILKAFMTKNPHkRLGcvaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05596   250 qFPddVEISKDAKSLICAFLTDREV-RLG----RNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPEL 311
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
406-687 5.22e-69

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: 227.46  E-value: 5.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILAlaRKHP-YLTQLYCCFQTKDRLFF 484
Cdd:cd05608     1 DWFLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILA--KVHSrFIVSLAYAFQTKTDLCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQI----QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN 560
Cdd:cd05608    79 VMTIMNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE----DDLFESILHDDVLYPVWLSKEAVS 636
Cdd:cd05608   159 QTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEkvenKELKQRILNDSVTYSEKFSPASKS 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 637 ILKAFMTKNPHKRLGcvaAQNGE-DAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05608   239 ICEALLAKDPEKRLG---FRDGNcDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
407-673 1.13e-68

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: 226.13  E-value: 1.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05609     1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFA-ENPFVVSMYCSFETKRHLCMVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT--- 563
Cdd:cd05609    80 EYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTnly 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 -------TTTF-----CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV--- 628
Cdd:cd05609   160 eghiekdTREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEgdd 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 629 WLSKEAVSILKAFMTKNPHKRLGCVAAQNgedaIKQHPFFKEIDW 673
Cdd:cd05609   240 ALPDDAQDLITRLLQQNPLERLGTGGAEE----VKQHPFFQDLDW 280
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
408-687 6.52e-68

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: 224.16  E-value: 6.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05605     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNS-RFVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTT 565
Cdd:cd05605    81 IMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGETIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE----DDLFESILHDDVLYPVWLSKEAVSILKAF 641
Cdd:cd05605   160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 642 MTKNPHKRLGCVaAQNGEDaIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05605   240 LQKDPKTRLGCR-GEGAED-VKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
402-689 2.69e-67

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: 226.07  E-value: 2.69e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDR 481
Cdd:cd05600     7 RLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTT-NSPWLVKLLYAFQDPEN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGI--- 558
Cdd:cd05600    86 VYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLspk 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 --------LNGVTTTTF--------------------------CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQ 604
Cdd:cd05600   166 kiesmkirLEEVKNTAFleltakerrniyramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGF 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 605 PPFEADNEDDLFESILH----------DDVLYPVWLSKEAVSILKAFMTkNPHKRLgcvaaQNGEDaIKQHPFFKEIDWV 674
Cdd:cd05600   246 PPFSGSTPNETWANLYHwkktlqrpvyTDPDLEFNLSDEAWDLITKLIT-DPQDRL-----QSPEQ-IKNHPFFKNIDWD 318
                         330
                  ....*....|....*
gi 1958782016 675 LLeQKKIKPPFKPRI 689
Cdd:cd05600   319 RL-REGSKPPFIPEL 332
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
408-687 7.14e-65

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: 216.40  E-value: 7.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHpYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSR-FVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTT 565
Cdd:cd05631    81 IMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGETVR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE----DDLFESILHDDVLYPVWLSKEAVSILKAF 641
Cdd:cd05631   160 GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICRML 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 642 MTKNPHKRLGCvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05631   240 LTKNPKERLGC--RGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
405-688 9.68e-63

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL 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: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 212.82  E-value: 9.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05610     3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALS-KSPFIVHLYYSLQSANNVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--------- 555
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnrelnm 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EGILN-------------------------GVTTTT-------------------FCGTPDYIAPEILQELEYGPSVDWW 591
Cdd:cd05610   162 MDILTtpsmakpkndysrtpgqvlslisslGFNTPTpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWW 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 592 ALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVW---LSKEAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd05610   242 ALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGeeeLSVNAQNAIEILLTMDPTKRAGL-------KELKQHPLF 314
                         330       340
                  ....*....|....*....|
gi 1958782016 669 KEIDWVLLEQKkiKPPFKPR 688
Cdd:cd05610   315 HGVDWENLQNQ--TMPFIPQ 332
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
402-689 1.91e-62

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 213.72  E-value: 1.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHpYLTQLYCCFQTKDR 481
Cdd:cd05624    68 QLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQ-WITTLHYAFQDENY 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQR-SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN 560
Cdd:cd05624   147 LYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDD 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 G-VTTTTFCGTPDYIAPEILQELE-----YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL-YPVWL-- 630
Cdd:cd05624   227 GtVQSSVAVGTPDYISPEILQAMEdgmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnHEERFqFPSHVtd 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 631 -SKEAVSILKAFMTKNpHKRLGcvaaQNGEDAIKQHPFFKEIDWVLLeqKKIKPPFKPRI 689
Cdd:cd05624   307 vSEEAKDLIQRLICSR-ERRLG----QNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDV 359
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
394-693 4.55e-62

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 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: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 211.78  E-value: 4.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 394 EVRQGQAKRlglDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLY 473
Cdd:cd05621    43 KIRELQMKA---EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS-PWVVQLF 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 474 CCFQTKDRLFFVMEYVNGGDLmfqIQRSRKFDEPR--SRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADF 551
Cdd:cd05621   119 CAFQDDKYLYMVMEYMPGGDL---VNLMSNYDVPEkwAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 552 GMCKEGILNG-VTTTTFCGTPDYIAPEILQ----ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL 625
Cdd:cd05621   196 GTCMKMDETGmVHCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdHKNSL 275
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 626 -YP--VWLSKEAVSILKAFMTkNPHKRLGcvaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIFASV 693
Cdd:cd05621   276 nFPddVEISKHAKNLICAFLT-DREVRLG----RNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDI 341
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
402-688 6.20e-62

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 210.22  E-value: 6.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKD-EVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKD 480
Cdd:PTZ00426   26 KMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKQVDHVFSERKILNYI-NHPFCVNLYGSFKDES 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegiLN 560
Cdd:PTZ00426  105 YLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK---VV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA 640
Cdd:PTZ00426  182 DTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKK 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 641 FMTKNPHKRLGCVaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPR 688
Cdd:PTZ00426  262 LLSHDLTKRYGNL--KKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPK 307
Pkinase pfam00069
Protein kinase domain;
408-668 4.37e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 203.63  E-value: 4.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVME 487
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLN-HPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEvtsalmflhqhgviyrdlkldnILldaeghckladfgmckEGILNGVTTTTF 567
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQ----------------------IL----------------EGLESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVW---LSKEAVSILKAFMTK 644
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|....
gi 1958782016 645 NPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:pfam00069 201 DPSKRLTA-------TQALQHPWF 217
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
406-687 5.89e-61

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: 206.75  E-value: 5.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHpYLTQLYCCFQTKDRLFFV 485
Cdd:cd05632     2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQ-FVVNLAYAYETKDALCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVT 563
Cdd:cd05632    81 LTIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE----DDLFESILHDDVLYPVWLSKEAVSILK 639
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 640 AFMTKNPHKRLGCvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05632   240 MLLTKDPKQRLGC--QEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
406-689 7.66e-61

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR 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: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 208.55  E-value: 7.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLA-ESDSPWVVSLYYSFQDAQYLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK---------- 555
Cdd:cd05629    80 MEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsay 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 -----EGILNGVTTTTF--------------------------------CGTPDYIAPEILQELEYGPSVDWWALGVLMY 598
Cdd:cd05629   160 yqkllQGKSNKNRIDNRnsvavdsinltmsskdqiatwkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 599 EMMAGQPPFEADNEDDLFESILH--DDVLYP--VWLSKEAVSILKAFMTkNPHKRLGcvaaQNGEDAIKQHPFFKEIDWV 674
Cdd:cd05629   240 ECLIGWPPFCSENSHETYRKIINwrETLYFPddIHLSVEAEDLIRRLIT-NAENRLG----RGGAHEIKSHPFFRGVDWD 314
                         330
                  ....*....|....*
gi 1958782016 675 LLEQkkIKPPFKPRI 689
Cdd:cd05629   315 TIRQ--IRAPFIPQL 327
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
412-667 2.19e-60

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: 203.02  E-value: 2.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14663     6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLR-HPNIVELHEVMATKTKIFFVMELVTG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC--KEGILNGVTTTTFCG 569
Cdd:cd14663    85 GELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDGLLHTTCG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHK 648
Cdd:cd14663   165 TPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPNPST 244
                         250
                  ....*....|....*....
gi 1958782016 649 RLGCVaaqngedAIKQHPF 667
Cdd:cd14663   245 RITVE-------QIMASPW 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
408-687 2.45e-60

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: 204.10  E-value: 2.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHpYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSR-FVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTT 565
Cdd:cd05630    81 LMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQTIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI--LHDDVL--YPVWLSKEAVSILKAF 641
Cdd:cd05630   160 GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVerLVKEVPeeYSEKFSPQARSLCSML 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 642 MTKNPHKRLGCVAAqnGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05630   240 LCKDPAERLGCRGG--GAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
402-689 3.21e-60

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 207.95  E-value: 3.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHpYLTQLYCCFQTKDR 481
Cdd:cd05623    68 RLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQ-WITTLHYAFQDDNN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQR-SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN 560
Cdd:cd05623   147 LYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMED 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 G-VTTTTFCGTPDYIAPEILQELE-----YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH--DDVLYPVWL-- 630
Cdd:cd05623   227 GtVQSSVAVGTPDYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNhkERFQFPTQVtd 306
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 631 -SKEAVSILKAFMTKNPHkRLGcvaaQNGEDAIKQHPFFKEIDWVLLeqKKIKPPFKPRI 689
Cdd:cd05623   307 vSENAKDLIRRLICSREH-RLG----QNGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEV 359
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
408-687 8.83e-60

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. 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 GRK7 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: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 202.83  E-value: 8.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05607     4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNS-PFIVSLAYAFETKTHLCLVMS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTT 565
Cdd:cd05607    83 LMNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKPIT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF----EADNEDDLFESILHDDVLY--PVWlSKEAVSILK 639
Cdd:cd05607   162 QRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrdhkEKVSKEELKRRTLEDEVKFehQNF-TEEAKDICR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 640 AFMTKNPHKRLGcvaAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05607   241 LFLAKKPENRLG---SRTNDDDPRKHEFFKSINFPRLEAGLIDPPFVP 285
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
411-649 6.49e-59

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 206.40  E-value: 6.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:COG0515    12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDGRPYLVMEYVE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT-TTTFCG 569
Cdd:COG0515    91 GESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTqTGTVVG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL--------YPVWLskEAVsILKAf 641
Cdd:COG0515   171 TPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPppselrpdLPPAL--DAI-VLRA- 246

                  ....*...
gi 1958782016 642 MTKNPHKR 649
Cdd:COG0515   247 LAKDPEER 254
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
402-689 7.14e-59

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 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: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 204.08  E-value: 7.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDR 481
Cdd:cd05622    69 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS-PWVVQLFYAFQDDRY 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC----KEG 557
Cdd:cd05622   148 LYMVMEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEG 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 IlngVTTTTFCGTPDYIAPEILQ----ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-HDDVL-YP--VW 629
Cdd:cd05622   227 M---VRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnHKNSLtFPddND 303
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 630 LSKEAVSILKAFMTkNPHKRLGcvaaQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRI 689
Cdd:cd05622   304 ISKEAKNLICAFLT-DREVRLG----RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDL 358
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
411-649 9.35e-59

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: 198.84  E-value: 9.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKV--LKKdviLQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd08215     5 IRVIGKGSFGSAYLVRRKSDGKLYVLKEidLSN---MSEKEREEALNEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRK----FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVT- 563
Cdd:cd08215    81 ADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK--VLESTTd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 -TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDvlY---PVWLSKEAVSILK 639
Cdd:cd08215   159 lAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQ--YppiPSQYSSELRDLVN 236
                         250
                  ....*....|
gi 1958782016 640 AFMTKNPHKR 649
Cdd:cd08215   237 SMLQKDPEKR 246
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
414-623 2.04e-57

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: 193.64  E-value: 2.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVIlqDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLN-HPNIVKLYDVFETENFLYLVMEYCEGGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LM-FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EGILNGVTTTTFCGT 570
Cdd:cd00180    78 LKdLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGTTP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMmagqPPFEadnedDLFESILHDD 623
Cdd:cd00180   158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL----EELK-----DLIRRMLQYD 201
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
407-668 8.90e-57

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: 193.57  E-value: 8.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLK------KDVILQdddvdctmtEKRILALArKHPYLTQLYCCFQTKD 480
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINleskekKESILN---------EIAILKKC-KHPNIVKYYGSYLKKD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMfQI--QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgI 558
Cdd:cd05122    71 ELWIVMEFCSGGSLK-DLlkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-L 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV---LYPVWLSKEAV 635
Cdd:cd05122   149 SDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPpglRNPKKWSKEFK 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958782016 636 SILKAFMTKNPHKRlgCVAAQngedaIKQHPFF 668
Cdd:cd05122   229 DFLKKCLQKDPEKR--PTAEQ-----LLKHPFI 254
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
412-668 2.50e-56

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: 192.35  E-value: 2.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdVDCTMTEKRIL-ALarKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEE-LEALEREIRILsSL--KHPNIVRYLGTERTENTLNIFLEYVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EGILNGVTTTTFC 568
Cdd:cd06606    83 GGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKSLR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLFESILHDDVL--YPVWLSKEAVSILKAFMTKN 645
Cdd:cd06606   163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGEPppIPEHLSEEAKDFLRKCLQRD 242
                         250       260
                  ....*....|....*....|...
gi 1958782016 646 PHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd06606   243 PKKRPTA-------DELLQHPFL 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
411-649 1.30e-55

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: 190.49  E-value: 1.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd14014     5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPE--LAEDEEFRERFLREARALARlSHPNIVRVYDVGEDDGRPYIVMEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT-TFC 568
Cdd:cd14014    83 EGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTgSVL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV----LYPVWLSKEAVSILKAFMTK 644
Cdd:cd14014   163 GTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVPPALDAIILRALAK 242

                  ....*
gi 1958782016 645 NPHKR 649
Cdd:cd14014   243 DPEER 247
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
408-649 1.45e-55

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: 190.29  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMS-SLNHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC----KEGILngvt 563
Cdd:cd14073    82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSnlysKDKLL---- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 tTTFCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSkEAVSILKAFM 642
Cdd:cd14073   158 -QTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWML 235

                  ....*..
gi 1958782016 643 TKNPHKR 649
Cdd:cd14073   236 TVNPKRR 242
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
406-667 2.36e-55

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: 189.38  E-value: 2.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilqdddvdcTMTEKRILALAR--------KHPYLTQLYCCFQ 477
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKR----------GKSEKELRNLRQeieilrklNHPNIIEMLDSFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 478 TKDRLFFVMEYVNGgDLmFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 556
Cdd:cd14002    71 TKKEFVVVTEYAQG-EL-FQIlEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 GILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVS 636
Cdd:cd14002   149 MSCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKS 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 637 ILKAFMTKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14002   229 FLQGLLNKDPSKRLSW-------PDLLEHPF 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
414-668 3.30e-54

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: 186.99  E-value: 3.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKD------VILQDDDVDCTMTE--KRILALARK--HPYLTQLYCCF--QTKDR 481
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSrlrkrrEGKNDRGKIKNALDdvRREIAIMKKldHPNIVRLYEVIddPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMF--QIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegIL 559
Cdd:cd14008    81 LYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE--MF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTFC--GTPDYIAPEILQELEY---GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH--DDVLYPVWLSK 632
Cdd:cd14008   159 EDGNDTLQKtaGTPAFLAPELCDGDSKtysGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNqnDEFPIPPELSP 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958782016 633 EAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14008   239 ELKDLLRRMLEKDPEKRITL-------KEIKEHPWV 267
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
412-668 4.26e-54

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: 186.22  E-value: 4.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14099     7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLK-HPNIVKFHDCFEDEENVYILLELCSN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd14099    86 GSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELE-YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP--VWLSKEAVSILKAFMTKNPHK 648
Cdd:cd14099   166 NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPshLSISDEAKDLIRSMLQPDPTK 245
                         250       260
                  ....*....|....*....|
gi 1958782016 649 RLGCvaaqngeDAIKQHPFF 668
Cdd:cd14099   246 RPSL-------DEILSHPFF 258
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
408-689 1.41e-53

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 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: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 189.07  E-value: 1.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEA-DNEWVVKLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC------------K 555
Cdd:cd05626    82 YIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCtgfrwthnskyyQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EG------------ILNGVTTT-----------------------TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEM 600
Cdd:cd05626   162 KGshirqdsmepsdLWDDVSNCrcgdrlktleqratkqhqrclahSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 601 MAGQPPFEADNEDDL------FESILHddVLYPVWLSKEAVSILKAFMTKNPHkRLGcvaaQNGEDAIKQHPFFKEIDWV 674
Cdd:cd05626   242 LVGQPPFLAPTPTETqlkvinWENTLH--IPPQVKLSPEAVDLITKLCCSAEE-RLG----RNGADDIKAHPFFSEVDFS 314
                         330
                  ....*....|....*
gi 1958782016 675 lLEQKKIKPPFKPRI 689
Cdd:cd05626   315 -SDIRTQPAPYVPKI 328
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
405-673 1.53e-52

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 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: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 185.65  E-value: 1.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05627     1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEA-DGAWVVKMFYSFQDKRNLYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGVTT 564
Cdd:cd05627    80 IMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTG--LKKAHR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTF-------------------------------------CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd05627   158 TEFyrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPF 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 608 EADNEDDLFESILH--DDVLYP--VWLSKEAVSILKAFMTkNPHKRLGcvaaQNGEDAIKQHPFFKEIDW 673
Cdd:cd05627   238 CSETPQETYRKVMNwkETLVFPpeVPISEKAKDLILRFCT-DAENRIG----SNGVEEIKSHPFFEGVDW 302
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
413-687 2.96e-50

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. 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 beta-ARK 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: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 176.47  E-value: 2.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKH---PYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGgdcPFIVCMTYAFQTPDKLCFILDLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGVTTTTFCG 569
Cdd:cd05606    81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACD--FSKKKPHASVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFE---SILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd05606   159 THGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEidrMTLTMNVELPDSFSPELKSLLEGLLQRD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 646 PHKRLGCVAaqNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05606   239 VSKRLGCLG--RGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
407-650 4.04e-50

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: 175.59  E-value: 4.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvdctMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEH----MIENEVAILRRvKHPNIVQLIEEYDTDTELYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL----DAEGHCKLADFGM---CKEGI 558
Cdd:cd14095    77 MELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLateVKEPL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LngvtttTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF--EADNEDDLFESILHDDV--LYPVW--LSK 632
Cdd:cd14095   157 F------TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEFefLSPYWdnISD 230
                         250
                  ....*....|....*...
gi 1958782016 633 EAVSILKAFMTKNPHKRL 650
Cdd:cd14095   231 SAKDLISRMLVVDPEKRY 248
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
408-668 5.43e-50

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: 175.45  E-value: 5.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELK--GKDEVYAVKVLKKDvILQDDDVdctmtEK---RILALARK--HPYLTQLYCCFQTKD 480
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTksGLKEKVACKIIDKK-KAPKDFL-----EKflpRELEILRKlrHPNIIQVYSIFERGS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG---MCKEG 557
Cdd:cd14080    76 KVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarLCPDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 iLNGVTTTTFCGTPDYIAPEILQELEYGPSV-DWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP---VWLSKE 633
Cdd:cd14080   156 -DGDVLSKTFCGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPE 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 634 AVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14080   235 CKDLIDQLLEPDPTKRATI-------EEILNHPWL 262
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
408-649 1.01e-49

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: 174.25  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAE--LKGKDevYAVKVLKKdVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARhvLTGRE--VAIKIIDK-TQLNPSSLQKLFREVRIMKIL-NHPNIVKLFEVIETEKTLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLM-FQIQRSR-KFDEPRSRFyaAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILnGVT 563
Cdd:cd14072    78 MEYASGGEVFdYLVAHGRmKEKEARAKF--RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTP-GNK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFM 642
Cdd:cd14072   155 LDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFL 234

                  ....*..
gi 1958782016 643 TKNPHKR 649
Cdd:cd14072   235 VLNPSKR 241
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
408-689 3.61e-49

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 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: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 176.78  E-value: 3.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEA-DNEWVVRLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC------------- 554
Cdd:cd05625    82 YIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 -----KEGILN-----GVTTTTFC------------------------GTPDYIAPEILQELEYGPSVDWWALGVLMYEM 600
Cdd:cd05625   162 sgdhlRQDSMDfsnewGDPENCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 601 MAGQPPFEADNEDDL------FESILHddVLYPVWLSKEAvSILKAFMTKNPHKRLGcvaaQNGEDAIKQHPFFKEIDWV 674
Cdd:cd05625   242 LVGQPPFLAQTPLETqmkvinWQTSLH--IPPQAKLSPEA-SDLIIKLCRGPEDRLG----KNGADEIKAHPFFKTIDFS 314
                         330
                  ....*....|....*
gi 1958782016 675 lLEQKKIKPPFKPRI 689
Cdd:cd05625   315 -SDLRQQSAPYIPKI 328
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
405-650 8.71e-49

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: 172.06  E-value: 8.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDViLQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14116     4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQ-LEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGilNGVTT 564
Cdd:cd14116    83 ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHA--PSSRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTK 644
Cdd:cd14116   161 TTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKH 240

                  ....*.
gi 1958782016 645 NPHKRL 650
Cdd:cd14116   241 NPSQRP 246
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
412-668 9.88e-49

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: 171.68  E-value: 9.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14079     8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFR-HPHIIRLYEVIETPTDIFMVMEYVSG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGmckegiLNGVTT-----TT 566
Cdd:cd14079    87 GELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFG------LSNIMRdgeflKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd14079   161 SCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVD 240
                         250       260
                  ....*....|....*....|...
gi 1958782016 646 PHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14079   241 PLKRITI-------PEIRQHPWF 256
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
161-224 2.58e-48

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 163.79  E-value: 2.58e-48
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 161 RRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLK 224
Cdd:cd20835     1 RRRVHQVNGHKFMATYLRQPTYCSHCKDFIWGVIGKQGYQCQVCTCVVHKRCHQLVVTKCPGNK 64
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
412-668 2.59e-48

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: 170.51  E-value: 2.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14081     7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIE-HPNVLKLYDVYENKKYLYLVLEYVSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM---CKEGILngvtTTTFC 568
Cdd:cd14081    86 GELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMaslQPEGSL----LETSC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPH 647
Cdd:cd14081   162 GSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPE 241
                         250       260
                  ....*....|....*....|.
gi 1958782016 648 KRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14081   242 KRITI-------EEIKKHPWF 255
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
414-651 2.89e-48

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: 170.10  E-value: 2.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDViLQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKK-LNKKLQENLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEgILNGVTTTTFCGT 570
Cdd:cd14009    79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARS-LQPASMAETLCGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAFMTKNP 646
Cdd:cd14009   158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPfpiaAQLSPDCKDLLRRLLRRDP 237

                  ....*
gi 1958782016 647 HKRLG 651
Cdd:cd14009   238 AERIS 242
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
406-673 3.61e-48

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 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: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 174.07  E-value: 3.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEA-DSLWVVKMFYSFQDKLNLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKeGI------- 558
Cdd:cd05628    80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT-GLkkahrte 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 ----LNGVTTTTF-------------------------CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEA 609
Cdd:cd05628   159 fyrnLNHSLPSDFtfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 610 DNEDDLFESILH--DDVLYP--VWLSKEAVSILKAFMTKNPHkRLGCvaaqNGEDAIKQHPFFKEIDW 673
Cdd:cd05628   239 ETPQETYKKVMNwkETLIFPpeVPISEKAKDLILRFCCEWEH-RIGA----PGVEEIKTNPFFEGVDW 301
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
414-650 1.82e-47

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: 168.33  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVIlqDDDVDCTMTEkrILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14078    11 IGSGGFAKVKLATHILTGEKVAIKIMDKKAL--GDDLPRVKTE--IEALKNlSHQHICRLYHVIETDNKIFMVLEYCPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC---KEGILNGVTTTtfCG 569
Cdd:cd14078    87 ELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCakpKGGMDHHLETC--CG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHK 648
Cdd:cd14078   165 SPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKK 244

                  ..
gi 1958782016 649 RL 650
Cdd:cd14078   245 RI 246
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
414-649 2.41e-47

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: 167.33  E-value: 2.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDeVyAVKVLKKDViLQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd13999     1 IGSGSFGEVYKGKWRGTD-V-AIKKLKVED-DNDELLKEFRREVSILSKLR-HPNIVQFIGACLSPPPLCIVTEYMPGGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQ-RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPD 572
Cdd:cd13999    77 LYDLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 573 YIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLFESILHDDVLY-PVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd13999   157 WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFkELSPIQIAAAVVQKGLRPPiPPDCPPELSKLIKRCWNEDPEKR 235
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
414-650 4.58e-47

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: 167.13  E-value: 4.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLA-ELKGKDEVyAVKVLKKDVIlqdDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14075    10 LGSGNFSQVKLGiHQLTKEKV-AIKILDKTKL---DQKTQRLLSREISSMEKlHHPNIIRLYEVVETLSKLHLVMEYASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG---MCKEG-ILNgvtttTF 567
Cdd:cd14075    86 GELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKRGeTLN-----TF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNP 646
Cdd:cd14075   161 CGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVP 240

                  ....
gi 1958782016 647 HKRL 650
Cdd:cd14075   241 SDRY 244
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
406-667 4.73e-47

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: 167.51  E-value: 4.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdcTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE----TSIENEIAVLHKiKHPNIVALDDIYESGGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL---LDAEGHCKLADFGMCK-EGilN 560
Cdd:cd14167    79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKiEG--S 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVS 636
Cdd:cd14167   157 GSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFdsPYWddISDSAKD 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 637 ILKAFMTKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14167   237 FIQHLMEKDPEKRFTC-------EQALQHPW 260
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
401-684 1.02e-46

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: 166.58  E-value: 1.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 401 KRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKD 480
Cdd:cd14117     1 RKFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLR-HPNILRLYNYFHDRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGilN 560
Cdd:cd14117    80 RIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHA--P 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKA 640
Cdd:cd14117   158 SLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISK 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 641 FMTKNPHKRLGCVaaqngedAIKQHPffkeidWVLLEQKKIKPP 684
Cdd:cd14117   238 LLRYHPSERLPLK-------GVMEHP------WVKANSRRVLPP 268
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
406-655 1.80e-46

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: 165.62  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvdctMTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKED----SLENEIAVLRKiKHPNIVQLLDIYESKSHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL---LDAEGHCKLADFGMCK---EGI 558
Cdd:cd14083    79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKmedSGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LngvttTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEA 634
Cdd:cd14083   159 M-----STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFdsPYWddISDSA 233
                         250       260
                  ....*....|....*....|.
gi 1958782016 635 VSILKAFMTKNPHKRLGCVAA 655
Cdd:cd14083   234 KDFIRHLMEKDPNKRYTCEQA 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
414-667 1.86e-46

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: 165.93  E-value: 1.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVL---KKDVILQdddvdctmtEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKCVdksKRPEVLN---------EVRLTH-ELKHPNVLKFYEWYETSNHLWLVVEYCT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM---------------CK 555
Cdd:cd14010    78 GGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLarregeilkelfgqfSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EGILNGVTT-TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVW----- 629
Cdd:cd14010   158 EGNVNKVSKkQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPkvssk 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 630 LSKEAVSILKAFMTKNPHKRLgcvaaqnGEDAIKQHPF 667
Cdd:cd14010   238 PSPDFKSLLKGLLEKDPAKRL-------SWDELVKHPF 268
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
403-687 8.33e-46

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. 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 GRK3 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: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 166.39  E-value: 8.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 403 LGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKH--PYLTQLYCCFQTKD 480
Cdd:cd05633     2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMTYAFHTPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLN 560
Cdd:cd05633    82 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACD--FS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFE---SILHDDVLYPVWLSKEAVS 636
Cdd:cd05633   160 KKKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDSFSPELKS 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 637 ILKAFMTKNPHKRLGCVAAqnGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd05633   240 LLEGLLQRDVSKRLGCHGR--GAQEVKEHSFFKGIDWQQVYLQKYPPPLIP 288
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
410-651 1.15e-45

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: 163.77  E-value: 1.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKGKDEVYAVKVL---------KKDVILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQT 478
Cdd:cd14077     5 FVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkKEREKRLEKEISRDIRTIREAALSSllNHPHICRLRDFLRT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC---- 554
Cdd:cd14077    85 PNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSnlyd 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KEGILNgvtttTFCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKE 633
Cdd:cd14077   165 PRRLLR-----TFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSE 239
                         250
                  ....*....|....*...
gi 1958782016 634 AVSILKAFMTKNPHKRLG 651
Cdd:cd14077   240 CKSLISRMLVVDPKKRAT 257
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
408-649 1.28e-45

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: 163.20  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMS-SLNHPHIISVYEVFENSSKIVIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMckEGILNGVT-TTT 566
Cdd:cd14161    83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL--SNLYNQDKfLQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSkEAVSILKAFMTKN 645
Cdd:cd14161   161 YCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLMVN 239

                  ....
gi 1958782016 646 PHKR 649
Cdd:cd14161   240 PERR 243
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
407-687 2.46e-45

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. 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. TheGRK2 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: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 164.45  E-value: 2.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKH--PYLTQLYCCFQTKDRLFF 484
Cdd:cd14223     1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMSYAFHTPDKLSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGVTT 564
Cdd:cd14223    81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACD--FSKKKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFE---SILHDDVLYPVWLSKEAVSILKA 640
Cdd:cd14223   159 HASVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTMAVELPDSFSPELRSLLEG 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 641 FMTKNPHKRLGCVAaqNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKP 687
Cdd:cd14223   239 LLQRDVNRRLGCMG--RGAQEVKEEPFFRGLDWQMVFLQKYPPPLIP 283
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
412-650 1.22e-44

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: 161.02  E-value: 1.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDV-----ILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14084    12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsRREINKPRNIETEIEILK-KLSHPCIIKIEDFFDAEDDYYIVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-DAEGHC--KLADFGMCKegIL-NGV 562
Cdd:cd14084    91 ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLsSQEEECliKITDFGLSK--ILgETS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQ---ELEYGPSVDWWALGVLMYEMMAGQPPFEADNED-DLFESILHDDVLY--PVW--LSKEA 634
Cdd:cd14084   169 LMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQmSLKEQILSGKYTFipKAWknVSEEA 248
                         250
                  ....*....|....*.
gi 1958782016 635 VSILKAFMTKNPHKRL 650
Cdd:cd14084   249 KDLVKKMLVVDPSRRP 264
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
408-666 1.48e-44

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: 160.25  E-value: 1.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDcTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKERED-SVNEIRLLA-SVNHPNIIRYKEAFLDGNRLCIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRK----FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVT 563
Cdd:cd08530    80 YAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLKKNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYPVWlSKEAVSILKAF 641
Cdd:cd08530   158 AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGkfPPIPPVY-SQDLQQIIRSL 236
                         250       260
                  ....*....|....*....|....*
gi 1958782016 642 MTKNPHKRLGCvaaqngeDAIKQHP 666
Cdd:cd08530   237 LQVNPKKRPSC-------DKLLQSP 254
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
408-667 4.05e-44

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: 160.16  E-value: 4.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVdctmtEKRILALAR-KHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSL-----ENEIAVLKRiKHENIVTLEDIYESTTHYYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGHCKL--ADFGMCKEGiLNGVT 563
Cdd:cd14166    80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKImiTDFGLSKME-QNGIM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSILK 639
Cdd:cd14166   159 STA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFesPFWddISESAKDFIR 237
                         250       260
                  ....*....|....*....|....*...
gi 1958782016 640 AFMTKNPHKRLGCvaaqngEDAIKqHPF 667
Cdd:cd14166   238 HLLEKNPSKRYTC------EKALS-HPW 258
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
408-668 4.40e-44

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: 159.03  E-value: 4.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKV--LKKDVILQDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdMKRAPGDCPENIKKEVCIQKML----SHKNVVRFYGHRREGEFQYLF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC-------KEGI 558
Cdd:cd14069    79 LEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfrykgKERL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LNGVttttfCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD--VLYPVW--LSKE 633
Cdd:cd14069   159 LNKM-----CGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENkkTYLTPWkkIDTA 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 634 AVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14069   234 ALSLLRKILTENPNKRITI-------EDIKKHPWY 261
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
407-667 2.31e-43

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: 157.25  E-value: 2.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVK-VLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqIVKRKVAGNDKNLQLFQREINILK-SLEHPGIVRLIDWYEDDQHIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG--HCKLADFGMCKEgILNGVT 563
Cdd:cd14098    80 MEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV-IHTGTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELE------YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI----LHDDVLYPVWLSKE 633
Cdd:cd14098   159 LVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIrkgrYTQPPLVDFNISEE 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958782016 634 AVSILKAFMTKNPHKRLgcVAAQngedaIKQHPF 667
Cdd:cd14098   239 AIDFILRLLDVDPEKRM--TAAQ-----ALDHPW 265
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
408-668 5.23e-43

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: 155.63  E-value: 5.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELK-GKDEVyAVKVLKKDViLQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRiTKTEV-AIKIIDKSQ-LDEENLKKIYREVQIMKMLN-HPHIIKLYQVMETKDMLYLVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMcKEGILNGVTTTT 566
Cdd:cd14071    79 EYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF-SNFFKPGELLKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd14071   158 WCGSPPYAAPEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLD 237
                         250       260
                  ....*....|....*....|...
gi 1958782016 646 PHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14071   238 PSKRLTI-------EQIKKHKWM 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
412-655 9.78e-43

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: 155.36  E-value: 9.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVM--LAELKGkdEVYAVKVLKKDVILQDDDVDCTMT-EKRILALARkHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd14070     8 RKLGEGSFAKVRegLHAVTG--EKVAIKVIDKKKAKKDSYVTKNLRrEGRIQQMIR-HPNITQLLDILETENSYYLVMEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTT--TT 566
Cdd:cd14070    85 CPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDpfST 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEAD--NEDDLFESILHDDV-LYPVWLSKEAVSILKAFMT 643
Cdd:cd14070   165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMnPLPTDLSPGAISFLRSLLE 244
                         250
                  ....*....|..
gi 1958782016 644 KNPHKRLGCVAA 655
Cdd:cd14070   245 PDPLKRPNIKQA 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
408-669 1.44e-42

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: 154.68  E-value: 1.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVlkkdVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKK----MRLRKQNKELIINEILIMK-ECKHPNIVDYYDSYLVGDELWVVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTT 566
Cdd:cd06614    77 YMDGGSLTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP-FEADNEDDLFESILHD--DVLYPVWLSKEAVSILKAFMT 643
Cdd:cd06614   157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFLITTKGipPLKNPEKWSPEFKDFLNKCLV 236
                         250       260
                  ....*....|....*....|....*.
gi 1958782016 644 KNPHKRLGCvaaqngEDAIkQHPFFK 669
Cdd:cd06614   237 KDPEKRPSA------EELL-QHPFLK 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
412-649 4.06e-42

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: 153.57  E-value: 4.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvdctMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd14185     6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKED----MIESEILIIKSlSHPNIVKLFEVYETEKEIYLILEYVR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL----DAEGHCKLADFGMCKEgilngVTTTT 566
Cdd:cd14185    82 GGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKY-----VTGPI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 F--CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEAD--NEDDLFESIL--HDDVLYPVW--LSKEAVSIL 638
Cdd:cd14185   157 FtvCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQlgHYEFLPPYWdnISEAAKDLI 236
                         250
                  ....*....|.
gi 1958782016 639 KAFMTKNPHKR 649
Cdd:cd14185   237 SRLLVVDPEKR 247
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
408-649 4.92e-42

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: 153.31  E-value: 4.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILqdddVDCTMTEKR---------ILALARK--HPYLTQLYCCF 476
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIL----VDTWVRDRKlgtvpleihILDTLNKrsHPNIVKLLDFF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 477 QTKDRLFFVME-YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG--- 552
Cdd:cd14004    78 EDDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGsaa 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 553 MCKEGILNgvtttTFCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEAdneddlFESILHDDVLYPVWLS 631
Cdd:cd14004   158 YIKSGPFD-----TFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYN------IEEILEADLRIPYAVS 226
                         250
                  ....*....|....*...
gi 1958782016 632 KEAVSILKAFMTKNPHKR 649
Cdd:cd14004   227 EDLIDLISRMLNRDVGDR 244
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
406-667 6.66e-42

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: 152.71  E-value: 6.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAE-LKGKDEVyAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARsLHTGLEV-AIKMIDKKAMQKAGMVQRVRNEVEIHC-QLKHPSILELYNYFEDSNYVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQ-RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd14186    79 VLEMCHNGEMSRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMT 643
Cdd:cd14186   159 HFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLR 238
                         250       260
                  ....*....|....*....|....
gi 1958782016 644 KNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14186   239 KNPADRLSL-------SSVLDHPF 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
406-672 1.61e-41

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: 151.98  E-value: 1.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvILQDDDVDCTM-TEKRILALArKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH---VDGDEEFRKQLlRELKTLRSC-ESPYVVKCYGAFYKEGEISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQ-HGVIYRDLKLDNILLDAEGHCKLADFGMCKeGILNGVT 563
Cdd:cd06623    77 VLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISK-VLENTLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 -TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH--DDVLYPvwLSKEAVSI-LK 639
Cdd:cd06623   156 qCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAicDGPPPS--LPAEEFSPeFR 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958782016 640 AFMT----KNPHKRLgcVAAQngedaIKQHPFFKEID 672
Cdd:cd06623   234 DFISaclqKDPKKRP--SAAE-----LLQHPFIKKAD 263
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
407-649 3.48e-41

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: 151.15  E-value: 3.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilqdddvdcTMTEK---------RILalaR--KHPYLTQLYCC 475
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYG----------KMSEKekqqlvsevNIL---RelKHPNIVRYYDR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 476 FQTKD--RLFFVMEYVNGGDLMFQIQRSRK----FDEPRSRFYAAEVTSALMFLH-----QHGVIYRDLKLDNILLDAEG 544
Cdd:cd08217    68 IVDRAntTLYIVMEYCEGGDLAQLIKKCKKenqyIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 545 HCKLADFGMCKegILNGVT--TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDL------- 615
Cdd:cd08217   148 NVKLGDFGLAR--VLSHDSsfAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELakkikeg 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 616 -FESIlhddvlyPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd08217   226 kFPRI-------PSRYSSELNEVIKSMLNVDPDKR 253
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
413-668 1.37e-40

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: 149.81  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVL-----KKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14093    10 ILGRGVSSTVRRCIEKETGQEFAVKIIditgeKSSENEAEELREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTF 567
Cdd:cd14093    90 LCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR-LDEGEKLREL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQ-----ELE-YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSI 637
Cdd:cd14093   169 CGTPGYLAPEVLKcsmydNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFgsPEWddISDTAKDL 248
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 638 LKAFMTKNPHKRLgcvaaqNGEDAIkQHPFF 668
Cdd:cd14093   249 ISKLLVVDPKKRL------TAEEAL-EHPFF 272
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
408-668 1.70e-40

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: 148.98  E-value: 1.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGL-KHPNLICFYEAIETTSRVYIIME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG----VT 563
Cdd:cd14162    81 LAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKdgkpKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSV-DWWALGVLMYEMMAGQPPFEADNEDDLFESIlHDDVLYP--VWLSKEAVSILKA 640
Cdd:cd14162   161 SETYCGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPknPTVSEECKDLILR 239
                         250       260
                  ....*....|....*....|....*...
gi 1958782016 641 FMTKNPhKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14162   240 MLSPVK-KRITI-------EEIKRDPWF 259
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
414-667 1.73e-40

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: 149.66  E-value: 1.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdcTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14169    11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKE----AMVENEIAVLRRiNHENIVSLEDIYESPTHLYLAMELVTGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDA---EGHCKLADFGMCKegILNGVTTTTFCG 569
Cdd:cd14169    87 ELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK--IEAQGMLSTACG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSILKAFMTKN 645
Cdd:cd14169   165 TPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFdsPYWddISESAKDFIRHLLERD 244
                         250       260
                  ....*....|....*....|..
gi 1958782016 646 PHKRLGCvaaqngEDAIkQHPF 667
Cdd:cd14169   245 PEKRFTC------EQAL-QHPW 259
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
408-655 1.12e-39

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: 148.27  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdcTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKE----SSIENEIAVLRKiKHENIVALEDIYESPNHLYLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCK-EGilNGV 562
Cdd:cd14168    88 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKmEG--KGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSIL 638
Cdd:cd14168   166 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFdsPYWddISDSAKDFI 245
                         250
                  ....*....|....*..
gi 1958782016 639 KAFMTKNPHKRLGCVAA 655
Cdd:cd14168   246 RNLMEKDPNKRYTCEQA 262
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
406-606 2.76e-39

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: 146.24  E-value: 2.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLkkDVILQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVI--DLEEAEDEIEDIQQEIQFLSQCDS-PYITKYYGSFLKGSKLWII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGG---DLMfqiqRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd06609    78 MEYCGGGsvlDLL----KPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP 606
Cdd:cd06609   154 KRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPP 197
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
412-668 2.90e-39

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: 145.54  E-value: 2.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVIL---QDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSkphQREKIDKEIELHRIL----HHKHVVQFYHYFEDKENIYILLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd14188    83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTIC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHK 648
Cdd:cd14188   163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPED 242
                         250       260
                  ....*....|....*....|
gi 1958782016 649 RLGCvaaqngeDAIKQHPFF 668
Cdd:cd14188   243 RPSL-------DEIIRHDFF 255
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
417-669 5.35e-39

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 145.00  E-value: 5.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 417 GSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdctmtEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMF 496
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAI--------EPMVHQLMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 497 QIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLD-AEGHCKLADFGMCK-EGilngvTTTTFCGTPDYI 574
Cdd:PHA03390   99 LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKiIG-----TPSCYDGTLDYF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 575 APEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD----DVLYPVWLSKEAVSILKAFMTKNPHKRL 650
Cdd:PHA03390  174 SPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKrqqkKLPFIKNVSKNANDFVQSMLKYNINYRL 253
                         250
                  ....*....|....*....
gi 1958782016 651 gcvaaqNGEDAIKQHPFFK 669
Cdd:PHA03390  254 ------TNYNEIIKHPFLK 266
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
414-668 9.47e-39

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: 143.90  E-value: 9.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMlaelKGKD----EVYAVKVLKKDVILQDDDVDCtMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd06627     8 IGRGAFGSVY----KGLNlntgEFVAIKQISLEKIPKSDLKSV-MGEIDLLK-KLNHPNIVKYIGSVKTKDSLYIILEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCG 569
Cdd:cd06627    82 ENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP-FEADNEDDLFEsILHDDvlYPVwLSKEAVSILKAFMT----K 644
Cdd:cd06627   162 TPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyYDLQPMAALFR-IVQDD--HPP-LPENISPELRDFLLqcfqK 237
                         250       260
                  ....*....|....*....|....
gi 1958782016 645 NPHKRlgcVAAQngedAIKQHPFF 668
Cdd:cd06627   238 DPTLR---PSAK----ELLKHPWL 254
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
414-666 1.41e-38

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: 143.18  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKdvilQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPK----RDKKKEAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILELCSGGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLD--AEGHCKLADFGMCKEgILNGVTTTTFCGTP 571
Cdd:cd14006    76 LLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARK-LNPGEELKEIFGTP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV----LYPVWLSKEAVSILKAFMTKNPH 647
Cdd:cd14006   155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVdfseEYFSSVSQEAKDFIRKLLVKEPR 234
                         250
                  ....*....|....*....
gi 1958782016 648 KRLgCVaaqngEDAIkQHP 666
Cdd:cd14006   235 KRP-TA-----QEAL-QHP 246
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
407-649 1.90e-38

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: 143.32  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVK---VLKKDVILQDDDVDctmtEKRILALARkHPYLTQLYCCFQTKDRLF 483
Cdd:cd08529     1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKqidISRMSRKMREEAID----EARVLSKLN-SPYVIKYYDSFVDKGKLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDL--MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd08529    76 IVMEYAENGDLhsLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL-YPVWLSKEAVSILKA 640
Cdd:cd08529   156 NFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDS 235

                  ....*....
gi 1958782016 641 FMTKNPHKR 649
Cdd:cd08529   236 CLTKDYRQR 244
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
407-670 4.45e-38

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: 143.16  E-value: 4.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDctmtekrILALARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIE-------ILLRYGQHPNIITLRDVYDDGNSVYLVT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-DAEGH---CKLADFGMCKE-----G 557
Cdd:cd14091    74 ELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQlraenG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILngvttTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeADNEDDLFESILHD------DVLYPVW-- 629
Cdd:cd14091   154 LL-----MTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILARigsgkiDLSGGNWdh 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 630 LSKEAVSILKAFMTKNPHKRlgCVAAQngedaIKQHPFFKE 670
Cdd:cd14091   228 VSDSAKDLVRKMLHVDPSQR--PTAAQ-----VLQHPWIRN 261
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
412-667 4.63e-38

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: 142.16  E-value: 4.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVlkkdVILQDDDVDCTMT----EKRILALAR-KHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKE----VSLVDDDKKSRESvkqlEQEIALLSKlRHPNIVQYYGTEREEDNLYIFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTT 566
Cdd:cd06632    82 EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEIL--QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV--WLSKEAVSILKAFM 642
Cdd:cd06632   161 FKGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIpdHLSPDAKDFIRLCL 240
                         250       260
                  ....*....|....*....|....*
gi 1958782016 643 TKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd06632   241 QRDPEDRPTA-------SQLLEHPF 258
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
408-668 1.05e-37

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: 141.90  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDDDvDCtMTEKRILALAR--KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKK--FYSWE-EC-MNLREVKSLRKlnEHPNIVKLKEVFRENDELYFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGdlMFQIQRSRK---FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGV 562
Cdd:cd07830    77 FEYMEGN--LYQLMKDRKgkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLARE-IRSRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILhdDVL----YPVWL------- 630
Cdd:cd07830   154 PYTDYVSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKIC--SVLgtptKQDWPegyklas 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 631 ---------------------SKEAVSILKAFMTKNPHKRlgCVAAQngedaIKQHPFF 668
Cdd:cd07830   232 klgfrfpqfaptslhqlipnaSPEAIDLIKDMLRWDPKKR--PTASQ-----ALQHPYF 283
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
413-655 1.64e-37

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: 140.75  E-value: 1.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqdDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14087     8 LIGRGSFSRVVRVEHRVTRQPYAIKMIETKC----RGREVCESELNVLRRVR-HTNIIQLIEVFETKERVYMVMELATGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH---CKLADFGMC---KEGILNGVTTTt 566
Cdd:cd14087    83 ELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLAstrKKGPNCLMKTT- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 fCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSILKAFM 642
Cdd:cd14087   162 -CGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsgEPWpsVSNLAKDFIDRLL 240
                         250
                  ....*....|...
gi 1958782016 643 TKNPHKRLGCVAA 655
Cdd:cd14087   241 TVNPGERLSATQA 253
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
414-618 2.06e-37

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: 140.52  E-value: 2.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDE--VYAVKVLKKDvilqDDDVDCTMTEKRILA---LARK--HPYLTQLYCCFQT-KDRLFFV 485
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSgvLYAVKEYRRR----DDESKRKDYVKRLTSeyiISSKlhHPNIVKVLDLCQDlHGKWCLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC-KEGILNGVTT 564
Cdd:cd13994    77 MEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKES 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 565 TTF---CGTPDYIAPEILQELEYGP-SVDWWALGVLMYEMMAGQPPFE-ADNEDDLFES 618
Cdd:cd13994   157 PMSaglCGSEPYMAPEVFTSGSYDGrAVDVWSCGIVLFALFTGRFPWRsAKKSDSAYKA 215
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
406-682 2.38e-37

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: 141.03  E-value: 2.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVlkkdVILQD-DDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKI----IQIESeEELEDFMVEIDILSEC-KHPNIVGLYEAYFYENKLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGG---DLMFQIQRSrkFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd06611    80 LIEFCDGGaldSIMLELERG--LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEIL-----QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD---VLYPVWLSKE 633
Cdd:cd06611   158 QKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 634 AVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFFKEIDwvllEQKKIK 682
Cdd:cd06611   238 FNDFLKSCLVKDPDDRPTA-------AELLKHPFVSDQS----DNKAIK 275
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
241-295 2.91e-37

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; 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. 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 132.78  E-value: 2.91e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 241 MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:cd20838     1 VPHRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNCGVN 55
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
408-667 6.99e-37

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: 139.05  E-value: 6.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIK--VLGKGSFGKVMLAELKGKDEVYAVK--VLKKDVILQDDDVDCTMTE--KRILALAR--KHPYLTQLYCCFQTK 479
Cdd:cd06629     1 FKWVKgeLIGKGTYGRVYLAMNATTGEMLAVKqvELPKTSSDRADSRQKTVVDalKSEIDTLKdlDHPNIVQYLGFEETE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EG 557
Cdd:cd06629    81 DYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKksDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTFCGTPDYIAPEILQELE--YGPSVDWWALGVLMYEMMAGQPPFeadNEDDLFESILH-----------DDV 624
Cdd:cd06629   161 IYGNNGATSMQGSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFKlgnkrsappvpEDV 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 625 LypvwLSKEAVSILKAFMTKNPHKRlgCVAAQngedaIKQHPF 667
Cdd:cd06629   238 N----LSPEALDFLNACFAIDPRDR--PTAAE-----LLSHPF 269
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
410-649 1.05e-36

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: 138.45  E-value: 1.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  410 FIKVLGKGSFGKVMLAELKGKD-----EVyAVKVLKKDVILQD-DDVdctMTEKRILALArKHPYLTQLY-CCFQtKDRL 482
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTLKGKGdgkevEV-AVKTLKEDASEQQiEEF---LREARIMRKL-DHPNIVKLLgVCTE-EEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRF--YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILN 560
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKELSLSDLlsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD-LYD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  561 GVTTTTFCGT-P-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLY-PVWLSKEAVS 636
Cdd:smart00221 156 DDYYKVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLPkPPNCPPELYK 235
                          250
                   ....*....|...
gi 1958782016  637 ILKAFMTKNPHKR 649
Cdd:smart00221 236 LMLQCWAEDPEDR 248
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
407-649 1.64e-36

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: 139.11  E-value: 1.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLA-ELKGKDEVYAVKVLKKDVIlqDDDVDCTMTEKRIL---ALARK--HPYLTQLYCCFQTKD 480
Cdd:cd14096     2 NYRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVRKADL--SSDNLKGSSRANILkevQIMKRlsHPNIVKLLDFQESDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDA------------------ 542
Cdd:cd14096    80 YYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkadddet 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 543 ---EGH------------CKLADFGMCKegILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd14096   160 kvdEGEfipgvggggigiVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 608 EADNEDDLFESILHDD--VLYPVW--LSKEAVSILKAFMTKNPHKR 649
Cdd:cd14096   238 YDESIETLTEKISRGDytFLSPWWdeISKSAKDLISHLLTVDPAKR 283
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
406-670 1.69e-36

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: 138.80  E-value: 1.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqddDVDCTMTEKRILaLARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14085     3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV-----DKKIVRTEIGVL-LRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH---CKLADFGMCKEgILNGV 562
Cdd:cd14085    77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKI-VDQQV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD-LFESILHDDVLY--PVW--LSKEAVSI 637
Cdd:cd14085   156 TMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRILNCDYDFvsPWWddVSLNAKDL 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958782016 638 LKAFMTKNPHKRLGCVAAQngedaikQHPFFKE 670
Cdd:cd14085   236 VKKLIVLDPKKRLTTQQAL-------QHPWVTG 261
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
414-668 1.93e-36

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: 137.39  E-value: 1.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVmlaelkgkDEV--------YAVKVLKKDVILQ----DDDVdctmteKRILALARK--HPYLTQLYCCFQT- 478
Cdd:cd14119     1 LGEGSYGKV--------KEVldtetlcrRAVKILKKRKLRRipngEANV------KREIQILRRlnHRNVIKLVDVLYNe 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 -KDRLFFVMEYVNGG-DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 556
Cdd:cd14119    67 eKQKLYMVMEYCVGGlQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 --GILNGVTTTTFCGTPDYIAPEILQELEY--GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSK 632
Cdd:cd14119   147 ldLFAEDDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDP 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958782016 633 EAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14119   227 DLQDLLRGMLEKDPEKRFTI-------EQIRQHPWF 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
414-667 2.19e-36

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: 138.00  E-value: 2.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVML------AELKGKDEVyAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14076     9 LGEGEFGKVKLgwplpkANHRSGVQV-AIKLIRRDTQQENCQTSKIMREINILK-GLTHPNIVRLLDVLKTKKYIGIVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE-GILNGVTTTT 566
Cdd:cd14076    87 FVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDLMST 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPE--ILQELEYGPSVDWWALGVLMYEMMAGQPPF-------EADNEDDLFESILHDDVLYPVWLSKEAVSI 637
Cdd:cd14076   167 SCGSPCYAAPElvVSDSMYAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKARDL 246
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958782016 638 LKAFMTKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14076   247 LRRILVPNPRKRIRL-------SAIMRHAW 269
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
408-650 2.33e-36

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: 137.68  E-value: 2.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINRE---KAGSSAVKLLEREVDILKHvNHAHIIHLEEVFETPKRMYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG-------HCKLADFGMC-KEGI 558
Cdd:cd14097    80 ELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvQKYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP--VW--LSKEA 634
Cdd:cd14097   160 LGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsVWqsVSDAA 239
                         250
                  ....*....|....*.
gi 1958782016 635 VSILKAFMTKNPHKRL 650
Cdd:cd14097   240 KNVLQQLLKVDPAHRM 255
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
408-668 2.64e-36

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: 138.00  E-value: 2.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilQDDDVDCT-MTEKRILaLARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDN--EEEGIPSTaLREISLL-KELKHPNIVKLLDVIHTENKLYLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGgDL-MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd07829    78 EYCDQ-DLkKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD-LFE--SIL---------------HDDVLY 626
Cdd:cd07829   157 HEVVTLWYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDqLFKifQILgtpteeswpgvtklpDYKPTF 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 627 PVW-----------LSKEAVSILKAFMTKNPHKRLGCvaaqngEDAIKqHPFF 668
Cdd:cd07829   237 PKWpkndlekvlprLDPEGIDLLSKMLQYNPAKRISA------KEALK-HPYF 282
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
412-649 2.99e-36

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: 137.29  E-value: 2.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKD----EVyAVKVLKKDviLQDDDVDCTMTEKRILALArKHPYLTQLY-CCFQtKDRLFFVM 486
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDgktvDV-AVKTLKED--ASESERKDFLKEARVMKKL-GHPNVVRLLgVCTE-EEPLYLVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSR-KFDEPRSRF--------YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG 557
Cdd:cd00192    76 EYMEGGDLLDFLRKSRpVFPSPEPSTlslkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTfCGTPDYI---APEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLY-PVWLSK 632
Cdd:cd00192   156 YDDDYYRKK-TGGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKGYRLPkPENCPD 234
                         250
                  ....*....|....*..
gi 1958782016 633 EAVSILKAFMTKNPHKR 649
Cdd:cd00192   235 ELYELMLSCWQLDPEDR 251
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
411-668 3.07e-36

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: 136.60  E-value: 3.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilqddDVDCTMTEKRILAL-----ARKHPYLTQLYCCF--QTKDRLF 483
Cdd:cd05118     4 LRKIGEGAFGTVWLARDKVTGEKVAIKKIKND------FRHPKAALREIKLLkhlndVEGHPNIVKLLDVFehRGGNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVnGGDLMFQIQ-RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLD-AEGHCKLADFGMCKegILNG 561
Cdd:cd05118    78 LVFELM-GMNLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLAR--SFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILhdDVLYPvwlsKEAVSILKA 640
Cdd:cd05118   155 PPYTPYVATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV--RLLGT----PEALDLLSK 228
                         250       260
                  ....*....|....*....|....*...
gi 1958782016 641 FMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd05118   229 MLKYDPAKRITA-------SQALAHPYF 249
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
406-667 3.35e-36

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: 137.09  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvdctMTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEH----LIENEVSILRRvKHPNIIMLIEEMDTPAELYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL----DAEGHCKLADFGMCK--EGI 558
Cdd:cd14184    77 VMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATvvEGP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LngvttTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN--EDDLFESIL--HDDVLYPVW--LSK 632
Cdd:cd14184   157 L-----YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILlgKLEFPSPYWdnITD 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 633 EAVSILKAFMTKNPHKRlgCVAAQngedaIKQHPF 667
Cdd:cd14184   232 SAKELISHMLQVNVEAR--YTAEQ-----ILSHPW 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
414-650 3.53e-36

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: 136.65  E-value: 3.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELK-GKDEVYAVKVLKKDViLQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14121     3 LGSGTYATVYKAYRKsGAREVVAVKCVSKSS-LNKASTENLLTEIELLKKLK-HPHIVELKDFQWDEEHIYLIMEYCSGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG--HCKLADFGMCKEgILNGVTTTTFCGT 570
Cdd:cd14121    81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQH-LKPNDEAHSLRGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD-VLYP--VWLSKEAVSILKAFMTKNPH 647
Cdd:cd14121   160 PLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPtrPELSADCRDLLLRLLQRDPD 239

                  ...
gi 1958782016 648 KRL 650
Cdd:cd14121   240 RRI 242
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
407-668 3.80e-36

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: 136.67  E-value: 3.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDvDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK----LEPGD-DFEIIQQEISMLKEcRHPNIVAYFGSYLRRDKLWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilngVTTT 565
Cdd:cd06613    76 MEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQ-----LTAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 -----TFCGTPDYIAPEILQELE---YGPSVDWWALGVLMYEMMAGQPPfeadneddLFEsiLHD-DVLYPV-------- 628
Cdd:cd06613   151 iakrkSFIGTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAELQPP--------MFD--LHPmRALFLIpksnfdpp 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 629 -------WlSKEAVSILKAFMTKNPHKRlgcvaaqNGEDAIKQHPFF 668
Cdd:cd06613   221 klkdkekW-SPDFHDFIKKCLTKNPKKR-------PTATKLLQHPFV 259
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
408-611 3.81e-36

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: 136.63  E-value: 3.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAelkgKDEVYAVKVLKKDVILQDDDV-DCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLA----KAKSDSEHCVIKEIDLTKMPVkEKEASKKEVILLAKmKHPNIVTFFASFQENGRLFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRK--FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH-CKLADFGMCKegILNGV 562
Cdd:cd08225    78 MEYCDGGDLMKRINRQRGvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMvAKLGDFGIAR--QLNDS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 563 T--TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd08225   156 MelAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNN 206
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
408-667 4.70e-36

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: 136.39  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVIlqdDDVDCT--MTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DDVSKAhlFQEVRCMKLV-QHPNVVRLYEVIDTQTKLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQR-SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-DAEGHCKLADFGMCKEgILNGVT 563
Cdd:cd14074    81 LELGDGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNK-FQPGEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFM 642
Cdd:cd14074   160 LETSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRML 239
                         250       260
                  ....*....|....*....|....*
gi 1958782016 643 TKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14074   240 IRDPKKRASL-------EEIENHPW 257
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
410-649 7.76e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 135.74  E-value: 7.76e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  410 FIKVLGKGSFGKVMLAELKGKD-----EVyAVKVLKKDVILQD-DDVdctMTEKRILALArKHPYLTQLY-CCFQtKDRL 482
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKGKGgkkkvEV-AVKTLKEDASEQQiEEF---LREARIMRKL-DHPNVVKLLgVCTE-EEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRF-YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:smart00219  77 YIVMEYMEGGDLLSYLRKNRPKLSLSDLLsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  562 VTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLY-PVWLSKEAVSIL 638
Cdd:smart00219 157 YYRKRGGKLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLPqPPNCPPELYDLM 236
                          250
                   ....*....|.
gi 1958782016  639 KAFMTKNPHKR 649
Cdd:smart00219 237 LQCWAEDPEDR 247
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
414-649 1.20e-35

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: 135.53  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVdctmTEKRI-LALArKHPYLTQLY-CCFQTKDRLFFVMEYVNG 491
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFL----REYNIsLELS-VHPHIIKTYdVAFETEDYYVFAQEYAPY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-DAE-GHCKLADFGMCKEgilNGVTTTTFCG 569
Cdd:cd13987    76 GDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTRR---VGSTVKRVSG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYG-----PSVDWWALGVLMYEMMAGQPPFE-ADNEDDLFESILH-----DDVLYPVW--LSKEAVS 636
Cdd:cd13987   153 TIPYTAPEVCEAKKNEgfvvdPSIDVWAFGVLLFCCLTGNFPWEkADSDDQFYEEFVRwqkrkNTAVPSQWrrFTPKALR 232
                         250
                  ....*....|...
gi 1958782016 637 ILKAFMTKNPHKR 649
Cdd:cd13987   233 MFKKLLAPEPERR 245
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
406-607 1.23e-35

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: 135.09  E-value: 1.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdctmTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd06612     3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQE-------IIKEISILKQcDSPYIVKYYGSYFKNTDLWI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGG---DLMfQIqRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMckEGILNG 561
Cdd:cd06612    76 VMEYCGAGsvsDIM-KI-TNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGV--SGQLTD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 562 VT--TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06612   152 TMakRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY 199
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
407-649 1.68e-35

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: 134.72  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIR----LPKSSSAVEDSRKEAVLLAKmKHPNIVAFKESFEADGHLYIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQI--QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd08219    77 MEYCDGGDLMQKIklQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL-YPVWLSKEAVSILKAFM 642
Cdd:cd08219   157 ACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMF 236

                  ....*..
gi 1958782016 643 TKNPHKR 649
Cdd:cd08219   237 KRNPRSR 243
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
414-674 2.23e-35

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: 135.18  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVIL-----------QDDDVDCTMTEK------RILALARK--HPYLTQLYC 474
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLkqagffrrpppRRKPGALGKPLDpldrvyREIAILKKldHPNVVKLVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 475 CFQ--TKDRLFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG 552
Cdd:cd14118    82 VLDdpNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 553 MCKEGILNGVTTTTFCGTPDYIAPEILQELEY---GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP-- 627
Cdd:cd14118   161 VSNEFEGDDALLSSTAGTPAFMAPEALSESRKkfsGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPdd 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 628 VWLSKEAVSILKAFMTKNPHKRLgcVAAQngedaIKQHPffkeidWV 674
Cdd:cd14118   241 PVVSEQLKDLILRMLDKNPSERI--TLPE-----IKEHP------WV 274
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
406-674 2.44e-35

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: 135.63  E-value: 2.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVL--KKdviLQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLF 483
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIIntKK---LSARDHQKLEREARICRLL-KHPNIVRLHDSISEEGFHY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEGILN 560
Cdd:cd14086    77 LVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV--W--LSKEAVS 636
Cdd:cd14086   157 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpeWdtVTPEAKD 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 637 ILKAFMTKNPHKRLGCVAAQngedaikQHPFFKEIDWV 674
Cdd:cd14086   237 LINQMLTVNPAKRITAAEAL-------KHPWICQRDRV 267
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
406-668 2.48e-35

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: 135.52  E-value: 2.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKdvILQDDDV-DCTMTEKRILALARkHPYLTQLYCCFQTKDRLFF 484
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKE--SEDDEDVkKTALREVKVLRQLR-HENIVNLKEAFRRKGRLYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVnGGDLMFQIQRSRK-FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGVT 563
Cdd:cd07833    78 VFEYV-ERTLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARA--LTARP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 T---TTFCGTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD------------------LFES--- 618
Cdd:cd07833   155 AsplTDYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDqlyliqkclgplppshqeLFSSnpr 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 619 --------ILHDDVL---YPVWLSKEAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd07833   235 fagvafpePSQPESLerrYPGKVSSPALDFLKACLRMDPKERLTC-------DELLQHPYF 288
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
402-670 2.52e-35

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: 135.89  E-value: 2.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDEfnfiKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqdddvDCtMTEKRILALARKHPYLTQLYCCFQTKDR 481
Cdd:cd14092     6 ELDLRE----EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL-------DT-SREVQLLRLCQGHPNIVKLHEVFQDELH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG---HCKLADFGMCKEGI 558
Cdd:cd14092    74 TYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFARLKP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LNGVTTTTfCGTPDYIAPEILQEL----EYGPSVDWWALGVLMYEMMAGQPPFEADNED----DLFESILHDDVLY--PV 628
Cdd:cd14092   154 ENQPLKTP-CFTLPYAAPEVLKQAlstqGYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFdgEE 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 629 W--LSKEAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFFKE 670
Cdd:cd14092   233 WknVSSEAKSLIQGLLTVDPSKRLTM-------SELRNHPWLQG 269
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
412-649 3.13e-35

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: 134.29  E-value: 3.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVM-LAELKGKdEVYAVKVLKKDVILQDDDVDCTMTEkriLALARK--HPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd14187    13 RFLGKGGFAKCYeITDADTK-EVFAGKIVPKSLLLKPHQKEKMSME---IAIHRSlaHQHVVGFHGFFEDNDFVYVVLEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd14187    89 CRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHK 648
Cdd:cd14187   169 GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA 248

                  .
gi 1958782016 649 R 649
Cdd:cd14187   249 R 249
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
412-668 6.22e-35

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: 133.13  E-value: 6.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEkriLALAR--KHPYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd14189     7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNE---IELHRdlHHKHVVKFSHHFEDAENIYIFLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCG 569
Cdd:cd14189    84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd14189   164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDR 243
                         250
                  ....*....|....*....
gi 1958782016 650 LGCvaaqngeDAIKQHPFF 668
Cdd:cd14189   244 LTL-------DQILEHEFF 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
410-613 1.47e-34

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 132.24  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKGKDEVY----AVKVLKKDVilQDDDVDCTMTEKRILALARkHPYLTQLY-CCFQTKDrLFF 484
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEGA--DEEEREDFLEEASIMKKLD-HPNIVKLLgVCTQGEP-LYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLM-FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVT 563
Cdd:pfam07714  79 VTEYMPGGDLLdFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD-IYDDDY 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 564 TTTFCGTPD---YIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEA-DNED 613
Cdd:pfam07714 158 YRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGmSNEE 212
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
406-607 2.04e-34

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: 132.10  E-value: 2.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLkkDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRI--DLEKCQTSMDELRKEIQAMSQC-NHPNVVSYYTSFVVGDELWLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGG---DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG----MCKEGI 558
Cdd:cd06610    78 MPLLSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGvsasLATGGD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LNGVTTTTFCGTPDYIAPEILQELE-YGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06610   158 RTRKVRKTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPY 207
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
402-669 5.27e-34

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: 130.64  E-value: 5.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDefNFIKVlGKGSFGKVMLAELKGKDEVYAVKvlKKDVILQdddvdctmtEKRIL-----ALAR--KHPYLTQLYC 474
Cdd:cd06648     6 RSDLD--NFVKI-GEGSTGIVCIATDKSTGRQVAVK--KMDLRKQ---------QRRELlfnevVIMRdyQHPNIVEMYS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 475 CFQTKDRLFFVMEYVNGGDLMFQIQRSRkFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC 554
Cdd:cd06648    72 SYLVGDELWVVMEFLEGGALTDIVTHTR-MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFC 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD---VLYPVWLS 631
Cdd:cd06648   151 AQVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEppkLKNLHKVS 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 632 KEAVSILKAFMTKNPHKRlgCVAAQngedaIKQHPFFK 669
Cdd:cd06648   231 PRLRSFLDRMLVRDPAQR--ATAAE-----LLNHPFLA 261
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
412-650 1.20e-33

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: 131.32  E-value: 1.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQdddvdcTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14179    13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEAN------TQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG---HCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd14179    87 GELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFARLKPPDNQPLKTPC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE-------DDLFESILHDDVLY--PVW--LSKEAVSI 637
Cdd:cd14179   167 FTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKsltctsaEEIMKKIKQGDFSFegEAWknVSQEAKDL 246
                         250
                  ....*....|...
gi 1958782016 638 LKAFMTKNPHKRL 650
Cdd:cd14179   247 IQGLLTVDPNKRI 259
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
411-667 1.52e-33

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: 129.47  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVI--LQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd08222     5 VRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLS-KLDHPAIVKFHDSFVEKESFCIVTEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQI----QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDaEGHCKLADFGMCKegILNGVT- 563
Cdd:cd08222    84 CEGGDLDDKIseykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK-NNVIKVGDFGISR--ILMGTSd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 -TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV-LYPVWLSKEAVSILKAF 641
Cdd:cd08222   161 lATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRM 240
                         250       260
                  ....*....|....*....|....*.
gi 1958782016 642 MTKNPHKRLGCVaaqngedAIKQHPF 667
Cdd:cd08222   241 LNKDPALRPSAA-------EILKIPF 259
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
408-650 2.40e-33

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: 128.95  E-value: 2.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILqDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKI-DENVQREIINHRSL----RHPNIVRFKEVILTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG--HCKLADFGMCKEGILNGVTTT 565
Cdd:cd14665    77 YAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TfCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYP----VWLSKEAVSIL 638
Cdd:cd14665   157 T-VGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRilSVQYSipdyVHISPECRHLI 235
                         250
                  ....*....|..
gi 1958782016 639 KAFMTKNPHKRL 650
Cdd:cd14665   236 SRIFVADPATRI 247
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
408-671 3.00e-33

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: 129.54  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKvlKkdvILQDddvdctmteKR-------ILaLARKHPYLTQLYCCFQTKD 480
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIK--K---VLQD---------KRyknrelqIM-RRLKHPNIVKLKYFFYSSG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 R------LFFVMEYVNggDLMFQIqrSRKFDEPRSRF-------YAAEVTSALMFLHQHGVIYRDLKLDNILLDAE-GHC 546
Cdd:cd14137    71 EkkdevyLNLVMEYMP--ETLYRV--IRHYSKNKQTIpiiyvklYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 547 KLADFGMCKEgILNGVTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH---- 621
Cdd:cd14137   147 KLCDFGSAKR-LVPGEPNVSYICSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKvlgt 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 622 ---DDV----------------------LYPVWLSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFFKEI 671
Cdd:cd14137   226 ptrEQIkamnpnytefkfpqikphpwekVFPKRTPPDAIDLLSKILVYNPSKRL------TALEAL-AHPFFDEL 293
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
407-649 3.09e-33

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: 128.27  E-value: 3.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKP-FRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRS---RKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCkegilngVT 563
Cdd:cd13997    80 ELCENGSLQDALEELspiSKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA-------TR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFC----GTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQP-PFEADNEDDLFESILHDdvLYPVWLSKEAVSI 637
Cdd:cd13997   153 LETSGdveeGDSRYLAPELLNEnYTHLPKADIFSLGVTVYEAATGEPlPRNGQQWQQLRQGKLPL--PPGLVLSQELTRL 230
                         250
                  ....*....|..
gi 1958782016 638 LKAFMTKNPHKR 649
Cdd:cd13997   231 LKVMLDPDPTRR 242
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
406-669 3.83e-33

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: 128.23  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDV-------ILQDDDVdctmtekrilaLARKH-PYLTQLYCCFQ 477
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIdealqkqILRELDV-----------LHKCNsPYIVGFYGAFY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 478 TKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLH-QHGVIYRDLKLDNILLDAEGHCKLADFGMckE 556
Cdd:cd06605    70 SEGDISICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGV--S 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 GILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNED------DLFESILHDD--VLYPV 628
Cdd:cd06605   148 GQLVDSLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEPppLLPSG 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 629 WLSKEAVSILKAFMTKNPHKRlgcvaaqNGEDAIKQHPFFK 669
Cdd:cd06605   228 KFSPDFQDFVSQCLQKDPTER-------PSYKELMEHPFIK 261
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
414-668 3.89e-33

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: 128.36  E-value: 3.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLA-ELKGKDEVyAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKD-RLFFVMEYVNG 491
Cdd:cd14165     9 LGEGSYAKVKSAySERLKCNV-AIKIIDKKKAPDDFVEKFLPRELEILARLN-HKSIIKTYEIFETSDgKVYIVMELGVQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG----VTTTTF 567
Cdd:cd14165    87 GDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEngriVLSKTF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQELEYGPSV-DWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP--VWLSKEAVSILKAFMTK 644
Cdd:cd14165   167 CGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPrsKNLTSECKDLIYRLLQP 246
                         250       260
                  ....*....|....*....|....
gi 1958782016 645 NPHKRLgCVaaqngeDAIKQHPFF 668
Cdd:cd14165   247 DVSQRL-CI------DEVLSHPWL 263
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
414-650 1.78e-32

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: 126.33  E-value: 1.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGK-DEVYAVKVLKKDVILQDDdvdcTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKpDLPVAIKCITKKNLSKSQ----NLLGKEIKILKElSHENVVALLDCQETSSSVYLVMEYCNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC---------KLADFGMCKegILN-G 561
Cdd:cd14120    77 GDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRkpspndirlKIADFGFAR--FLQdG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDL---FESILHDDVLYPVWLSKEAVSIL 638
Cdd:cd14120   155 MMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPSGTSPALKDLL 234
                         250
                  ....*....|..
gi 1958782016 639 KAFMTKNPHKRL 650
Cdd:cd14120   235 LGLLKRNPKDRI 246
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
406-667 2.00e-32

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: 126.65  E-value: 2.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLkkDVILqdDDVDCTMTEKRILALARKHPYLTQLYCCFQTK------ 479
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIM--DIIE--DEEEEIKLEINILRKFSNHPNIATFYGAFIKKdppggd 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAA----EVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK 555
Cdd:cd06608    82 DQLWLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAyilrETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgilngVTTT-----TFCGTPDYIAPEIL---QELE--YGPSVDWWALGVLMYEMMAGQPPFeADNEDD--LFEsILHDD 623
Cdd:cd06608   162 Q-----LDSTlgrrnTFIGTPYWMAPEVIacdQQPDasYDARCDVWSLGITAIELADGKPPL-CDMHPMraLFK-IPRNP 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 624 ---VLYPVWLSKEAVSILKAFMTKNPHKRlgcvaaqNGEDAIKQHPF 667
Cdd:cd06608   235 pptLKSPEKWSKEFNDFISECLIKNYEQR-------PFTEELLEHPF 274
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
408-607 2.11e-32

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: 126.82  E-value: 2.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilQDDDVDCTMTEKRILALARKHPY--LTQLYCCFQTKDRLFFV 485
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT--DDDDVSDIQKEVALLSQLKLGQPknIIKYYGSYLKGPSLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd06917    81 MDYCEGGSIR-TLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 566 TFCGTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06917   160 TFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPY 202
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
413-674 2.36e-32

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: 126.76  E-value: 2.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVdctMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14090     9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRV---FREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH---CKLADFGMCKEGILNG-----VTT 564
Cdd:cd14090    86 PLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIKLSStsmtpVTT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 ---TTFCGTPDYIAPEIL-----QELEYGPSVDWWALGVLMYEMMAGQPPF-------------EA--DNEDDLFESILH 621
Cdd:cd14090   166 pelLTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFygrcgedcgwdrgEAcqDCQELLFHSIQE 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 622 DDVLYP--VW--LSKEAVSILKAFMTKNPHKRLGcvAAQngedaIKQHPffkeidWV 674
Cdd:cd14090   246 GEYEFPekEWshISAEAKDLISHLLVRDASQRYT--AEQ-----VLQHP------WV 289
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
408-667 2.40e-32

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: 126.04  E-value: 2.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILqDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKI-DENVQREIINHRSL----RHPNIIRFKEVVLTPTHLAIVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE--GHCKLADFGMCKEGILNGVTTT 565
Cdd:cd14662    77 YAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVLHSQPKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TfCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYP----VWLSKEAVSIL 638
Cdd:cd14662   157 T-VGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRimSVQYKipdyVRVSQDCRHLL 235
                         250       260
                  ....*....|....*....|....*....
gi 1958782016 639 KAFMTKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14662   236 SRIFVANPAKRITI-------PEIKNHPW 257
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
412-668 4.29e-32

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: 125.82  E-value: 4.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdCTMT---EKRILALARKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd14197    15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQD----CRMEiihEIAVLELAQANPWVINLHEVYETASEMILVLEY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQI--QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE---GHCKLADFGMCKegIL-NGV 562
Cdd:cd14197    91 AAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSR--ILkNSE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPV----WLSKEAVSIL 638
Cdd:cd14197   169 ELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEeefeHLSESAIDFI 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958782016 639 KAFMTKNPHKRlgcvaaQNGEDAIkQHPFF 668
Cdd:cd14197   249 KTLLIKKPENR------ATAEDCL-KHPWL 271
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
406-627 4.43e-32

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: 125.49  E-value: 4.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDvdctMTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEH----MIQNEVSILRRvKHPNIVLLIEEMDMPTELYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL----DAEGHCKLADFGMCKegILN 560
Cdd:cd14183    82 VMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT--VVD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 561 GvTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD--LFESILHDDVLYP 627
Cdd:cd14183   160 G-PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQevLFDQILMGQVDFP 227
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
412-611 9.44e-32

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated 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 MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 124.32  E-value: 9.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvilqddDVDCTMTEKRILALARKHPYLTQLY----CCFQTKDRLFFVME 487
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLR--------DNPKARREVELHWRASGCPHIVRIIdvyeNTYQGRKCLLVVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQR--SRKFDEPRsrfyAAEVT----SALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEGI 558
Cdd:cd14089    79 CMEGGELFSRIQEraDSAFTERE----AAEIMrqigSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGFAKETT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 559 LNgVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd14089   155 TK-KSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNH 206
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
414-611 1.59e-31

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: 123.88  E-value: 1.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLA-ELKGKDEVyAVKVL------KKDVILQDDDVdctMTEKrilalarKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd06647    15 IGQGASGTVYTAiDVATGQEV-AIKQMnlqqqpKKELIINEILV---MREN-------KNPNIVNYLDSYLVGDELWVVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTT 566
Cdd:cd06647    84 EYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd06647   163 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 207
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
410-649 2.01e-31

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: 123.61  E-value: 2.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKD----VILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd13993     4 LISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnsKDGNDFQKLPQLREIDLHRRVSRHPNIITLHDVFETEVAIYIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKF-DEPRS-RFYAAEVTSALMFLHQHGVIYRDLKLDNILLD-AEGHCKLADFGMckegilngV 562
Cdd:cd13993    84 LEYCPNGDLFEAITENRIYvGKTELiKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGL--------A 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTF-----CGTPDYIAPEILQEL-----EYGP-SVDWWALGVLMYEMMAGQPPFE-ADNEDDLF-ESILHDDVLYPVW 629
Cdd:cd13993   156 TTEKIsmdfgVGSEFYMAPECFDEVgrslkGYPCaAGDIWSLGIILLNLTFGRNPWKiASESDPIFyDYYLNSPNLFDVI 235
                         250       260
                  ....*....|....*....|..
gi 1958782016 630 L--SKEAVSILKAFMTKNPHKR 649
Cdd:cd13993   236 LpmSDDFYNLLRQIFTVNPNNR 257
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
414-671 3.02e-31

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: 123.99  E-value: 3.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd06644    20 LGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEILATC-NHPYIVKLLGAFYWDGKLWIMIEFCPGGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 ---LMFQIQRSRKfdEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGT 570
Cdd:cd06644    96 vdaIMLELDRGLT--EPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEI-----LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD---VLYPVWLSKEAVSILKAFM 642
Cdd:cd06644   174 PYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTAL 253
                         250       260
                  ....*....|....*....|....*....
gi 1958782016 643 TKNPHKRLGcvAAQngedaIKQHPFFKEI 671
Cdd:cd06644   254 DKHPETRPS--AAQ-----LLEHPFVSSV 275
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
412-670 3.71e-31

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 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). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. 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 PhKG1 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: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 123.10  E-value: 3.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVL--KKDVILQDDDV----DCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14182     9 EILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVqelrEATLKEIDILRKVSGHPNIIQLKDTYETNTFFFLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTT 565
Cdd:cd14182    89 FDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPGEKLR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQ------ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAV 635
Cdd:cd14182   168 EVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPEWddRSDTVK 247
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 636 SILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFFKE 670
Cdd:cd14182   248 DLISRFLVVQPQKRY------TAEEAL-AHPFFQQ 275
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
407-668 4.30e-31

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: 122.81  E-value: 4.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEV-YAVKVLKKDVILQDDdvdcTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14202     3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQ----TLLGKEIKILKElKHENIVALYDFQEIANSVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG---------HCKLADFGMCK 555
Cdd:cd14202    79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVwLSKEAV 635
Cdd:cd14202   159 Y-LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPN-IPRETS 236
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958782016 636 SILK----AFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14202   237 SHLRqlllGLLQRNQKDRMDF-------DEFFHHPFL 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
412-650 6.82e-31

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: 122.07  E-value: 6.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDcTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNE-ILHEIAVLELCKDCPRVVNLHEVYETRSELILILELAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE---GHCKLADFGMCKEgILNGVTTTTFC 568
Cdd:cd14106    93 GELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRV-IGEGEEIREIL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQeleYGP---SVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWL----SKEAVSILKAF 641
Cdd:cd14106   172 GTPDYVAPEILS---YEPislATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAIDFIKRL 248

                  ....*....
gi 1958782016 642 MTKNPHKRL 650
Cdd:cd14106   249 LVKDPEKRL 257
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
411-649 8.38e-31

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: 121.46  E-value: 8.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvILQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd08218     5 IKKIGEGSFGKALLVKSKEDGKQYVIKEIN---ISKMSPKEREESRKEVAVLSKmKHPNIVQYQESFEENGNLYIVMDYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQI--QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVT--TT 565
Cdd:cd08218    82 DGGDLYKRInaQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIAR--VLNSTVelAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDvlYP---VWLSKEAVSILKAFM 642
Cdd:cd08218   160 TCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGS--YPpvpSRYSYDLRSLVSQLF 237

                  ....*..
gi 1958782016 643 TKNPHKR 649
Cdd:cd08218   238 KRNPRDR 244
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
408-649 1.11e-30

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: 121.12  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdctMTEK---RILALARK--HPYLTQLYCCFQ-TKDR 481
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPD------FVQKflpRELSILRRvnHPNIVQMFECIEvANGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVnGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG-HCKLADFGMCKEGILN 560
Cdd:cd14164    76 LYIVMEAA-ATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGP-SVDWWALGVLMYEMMAGQPPFEADNEDDLfeSILHDDVLYP--VWLSKEAVSI 637
Cdd:cd14164   155 PELSTTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRGVLYPsgVALEEPCRAL 232
                         250
                  ....*....|..
gi 1958782016 638 LKAFMTKNPHKR 649
Cdd:cd14164   233 IRTLLQFNPSTR 244
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
414-668 1.54e-30

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: 121.61  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKkdVILQDDDVDCTMTekRILALARK-----HPYLTQLY--CCFQTKDR---LF 483
Cdd:cd07838     7 IGEGAYGTVYKARDLQDGRFVALKKVR--VPLSEEGIPLSTI--REIALLKQlesfeHPNVVRLLdvCHGPRTDRelkLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGgDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK----EG 557
Cdd:cd07838    83 LVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARiysfEM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTFcgtpdYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----------DDVLY 626
Cdd:cd07838   162 ALTSVVVTLW-----YRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDviglpseeewpRNSAL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 627 PvW-----------------LSKEAVSILKAFMTKNPHKRLGCVAAQngedaikQHPFF 668
Cdd:cd07838   237 P-RssfpsytprpfksfvpeIDEEGLDLLKKMLTFNPHKRISAFEAL-------QHPYF 287
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
169-222 5.06e-30

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 112.34  E-value: 5.06e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 169 GHKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20792     1 GHKFVATFFKQPTFCSHCKDFIWG-LGKQGYQCQVCRFVVHKRCHEYVVFKCPG 53
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
414-669 5.35e-30

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: 120.21  E-value: 5.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAelkgKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd06655    27 IGQGASGTVFTA----IDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDY 573
Cdd:cd06655   103 LT-DVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 574 IAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEadNEDDLFESILHDDVLYPVWLSKEAVS-ILKAFMTKNPHKRlgc 652
Cdd:cd06655   182 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPELQNPEKLSpIFRDFLNRCLEMD--- 256
                         250
                  ....*....|....*..
gi 1958782016 653 VAAQNGEDAIKQHPFFK 669
Cdd:cd06655   257 VEKRGSAKELLQHPFLK 273
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
163-222 9.59e-30

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. 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. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 111.65  E-value: 9.59e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 163 RVHQVNGHKFMATYLRQPTYCSHCRDFIWGViGKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20834     1 KVHEVKGHEFIAKFFRQPTFCSVCKEFLWGF-NKQGYQCRQCNAAVHKKCHDKILGKCPG 59
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
402-669 1.14e-29

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: 119.37  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 402 RLGLDefNFIKVlGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDR 481
Cdd:cd06658    21 REYLD--SFIKI-GEGSTGIVCIATEKHTGKQVAVKKMD----LRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRkFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd06658    94 LWVVMEFLEGGALTDIVTHTR-MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEadNEDDLFESILHDDVLYP-VWLSKEAVSILKA 640
Cdd:cd06658   173 PKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYF--NEPPLQAMRRIRDNLPPrVKDSHKVSSVLRG 250
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958782016 641 F----MTKNPHKRlgcVAAQNgedaIKQHPFFK 669
Cdd:cd06658   251 FldlmLVREPSQR---ATAQE----LLQHPFLK 276
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
414-668 1.34e-29

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: 118.97  E-value: 1.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKdVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVnGGD 493
Cdd:cd07832     8 IGEGAHGIVFKAKDRETGETVALKKVAL-RKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYM-LSS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRK-FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVTTTTF---CG 569
Cdd:cd07832    86 LSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR--LFSEEDPRLYshqVA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILhdDVL----YPVW--------------- 629
Cdd:cd07832   164 TRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVL--RTLgtpnEKTWpeltslpdynkitfp 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 630 -------------LSKEAVSILKAFMTKNPHKRLGCvaaqngEDAIKqHPFF 668
Cdd:cd07832   242 eskgirleeifpdCSPEAIDLLKGLLVYNPKKRLSA------EEALR-HPYF 286
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
409-668 1.45e-29

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: 118.97  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIKVlGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd06657    24 NFIKI-GEGSTGIVCIATVKSSGKLVAVKKMD----LRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRkFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd06657    99 LEGGALTDIVTHTR-MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEadNEDDLFESILHDDVLYPVWLSKEAVS-ILKAF----MT 643
Cdd:cd06657   178 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYF--NEPPLKAMKMIRDNLPPKLKNLHKVSpSLKGFldrlLV 255
                         250       260
                  ....*....|....*....|....*
gi 1958782016 644 KNPHKRlgcVAAQNgedaIKQHPFF 668
Cdd:cd06657   256 RDPAQR---ATAAE----LLKHPFL 273
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
412-668 1.69e-29

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: 117.72  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLA-ELKGKDEVyAVKVLKKDVILQ----DDDVDCTMtEKRILALARK--HPYLTQLYCCFQTKDRLFF 484
Cdd:cd14005     6 DLLGKGGFGTVYSGvRIRDGLPV-AVKFVPKSRVTEwamiNGPVPVPL-EIALLLKASKpgVPGVIRLLDWYERPDGFLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQ-IQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC-KLADFGmCKEgILNGV 562
Cdd:cd14005    84 IMERPEPCQDLFDfITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEvKLIDFG-CGA-LLKDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADneddlfESILHDDVLYPVWLSKEAVSILKAF 641
Cdd:cd14005   162 VYTDFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLFRPRLSKECCDLISRC 235
                         250       260
                  ....*....|....*....|....*..
gi 1958782016 642 MTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14005   236 LQFDPSKRPSL-------EQILSHPWF 255
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
406-672 1.84e-29

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: 118.59  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILA-SCDHPNIVKLLDAFYYENNLWIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDL---MFQIQRSrkFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd06643    81 IEFCAGGAVdavMLELERP--LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEIL-----QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD---VLYPVWLSKEA 634
Cdd:cd06643   159 RRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEF 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 635 VSILKAFMTKNphkrlgcVAAQNGEDAIKQHPFFKEID 672
Cdd:cd06643   239 KDFLRKCLEKN-------VDARWTTSQLLQHPFVSVLV 269
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
413-668 1.95e-29

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 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). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. 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 PhKG2 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: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 118.15  E-value: 1.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLK----KDVILQDDDV-DCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14181    17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVrSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVFD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM-CKEGilNGVTTTT 566
Cdd:cd14181    97 LMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsCHLE--PGEKLRE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQ------ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVS 636
Cdd:cd14181   175 LCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssPEWddRSSTVKD 254
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958782016 637 ILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFF 668
Cdd:cd14181   255 LISRLLVVDPEIRL------TAEQAL-QHPFF 279
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
407-669 2.49e-29

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: 117.80  E-value: 2.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGK-DEVYAVKVLKKDVILQDDdvdcTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14201     7 EYSRKDLVGHGAFAVVFKGRHRKKtDWEVAIKSINKKNLSKSQ----ILLGKEIKILKElQHENIVALYDVQEMPNSVFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG---------HCKLADFGMCK 555
Cdd:cd14201    83 VMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFAR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDL---FESILHDDVLYPVWLSK 632
Cdd:cd14201   163 Y-LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSIPRETSP 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958782016 633 EAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFFK 669
Cdd:cd14201   242 YLADLLLGLLQRNQKDRMDF-------EAFFSHPFLE 271
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
405-649 3.35e-29

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: 117.12  E-value: 3.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAelkgKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd06624     7 YDESGERVVLGKGTFGVVYAA----RDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMfQIQRSR----KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDA-EGHCKLADFGMCKEgiL 559
Cdd:cd06624    83 FMEQVPGGSLS-ALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKR--L 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVT--TTTFCGTPDYIAPEILQELE--YGPSVDWWALGVLMYEMMAGQPPF--EADNEDDLFES---ILHDDVlyPVWL 630
Cdd:cd06624   160 AGINpcTETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFieLGEPQAAMFKVgmfKIHPEI--PESL 237
                         250
                  ....*....|....*....
gi 1958782016 631 SKEAVSILKAFMTKNPHKR 649
Cdd:cd06624   238 SEEAKSFILRCFEPDPDKR 256
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
412-609 4.81e-29

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: 116.69  E-value: 4.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdctmTEKRILALAR--------KHPYLTQLYCCFQTKDRLF 483
Cdd:cd06625     6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTE-------ASKEVKALECeiqllknlQHERIVQYYGCLQDEKSLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EGILNG 561
Cdd:cd06625    79 IFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP---FEA 609
Cdd:cd06625   159 TGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPwaeFEP 209
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
409-612 6.05e-29

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: 116.25  E-value: 6.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIkvlGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDvdctmtEKRILALAR--------KHPYLTQLYCCFQTKD 480
Cdd:cd06626     6 NKI---GEGTFGKVYTAVNLDTGELMAMKEIR----FQDND------PKTIKEIADemkvleglDHPNLVRYYGVEVHRE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGmCKEGILN 560
Cdd:cd06626    73 EVYIFMEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKLKN 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 561 GVTTT------TFCGTPDYIAPEIL---QELEYGPSVDWWALGVLMYEMMAGQPPF-EADNE 612
Cdd:cd06626   152 NTTTMapgevnSLVGTPAYMAPEVItgnKGEGHGRAADIWSLGCVVLEMATGKRPWsELDNE 213
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
407-649 6.73e-29

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: 116.22  E-value: 6.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvILQDDDV----DCtmtEKRILALARK-HPYLTQLYCCFQTKDR 481
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQ---IFEMMDAkarqDC---LKEIDLLQQLnHPNIIKYLASFIENNE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRK----FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKeg 557
Cdd:cd08224    75 LNIVLELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTF--CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNED--DLFESILHDDvlYPVwLSKE 633
Cdd:cd08224   153 FFSSKTTAAHslVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCE--YPP-LPAD 229
                         250       260
                  ....*....|....*....|.
gi 1958782016 634 AVS-----ILKAFMTKNPHKR 649
Cdd:cd08224   230 LYSqelrdLVAACIQPDPEKR 250
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
411-667 6.89e-29

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: 116.16  E-value: 6.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAeLKGKDEVYAVKVlkkdVILQDDD---VDCTMTEKRILALARKHPYLTQL--YCCFQTKDRLFFV 485
Cdd:cd14131     6 LKQLGKGGSSKVYKV-LNPKKKIYALKR----VDLEGADeqtLQSYKNEIELLKKLKGSDRIIQLydYEVTDEDDYLYMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYvNGGDL--MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLdAEGHCKLADFGMCKeGILNGVT 563
Cdd:cd14131    81 MEC-GEIDLatILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAK-AIQNDTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTF---CGTPDYIAPEILQELEY----------GPSVDWWALGVLMYEMMAGQPPF-EADNEDDLFESIL--HDDVLYP 627
Cdd:cd14131   158 SIVRdsqVGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFqHITNPIAKLQAIIdpNHEIEFP 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958782016 628 VWLSKEAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14131   238 DIPNPDLIDVMKRCLQRDPKKRPSI-------PELLNHPF 270
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
395-668 7.08e-29

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: 117.01  E-value: 7.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 395 VRQGQAKRLgLDefNFIKVlGKGSFGKVMLAELKGKDEVYAVKVLkkdvilqdddvDCTMTEKRILALAR-------KHP 467
Cdd:cd06659    14 VDQGDPRQL-LE--NYVKI-GEGSTGVVCIAREKHSGRQVAVKMM-----------DLRKQQRRELLFNEvvimrdyQHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 468 YLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAeVTSALMFLHQHGVIYRDLKLDNILLDAEGHCK 547
Cdd:cd06659    79 NVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEA-VLQALAYLHSQGVIHRDIKSDSILLTLDGRVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 548 LADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESiLHDDVLYP 627
Cdd:cd06659   158 LSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKR-LRDSPPPK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 628 VWLSKEAVSILKAF----MTKNPHKRlgcVAAQNgedaIKQHPFF 668
Cdd:cd06659   237 LKNSHKASPVLRDFlermLVRDPQER---ATAQE----LLDHPFL 274
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
412-669 7.42e-29

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: 116.67  E-value: 7.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVM--LAELKGKDevYAVKVLKKDVILQDDDVdctMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYV 489
Cdd:cd14174     8 ELLGEGAYAKVQgcVSLQNGKE--YAVKIIEKNAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEGILNGVTT-- 564
Cdd:cd14174    83 RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSGVKLNSACTpi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 -----TTFCGTPDYIAPEILQELE-----YGPSVDWWALGVLMYEMMAGQPPFEAD---------------NEDDLFESI 619
Cdd:cd14174   163 ttpelTTPCGSAEYMAPEVVEVFTdeatfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFESI 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 620 LHDDVLYP--VW--LSKEAVSILKAFMTKNPHKRLGcvAAQngedaIKQHPFFK 669
Cdd:cd14174   243 QEGKYEFPdkDWshISSEAKDLISKLLVRDAKERLS--AAQ-----VLQHPWVQ 289
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
407-649 1.03e-28

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: 115.60  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAElKGKDEVYavkVLKKDVILQ---DDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLF 483
Cdd:cd08221     1 HYIPVRVLGRGAFGEAVLYR-KTEDNSL---VVWKEVNLSrlsEKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQI--QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:cd08221    76 IEMEYCNGGNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD--VLYPVWlSKEAVSILK 639
Cdd:cd08221   156 SMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEyeDIDEQY-SEEIIQLVH 234
                         250
                  ....*....|
gi 1958782016 640 AFMTKNPHKR 649
Cdd:cd08221   235 DCLHQDPEDR 244
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
406-659 1.18e-28

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-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 uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized 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: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 115.51  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVK-VLKKDvilQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkFLKRD---GRKVRKAAKNEINILKMV-KHPNILQLVDVFETRKEYFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGHCKL--ADFGMCKegILNG 561
Cdd:cd14088    77 FLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNSKIviSDFHLAK--LENG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF--EADNED------DLFESILHDDVLY--PVW-- 629
Cdd:cd14088   155 LIKEP-CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFydEAEEDDyenhdkNLFRKILAGDYEFdsPYWdd 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958782016 630 LSKEAVSILKAFMTKNPHKRLGCVAAQNGE 659
Cdd:cd14088   234 ISQAAKDLVTRLMEVEQDQRITAEEAISHE 263
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
408-606 1.26e-28

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: 115.92  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLkkDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd06640     6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKII--DLEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTF 567
Cdd:cd06640    83 YLGGGSAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958782016 568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP 606
Cdd:cd06640   162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
417-668 1.37e-28

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 115.34  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 417 GSFGKVMLAELKGKDEVYAVKVLKKDVilqdddvDCTMTEKRILAlaRKHPYLTQLYCCFQTKDRLFFVMEYVNGGDL-- 494
Cdd:cd05576    10 GVIDKVLLVMDTRTQETFILKGLRKSS-------EYSRERKTIIP--RCVPNMVCLRKYIISEESVFLVLQHAEGGKLws 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 495 --------MFQIQRSRKFDE---PRSRFY---------AAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM- 553
Cdd:cd05576    81 ylskflndKEIHQLFADLDErlaAASRFYipeeciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRw 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 554 -------CKEGILNGvttttfcgtpdYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNeddlfESI-LHDDVL 625
Cdd:cd05576   161 sevedscDSDAIENM-----------YCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHP-----AGInTHTTLN 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 626 YPVWLSKEAVSILKAFMTKNPHKRLGcvAAQNGEDAIKQHPFF 668
Cdd:cd05576   225 IPEWVSEEARSLLQQLLQFNPTERLG--AGVAGVEDIKSHPFF 265
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
412-667 3.29e-28

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: 114.74  E-value: 3.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVdctMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRV---FREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH---CKLADFGMCKEGILNG----VTT 564
Cdd:cd14173    85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFDLGSGIKLNSdcspIST 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 T---TFCGTPDYIAPEILQELE-----YGPSVDWWALGVLMYEMMAGQPPFEADNEDD---------------LFESILH 621
Cdd:cd14173   165 PellTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDcgwdrgeacpacqnmLFESIQE 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 622 DDVLYPV--W--LSKEAVSILKAFMTKNPHKRLGcvAAQngedaIKQHPF 667
Cdd:cd14173   245 GKYEFPEkdWahISCAAKDLISKLLVRDAKQRLS--AAQ-----VLQHPW 287
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
427-649 4.15e-28

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 118.58  E-value: 4.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 427 LKGKDEvyAVKVLKKDVILQDD-DVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRK-- 503
Cdd:PTZ00267   87 TRGSDP--KEKVVAKFVMLNDErQAAYARSELHCLA-ACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKeh 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 504 --FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVT---TTTFCGTPDYIAPEI 578
Cdd:PTZ00267  164 lpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQ-YSDSVSldvASSFCGTPYYLAPEL 242
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 579 LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV-LYPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:PTZ00267  243 WERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYdPFPCPVSSGMKALLDPLLSKNPALR 314
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
407-611 4.68e-28

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: 114.14  E-value: 4.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELK-GKDEVYAVK-------VLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQT 478
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKsNGQTLLALKeinmtnpAFGRTEQERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDRLFFVMEYVNG---GDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLH-QHGVIYRDLKLDNILLDAEGHCKLADFGM 553
Cdd:cd08528    81 NDRLYIVMELIEGaplGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 554 CKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd08528   161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTN 218
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
405-649 5.89e-28

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: 113.54  E-value: 5.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLF 483
Cdd:cd13996     5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR----LTEKSSASEKVLREVKALAKlNHPNIVRYYTAWVEEPPLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGG---DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE-GHCKLADFGMCK---- 555
Cdd:cd13996    81 IQMELCEGGtlrDWIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATsign 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 --------EGILNGVTT--TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAgqpPFEADNE-----DDLFESIL 620
Cdd:cd13996   161 qkrelnnlNNNNNGNTSnnSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMErstilTDLRNGIL 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 621 HDDVL--YPVWLskeavSILKAFMTKNPHKR 649
Cdd:cd13996   238 PESFKakHPKEA-----DLIQSLLSKNPEER 263
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
414-611 6.04e-28

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: 114.44  E-value: 6.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAelkgKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd06654    28 IGQGASGTVYTA----MDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDY 573
Cdd:cd06654   104 LT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 182
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958782016 574 IAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd06654   183 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 220
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
390-649 6.34e-28

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 118.05  E-value: 6.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 390 GENGEVRQGQAKRLGLDefnfiKVLGKGSFGKVMLAELKGKDEVYAVKVL------KKDVILQDDDVDCTMTEKrilala 463
Cdd:PTZ00283   21 AKDEATAKEQAKKYWIS-----RVLGSGATGTVLCAKRVSDGEPFAVKVVdmegmsEADKNRAQAEVCCLLNCD------ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 464 rkhpYLTQLYCC--FQTKDR--------LFFVMEYVNGGDLMFQIQR----SRKFDEPRSRFYAAEVTSALMFLHQHGVI 529
Cdd:PTZ00283   90 ----FFSIVKCHedFAKKDPrnpenvlmIALVLDYANAGDLRQEIKSraktNRTFREHEAGLLFIQVLLAVHHVHSKHMI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 530 YRDLKLDNILLDAEGHCKLADFGMCK--EGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:PTZ00283  166 HRDIKSANILLCSNGLVKLGDFGFSKmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPF 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 608 EADNEDDLFESILHD--DVLyPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:PTZ00283  246 DGENMEEVMHKTLAGryDPL-PPSISPEMQEIVTALLSSDPKRR 288
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
406-672 6.71e-28

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: 113.97  E-value: 6.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDctmtEKRILALARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKS---KRDPSE----EIEILLRYGQHPNIITLKDVYDDGKHVYLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGH---CKLADFGMCKEGILNG 561
Cdd:cd14175    74 TELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAEN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeADNEDDLFESILHD------DVLYPVW--LSKE 633
Cdd:cd14175   154 GLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF-ANGPSDTPEEILTRigsgkfTLSGGNWntVSDA 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958782016 634 AVSILKAFMTKNPHKRLgcVAAQngedaIKQHPFFKEID 672
Cdd:cd14175   233 AKDLVSKMLHVDPHQRL--TAKQ-----VLQHPWITQKD 264
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
405-650 8.80e-28

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: 113.52  E-value: 8.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDV--------------DCTMTEKRI------LALAR 464
Cdd:cd14199     1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFprrppprgaraapeGCTQPRGPIervyqeIAILK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 465 K--HPYLTQLYCCFQ--TKDRLFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL 540
Cdd:cd14199    81 KldHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 541 DAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELE---YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFE 617
Cdd:cd14199   160 GEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRkifSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958782016 618 SILHDDVLYPVW--LSKEAVSILKAFMTKNPHKRL 650
Cdd:cd14199   240 KIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI 274
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
414-611 9.49e-28

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: 113.66  E-value: 9.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAelkgKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd06656    27 IGQGASGTVYTA----IDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDY 573
Cdd:cd06656   103 LT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 181
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958782016 574 IAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd06656   182 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 219
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
406-650 2.84e-27

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: 112.42  E-value: 2.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDctmtEKRILALARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14178     3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKS---KRDPSE----EIEILLRYGQHPNIITLKDVYDDGKFVYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGH---CKLADFGMCKE-GILN 560
Cdd:cd14178    76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQlRAEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeADNEDDLFESILH--DDVLYPV----W--LSK 632
Cdd:cd14178   156 GLLMTP-CYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF-ANGPDDTPEEILAriGSGKYALsggnWdsISD 233
                         250
                  ....*....|....*...
gi 1958782016 633 EAVSILKAFMTKNPHKRL 650
Cdd:cd14178   234 AAKDIVSKMLHVDPHQRL 251
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
405-649 2.93e-27

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: 111.69  E-value: 2.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLF 483
Cdd:cd14046     5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK----LRSESKNNSRILREVMLLSRlNHQHVVRYYQAWIERANLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN--- 560
Cdd:cd14046    81 IQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNvel 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 ---------------GVTTTTFCGTPDYIAPEILQELE--YGPSVDWWALGVLMYEMMAgqpPFEADNEDDLF------E 617
Cdd:cd14046   161 atqdinkstsaalgsSGDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMCY---PFSTGMERVQIltalrsV 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958782016 618 SILHDDVLYPVWLSKEAvSILKAFMTKNPHKR 649
Cdd:cd14046   238 SIEFPPDFDDNKHSKQA-KLIRWLLNHDPAKR 268
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
414-652 3.04e-27

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: 111.16  E-value: 3.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKkdVILQDDDVDCTMtEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIK--CRKAKDREDVRN-EIEIMNQLR-HPRLLQLYDAFETPREMVLVMEYVAGGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LmFQ--IQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGH-CKLADFGMCKEGILNGVTTTTFcG 569
Cdd:cd14103    77 L-FErvVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLKVLF-G 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN---------------EDDLFESIlhddvlypvwlSKEA 634
Cdd:cd14103   155 TPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNdaetlanvtrakwdfDDEAFDDI-----------SDEA 223
                         250       260
                  ....*....|....*....|..
gi 1958782016 635 vsilKAFMT----KNPHKRLGC 652
Cdd:cd14103   224 ----KDFISkllvKDPRKRMSA 241
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
407-649 3.21e-27

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: 110.99  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYavkVLKKDVILQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKD-RLFF 484
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQY---VIKKLNLKNASKRERKAAEQEAKLLSKlKHPNIVSYKESFEGEDgFLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQI--QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGV 562
Cdd:cd08223    78 VMGFCEGGDLYTRLkeQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR--VLESS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 T--TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV-LYPVWLSKEAVSILK 639
Cdd:cd08223   156 SdmATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIK 235
                         250
                  ....*....|
gi 1958782016 640 AFMTKNPHKR 649
Cdd:cd08223   236 AMLHQDPEKR 245
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
406-672 3.57e-27

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: 112.25  E-value: 3.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVI-----LQDDDVDctmTEKRILALArKHPYLTQLYCCFQTKD 480
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFtsspgLSTEDLK---REASICHML-KHPHIVELLETYSSDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQI-QRSRK---FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGM 553
Cdd:cd14094    79 MLYMVFEFMDGADLCFEIvKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 554 CKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEdDLFESILHDDVLY--PVW-- 629
Cdd:cd14094   159 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMnpRQWsh 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 630 LSKEAVSILKAFMTKNPHKRLGCVAAQNgedaikqHPFFKEID 672
Cdd:cd14094   238 ISESAKDLVRRMLMLDPAERITVYEALN-------HPWIKERD 273
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
414-650 3.78e-27

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: 112.27  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVIlqdddvdcTMTEKRILAL--ARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRME--------ANTQREVAALrlCQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH---CKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd14180    86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQTPC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE-------ADNEDDLFESILHDDVLY--PVW--LSKEAVSI 637
Cdd:cd14180   166 FTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQskrgkmfHNHAADIMHKIKEGDFSLegEAWkgVSEEAKDL 245
                         250
                  ....*....|...
gi 1958782016 638 LKAFMTKNPHKRL 650
Cdd:cd14180   246 VRGLLTVDPAKRL 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
413-607 3.79e-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: 111.09  E-value: 3.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKvlkkDVILQDDDVDCTMTEKRIL-ALARK--------HPYLTQLYCCFQTKDRLF 483
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVK----QVELPSVSAENKDRKKSMLdALQREiallrelqHENIVQYLGSSSDANHLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd06628    83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTT------FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06628   163 TKNngarpsLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF 212
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
412-668 4.34e-27

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: 111.59  E-value: 4.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGK---GSFGKVMLAELKGKDEVYAVKVLKKDVilqdDDVDCTMTEKRILALAR--KHPYLTQLYCCF--QTKDRLFF 484
Cdd:cd07831     2 KILGKigeGTFSEVLKAQSRKTGKYYAIKCMKKHF----KSLEQVNNLREIQALRRlsPHPNILRLIEVLfdRKTGRLAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEyvnggdLM----FQIQRSRK--FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEgHCKLADFGMCKeGI 558
Cdd:cd07831    78 VFE------LMdmnlYELIKGRKrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCR-GI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 LNGVTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIlHD-------DVLY---- 626
Cdd:cd07831   150 YSKPPYTEYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKI-HDvlgtpdaEVLKkfrk 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 627 ------------PVWLSK-------EAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFF 668
Cdd:cd07831   229 srhmnynfpskkGTGLRKllpnasaEGLDLLKKLLAYDPDERI------TAKQAL-RHPYF 282
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
243-292 5.96e-27

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 103.51  E-value: 5.96e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLYGLVRQGLKCKDCGMNVHHRCKENVPHLC 50
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
408-670 6.00e-27

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: 111.51  E-value: 6.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDD-VDctMTEKRILALAR--KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDgIN--FTALREIKLLQelKHPNIIGLLDVFGHKSNINL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVnGGDLMFQIQ-RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegilngvt 563
Cdd:cd07841    80 VFEFM-ETDLEKVIKdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR-------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 tttFCGTPD-----------YIAPEILQELE-YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI------------ 619
Cdd:cd07841   151 ---SFGSPNrkmthqvvtrwYRAPELLFGARhYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIfealgtpteenw 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 620 -----LHDDVLY------PVW-----LSKEAVSILKAFMTKNPHKRLGCVAAQngedaikQHPFFKE 670
Cdd:cd07841   228 pgvtsLPDYVEFkpfpptPLKqifpaASDDALDLLQRLLTLNPNKRITARQAL-------EHPYFSN 287
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
406-672 9.75e-27

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: 112.04  E-value: 9.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDctmtEKRILALARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14176    19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGH---CKLADFGMCKE-GILN 560
Cdd:cd14176    92 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQlRAEN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeADNEDDLFESILHD------DVLYPVW--LSK 632
Cdd:cd14176   172 GLLMTP-CYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARigsgkfSLSGGYWnsVSD 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958782016 633 EAVSILKAFMTKNPHKRLgcVAAQngedaIKQHPFFKEID 672
Cdd:cd14176   250 TAKDLVSKMLHVDPHQRL--TAAL-----VLRHPWIVHWD 282
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
408-606 1.14e-26

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: 110.16  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVmlaeLKGKD----EVYAVKVLkkDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLF 483
Cdd:cd06641     6 FTKLEKIGKGSFGEV----FKGIDnrtqKVVAIKII--DLEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKDTKLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd06641    79 IIMEYLGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP 606
Cdd:cd06641   158 RN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
411-668 1.46e-26

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: 109.28  E-value: 1.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLK--KDVILQdddvdcTMTEKRILALARKHP-----YLTQLYCCFQTKDRLF 483
Cdd:cd14133     4 LEVLGKGTFGQVVKCYDLLTGEEVALKIIKnnKDYLDQ------SLDEIRLLELLNKKDkadkyHIVRLKDVFYFKNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVngGDLMFQIQRSRK---FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC--KLADFGMCkegi 558
Cdd:cd14133    78 IVFELL--SQNLYEFLKQNKfqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCqiKIIDFGSS---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 lngVTTTTFCGTpdYI------APEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSK 632
Cdd:cd14133   152 ---CFLTQRLYS--YIqsryyrAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLD 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 633 EA-------VSILKAFMTKNPHKRLgcVAAQngedAIkQHPFF 668
Cdd:cd14133   227 QGkaddelfVDFLKKLLEIDPKERP--TASQ----AL-SHPWL 262
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
408-607 2.15e-26

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: 109.38  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLkkDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd06642     6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKII--DLEEAEDEIEDIQQEITVLSQC-DSPYITRYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTF 567
Cdd:cd06642    83 YLGGGSAL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06642   162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
412-652 2.19e-26

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: 108.65  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKdVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDK-LRFPTKQESQLRNEVAILQQLS-HPGVVNLECMFETPERVFVVMEKLHG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 gDLMFQIQRSRK--FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG---HCKLADFGMCKEgILNGVTTTT 566
Cdd:cd14082    87 -DMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI-IGEKSFRRS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeadNED-DLFESILHDDVLYPV--W--LSKEAVSILKAF 641
Cdd:cd14082   165 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---NEDeDINDQIQNAAFMYPPnpWkeISPDAIDLINNL 241
                         250
                  ....*....|.
gi 1958782016 642 MTKNPHKRLGC 652
Cdd:cd14082   242 LQVKMRKRYSV 252
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
411-649 2.57e-26

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: 108.67  E-value: 2.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKgkdevyavkVLKKDVILQDDDVDCTMTEKRILALAR-------KHPYLTQLYCCFQTKDRLF 483
Cdd:cd08220     5 IRVVGRGAYGTVYLCRRK---------DDNKLVIIKQIPVEQMTKEERQAALNEvkvlsmlHHPNIIEYYESFLEDKALM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRK--FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH-CKLADFGMCKegILN 560
Cdd:cd08220    76 IVMEYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISK--ILS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVT-TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYPVWlSKEAVSI 637
Cdd:cd08220   154 SKSkAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGtfAPISDRY-SEELRHL 232
                         250
                  ....*....|..
gi 1958782016 638 LKAFMTKNPHKR 649
Cdd:cd08220   233 ILSMLHLDPNKR 244
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
412-649 2.79e-26

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: 108.86  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDcTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAE-ILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLmFQI---QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDA---EGHCKLADFGMCKEgILNGVTTT 565
Cdd:cd14198    93 GEI-FNLcvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDIKIVDFGMSRK-IGHACELR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAF 641
Cdd:cd14198   171 EIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSeetfSSVSQLATDFIQKL 250

                  ....*...
gi 1958782016 642 MTKNPHKR 649
Cdd:cd14198   251 LVKNPEKR 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
405-650 6.63e-26

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 108.32  E-value: 6.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEF--NFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvilqddDVDCTMTEKRILALARKHPYLTQLYCCFQT---- 478
Cdd:cd14171     3 LEEYevNWTQKLGTGISGPVRVCVKKSTGERFALKILL--------DRPKARTEVRLHMMCSGHPNIVQIYDVYANsvqf 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 ------KDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-----DAEghCK 547
Cdd:cd14171    75 pgesspRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnseDAP--IK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 548 LADFGMCKEGILNGVTTTTfcgTPDYIAPEIL-----QELE------------YGPSVDWWALGVLMYEMMAGQPPFEAD 610
Cdd:cd14171   153 LCDFGFAKVDQGDLMTPQF---TPYYVAPQVLeaqrrHRKErsgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSE 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 611 N-----EDDLFESILHDDVLYPV--W--LSKEAVSILKAFMTKNPHKRL 650
Cdd:cd14171   230 HpsrtiTKDMKRKIMTGSYEFPEeeWsqISEMAKDIVRKLLCVDPEERM 278
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
243-295 1.26e-25

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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. 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. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 99.72  E-value: 1.26e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:cd20836     1 HKFKVHTYSSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKRCVKNVPSLCGTD 53
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
406-607 1.42e-25

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: 107.02  E-value: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLK--KDVilqDDDVDctmTEKRILALARKHPYLTQLYCCFQTKD--- 480
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpiHDI---DEEIE---AEYNILKALSDHPNVVKFYGMYYKKDvkn 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 --RLFFVMEYVNGG---DLMFQ-IQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC 554
Cdd:cd06638    92 gdQLWLVLELCNGGsvtDLVKGfLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVS 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 555 KEGILNGVTTTTFCGTPDYIAPEIL---QELE--YGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06638   172 AQLTSTRLRRNTSVGTPFWMAPEVIaceQQLDstYDARCDVWSLGITAIELGDGDPPL 229
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
414-667 2.26e-25

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: 106.57  E-value: 2.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVIL-----------------QDDDVDCTMTEKRI---LALARK--HPYLTQ 471
Cdd:cd14200     8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLkqygfprrppprgskaaQGEQAKPLAPLERVyqeIAILKKldHVNIVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 472 LYCCFQ--TKDRLFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLA 549
Cdd:cd14200    88 LIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 550 DFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEY---GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY 626
Cdd:cd14200   167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQsfsGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEF 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 627 P--VWLSKEAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPF 667
Cdd:cd14200   247 PeePEISEELKDLILKMLDKNPETRITV-------PEIKVHPW 282
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
411-668 3.17e-25

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: 106.11  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAvkvLKKdvILQDDDVD----CTMTEKRIL-ALarKHPYLTQLYCCFQTKDR---- 481
Cdd:cd07840     4 IAQIGEGTYGQVYKARNKKTGELVA---LKK--IRMENEKEgfpiTAIREIKLLqKL--DHPNVVRLKEIVTSKGSakyk 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 --LFFVMEYVNGgDLM-FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG----MC 554
Cdd:cd07840    77 gsIYMVFEYMDH-DLTgLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGlarpYT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KEGIL---NGVTTTTfcgtpdYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVL 625
Cdd:cd07840   156 KENNAdytNRVITLW------YRPPELLlGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFElcgspTEEN 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 626 YPVW--------------------------LSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFF 668
Cdd:cd07840   230 WPGVsdlpwfenlkpkkpykrrlrevfknvIDPSALDLLDKLLTLDPKKRI------SADQAL-QHEYF 291
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
413-667 3.36e-25

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: 105.60  E-value: 3.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAeLKGKDEVYAVKvlkkDVILQDDDVDCTMTEKR-------ILALARKHPYLTQLYCCFQTKDRLFFv 485
Cdd:cd06631     8 VLGKGAYGTVYCG-LTSTGQLIAVK----QVELDTSDKEKAEKEYEklqeevdLLKTLKHVNIVGYLGTCLEDNVVSIF- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd06631    82 MEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 ------TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP----------FEADNEDDLFESIlhddvlyPVW 629
Cdd:cd06631   162 qsqllkSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFAIGSGRKPVPRL-------PDK 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782016 630 LSKEAVSILKAFMTKNPHKRLGcvAAQngedaIKQHPF 667
Cdd:cd06631   235 FSPEARDFVHACLTRDQDERPS--AEQ-----LLKHPF 265
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
406-620 3.56e-25

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: 105.39  E-value: 3.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNF--IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLF 483
Cdd:cd14190     2 STFSIhsKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQ---NSKDKEMVLLEIQVMN-QLNHRNLIQLYEAIETPNEIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-DAEGH-CKLADFGMCKEGILN 560
Cdd:cd14190    78 LFMEYVEGGELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNPR 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFcGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd14190   158 EKLKVNF-GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVL 216
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
414-624 4.15e-25

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: 105.43  E-value: 4.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGkDEVYAVKVLKKdvilQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14066     1 IGSGGFGTVYKGVLEN-GTVVAVKRLNE----MNCAASKKEFLTELEMLGRlRHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLmFQIQRSRKFDEP---RSRF-YAAEVTSALMFLHQHG---VIYRDLKLDNILLDAEGHCKLADFGMCKEG--ILNGVT 563
Cdd:cd14066    76 SL-EDRLHCHKGSPPlpwPQRLkIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIppSESVSK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFeSILHDDV 624
Cdd:cd14066   155 TSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASR-KDLVEWV 214
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
409-668 4.23e-25

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: 105.66  E-value: 4.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIKV--LGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd07860     1 NFQKVekIGEGTYGVVYKARNKLTGEVVALKKIRLD--TETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGgDLMFQIQRSRKFDEPRS--RFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNGVTT 564
Cdd:cd07860    79 EFLHQ-DLKKFMDASALTGIPLPliKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARA---FGVPV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCG---TPDYIAPEILQELE-YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVL---------- 625
Cdd:cd07860   155 RTYTHevvTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRtlgtpDEVVwpgvtsmpdy 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 626 ---YPVW-----------LSKEAVSILKAFMTKNPHKRLGCVAAQNgedaikqHPFF 668
Cdd:cd07860   235 kpsFPKWarqdfskvvppLDEDGRDLLSQMLHYDPNKRISAKAALA-------HPFF 284
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
411-668 4.32e-25

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: 105.58  E-value: 4.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDV--DCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd07846     6 LGLVGEGSYGMVMKCRHKETGQIVAIKKFLES---EDDKMvkKIAMREIKMLKQLR-HENLVNLIEVFRRKKRWYLVFEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd07846    82 VDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD------------------------LFESILHDD 623
Cdd:cd07846   162 ATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDqlyhiikclgnliprhqelfqknpLFAGVRLPE 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 624 V--------LYPVWlSKEAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd07846   242 VkeveplerRYPKL-SGVVIDLAKKCLHIDPDKRPSC-------SELLHHEFF 286
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
168-225 4.58e-25

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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. 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. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410383  Cd Length: 58  Bit Score: 98.25  E-value: 4.58e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 168 NGHKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKCAGLKK 225
Cdd:cd20833     1 KDHKFIARFFKQPTFCSHCTDFIWG-FGKQGFQCQVCSFVVHKRCHEFVTFSCPGADK 57
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
410-622 8.04e-25

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: 104.39  E-value: 8.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKGkdEVYAVKVLKK--DVILQDDDVDctmTEKRILALarKHPYLTQLY----CCfqTKDRL- 482
Cdd:cd13979     7 LQEPLGSGGFGSVYKATYKG--ETVAVKIVRRrrKNRASRQSFW---AELNAARL--RHENIVRVLaaetGT--DFASLg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLmfqiqrSRKFDEPRSRFYAAE-------VTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG--- 552
Cdd:cd13979    78 LIIMEYCGNGTL------QQLIYEGSEPLPLAHrilisldIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsv 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 553 -----MCKEGILNGVTtttfcGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD 622
Cdd:cd13979   152 klgegNEVGTPRSHIG-----GTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKD 221
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
406-650 9.22e-25

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: 104.49  E-value: 9.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVI------LQDDDVDctmTEKRILALARkHPYLTQLYCCFQTK 479
Cdd:cd14105     5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIE---REVSILRQVL-HPNIITLHDVFENK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG----HCKLADFGMCK 555
Cdd:cd14105    81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVLYPvWL 630
Cdd:cd14105   161 K-IEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAvnydfDDEYFS-NT 238
                         250       260
                  ....*....|....*....|
gi 1958782016 631 SKEAVSILKAFMTKNPHKRL 650
Cdd:cd14105   239 SELAKDFIRQLLVKDPRKRM 258
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
400-670 1.07e-24

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: 104.36  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 400 AKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKrILALARKHPYLTQLYCCFQTK 479
Cdd:cd06645     5 SRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE---PGEDFAVVQQEI-IMMKDCKHSNIVAYFGSYLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL 559
Cdd:cd06645    81 DKLWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTFCGTPDYIAPEIL---QELEYGPSVDWWALGVLMYEMMAGQPP-FEADNEDDLFesILHDDVLYPVWL----- 630
Cdd:cd06645   161 TIAKRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALF--LMTKSNFQPPKLkdkmk 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 631 -SKEAVSILKAFMTKNPHKRlgcvaaqNGEDAIKQHPFFKE 670
Cdd:cd06645   239 wSNSFHHFVKMALTKNPKKR-------PTAEKLLQHPFVTQ 272
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
414-668 1.89e-24

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: 103.91  E-value: 1.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAvkvLKKdVILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd07835     7 IGEGTYGVVYKARDKLTGEIVA---LKK-IRLETEDEGVPSTAIREISLLKelNHPNIVRLLDVVHSENKLYLVFEFLDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 gDLMFQIQRSRKFDEPRSRF--YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNGVTTTTFCG 569
Cdd:cd07835    83 -DLKKYMDSSPLTGLDPPLIksYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARA---FGVPVRTYTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 ---TPDYIAPEILqeL---EYGPSVDWWALGVLMYEMMAGQPPFEADNE-DDLFE----------------SILHDDV-L 625
Cdd:cd07835   159 evvTLWYRAPEIL--LgskHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEiDQLFRifrtlgtpdedvwpgvTSLPDYKpT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 626 YPVW-----------LSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFF 668
Cdd:cd07835   237 FPKWarqdlskvvpsLDEDGLDLLSQMLVYDPAKRI------SAKAAL-QHPYF 283
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
406-607 2.41e-24

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: 103.53  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLkkDVIlqdDDVDCTM-TEKRILALARKHPYLTQLYCCFQTKDR--- 481
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL--DPI---SDVDEEIeAEYNILRSLPNHPNVVKFYGMFYKADQyvg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 --LFFVMEYVNGGDLMFQIQ----RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK 555
Cdd:cd06639    97 gqLWLVLELCNGGSVTELVKgllkCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 556 EGILNGVTTTTFCGTPDYIAPEIL---QELEYGPSV--DWWALGVLMYEMMAGQPPF 607
Cdd:cd06639   177 QLTSARLRRNTSVGTPFWMAPEVIaceQQYDYSYDArcDVWSLGITAIELADGDPPL 233
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
411-620 3.29e-24

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: 103.78  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAeLKGKD-EVYAVKVLK--KDVILQdddvdcTMTEKRILA-LARKHPylTQLYCCFQTKDRLFF-- 484
Cdd:cd14210    18 LSVLGKGSFGQVVKC-LDHKTgQLVAIKIIRnkKRFHQQ------ALVEVKILKhLNDNDP--DDKHNIVRYKDSFIFrg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 ----VMEyVNGGDL--MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH--CKLADFGM-CK 555
Cdd:cd14210    89 hlciVFE-LLSINLyeLLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSsCF 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 556 EGilNGVTTttfcgtpdYI------APEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd14210   168 EG--EKVYT--------YIqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIM 228
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
407-649 5.52e-24

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: 101.76  E-value: 5.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDDdvdctMTEKRILALARKHPYLTQLY-CCfqTKDR-LFF 484
Cdd:cd05059     5 ELTFLKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDD-----FIEEAKVMMKLSHPKLVQLYgVC--TKQRpIFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEY-VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd05059    77 VTEYmANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLY-PVWLSKEAVSILKA 640
Cdd:cd05059   157 SSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGYRLYrPHLAPTEVYTIMYS 236

                  ....*....
gi 1958782016 641 FMTKNPHKR 649
Cdd:cd05059   237 CWHEKPEER 245
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
401-649 9.51e-24

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: 101.41  E-value: 9.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 401 KRLGLDeFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVdctmtEKRILALAR-KHPYLTQLYCCFQTK 479
Cdd:cd14047     2 ERFRQD-FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK----LNNEKA-----EREVKALAKlDHPNIVRYNGCWDGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DR----------------LFFVMEYVNGGDLMFQIQRSRKfdEPRSRFYAA----EVTSALMFLHQHGVIYRDLKLDNIL 539
Cdd:cd14047    72 DYdpetsssnssrsktkcLFIQMEFCEKGTLESWIEKRNG--EKLDKVLALeifeQITKGVEYIHSKKLIHRDLKPSNIF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 540 LDAEGHCKLADFGMCKEgILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAgqpPFEADNEDDLFESI 619
Cdd:cd14047   150 LVDTGKVKIGDFGLVTS-LKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLH---VCDSAFEKSKFWTD 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958782016 620 LHDDVLYPVWLS--KEAVSILKAFMTKNPHKR 649
Cdd:cd14047   226 LRNGILPDIFDKryKIEKTIIKKMLSKKPEDR 257
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
407-621 1.22e-23

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: 100.81  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14192     5 AVCPHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQL----NHVNLIQLYDAFESKTNLTLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGH-CKLADFGMCKEGILNGVT 563
Cdd:cd14192    81 EYVDGGELFDRItDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 564 TTTFcGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH 621
Cdd:cd14192   161 KVNF-GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVN 217
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
412-609 1.28e-23

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: 100.87  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqdddvDCTMTEKRILAL--------ARKHPYLTQLYCCFQ--TKDR 481
Cdd:cd06653     8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDP-------DSQETSKEVNALeceiqllkNLRHDRIVQYYGCLRdpEEKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EGI- 558
Cdd:cd06653    81 LSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriQTIc 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 559 LNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP---FEA 609
Cdd:cd06653   161 MSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPwaeYEA 214
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
412-649 1.37e-23

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: 100.87  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLkkdvILQD-DDVDCTMTEKRILALARKHPYLTQLYCC--FQTKDRLFF--VM 486
Cdd:cd13985     6 KQLGEGGFSYVYLAHDVNTGRRYALKRM----YFNDeEQLRVAIKEIEIMKRLCGHPNIVQYYDSaiLSSEGRKEVllLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVnGGDLMFQIQRS--RKFDEPRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNILLDAEGHCKLADFGmckegilNGV 562
Cdd:cd13985    82 EYC-PGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG-------SAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFC----------------GTPDYIAPEILQELEYGP---SVDWWALGVLMYEMMAGQPPFEAdneddlfESILHD- 622
Cdd:cd13985   154 TEHYPLeraeevniieeeiqknTTPMYRAPEMIDLYSKKPigeKADIWALGCLLYKLCFFKLPFDE-------SSKLAIv 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 623 DVLYPV----WLSKEAVSILKAFMTKNPHKR 649
Cdd:cd13985   227 AGKYSIpeqpRYSPELHDLIRHMLTPDPAER 257
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
406-668 1.55e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. 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 followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 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: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 100.46  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCL----HHPKLVQCVDAFEEKANIVMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEG-HCKLADFGMCKEgILNGV 562
Cdd:cd14191    78 LEMVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARR-LENAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVLYPVwLSKEAVSI 637
Cdd:cd14191   157 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSatwdfDDEAFDE-ISDDAKDF 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 638 LKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14191   236 ISNLLKKDMKARLTC-------TQCLQHPWL 259
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
406-682 2.05e-23

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: 100.96  E-value: 2.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVlkkdvILQDDDVDCTMTEKRILALARK--HPYLTQLYCCF--QTKDR 481
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKT-----ITTDPNPDVQKQILRELEINKScaSPYIVKYYGAFldEQDSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKF-----DEPRSRFyAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 556
Cdd:cd06621    76 IGIAMEYCEGGSLDSIYKKVKKKggrigEKVLGKI-AESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 GILNGvtTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNED-----DLFESI-------LHDDV 624
Cdd:cd06621   155 LVNSL--AGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIvnmpnpeLKDEP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 625 LYPVWLSKEAVSILKAFMTKNPHKRlgcvaaqNGEDAIKQHPFfkeidWVLLEQKKIK 682
Cdd:cd06621   233 ENGIKWSESFKDFIEKCLEKDGTRR-------PGPWQMLAHPW-----IKAQEKKKVN 278
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
243-292 2.08e-23

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 93.27  E-value: 2.08e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20837     1 HRFKVYNYMSPTFCDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
406-605 2.31e-23

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: 100.52  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKvlkKDVILQDDDV--DCTMTEKRILALArKHPYLTQLYCCFQTKDRLF 483
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIK---KFVESEDDPVikKIALREIRMLKQL-KHPNLVNLIEVFRRKRKLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNG-- 561
Cdd:cd07847    77 LVFEYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR--ILTGpg 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 562 VTTTTFCGTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQP 605
Cdd:cd07847   155 DDYTDYVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQP 199
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
412-609 2.91e-23

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: 99.73  E-value: 2.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARK-HPYLTQLYCCFQ-TKDR-LFFVMEY 488
Cdd:cd06652     8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLlHERIVQYYGCLRdPQERtLSIFMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG---ILNGVTTT 565
Cdd:cd06652    88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLqtiCLSGTGMK 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP---FEA 609
Cdd:cd06652   168 SVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPwaeFEA 214
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
412-620 3.23e-23

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: 99.60  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILalarKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQL----NHANLIQLYDAFESRNDIVLVMEYVDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQ-IQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGH-CKLADFGMCKEGILNGVTTTTFc 568
Cdd:cd14193    86 GELFDRiIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLRVNF- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd14193   165 GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNIL 216
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
405-650 4.39e-23

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-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: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 99.20  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVlkkdvILQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLF 483
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKF-----IMTPHESDKETVRKEIQIMNQlHHPKLINLHDAFEDDNEMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE--GHCKLADFGMCKEGILN 560
Cdd:cd14114    76 LILEFLSGGELFERIaAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATHLDPK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDvlypvW---------LS 631
Cdd:cd14114   156 ESVKVT-TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCD-----WnfddsafsgIS 229
                         250
                  ....*....|....*....
gi 1958782016 632 KEAVSILKAFMTKNPHKRL 650
Cdd:cd14114   230 EEAKDFIRKLLLADPNKRM 248
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
414-608 6.02e-23

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: 99.06  E-value: 6.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDcTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKA-LLKEAEKMERAR-HSYVLPLLGVCVERRSLGLVMEYMENGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMfQIQRSRKFDEPRS-RF-YAAEVTSALMFLH--QHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL----NGVTTT 565
Cdd:cd13978    79 LK-SLLEREIQDVPWSlRFrIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKsisaNRRRGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 566 -TFCGTPDYIAPEILQELEYGPSV--DWWALGVLMYEMMAGQPPFE 608
Cdd:cd13978   158 eNLGGTPIYMAPEAFDDFNKKPTSksDVYSFAIVIWAVLTRKEPFE 203
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
414-649 8.20e-23

Catalytic kinase domain, first 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: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 98.42  E-value: 8.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14107    10 IGRGTFGFVKRVTHKGNGECCAAKFIP----LRSSTRARAFQERDILA-RLSHRRLTCLLDQFETRKTLILILELCSSEE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL--DAEGHCKLADFGMCKEGILNGVTTTTFcGTP 571
Cdd:cd14107    85 LLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQFSKY-GSP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAFMTKNPH 647
Cdd:cd14107   164 EFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDtpeiTHLSEDAKDFIKRVLQPDPE 243

                  ..
gi 1958782016 648 KR 649
Cdd:cd14107   244 KR 245
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
412-669 9.99e-23

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: 98.27  E-value: 9.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLK--KDVILQDDDVDCTMTEKrILALAR-KHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEVVEAIREE-IRMMARlNHPNIVRMLGATQHKSHFNIFVEW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG-HCKLADFG----MCKEGILNGVT 563
Cdd:cd06630    85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGaaarLASKGTGAGEF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDlfesilHDDVLYPVWLSKEAVSILKAFMT 643
Cdd:cd06630   165 QGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISN------HLALIFKIASATTPPPIPEHLSP 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 644 KNPHKRLGCVaAQNGEDAIK-----QHPFFK 669
Cdd:cd06630   239 GLRDVTLRCL-ELQPEDRPParellKHPVFT 268
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
412-650 1.06e-22

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 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: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 98.14  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKkDVILQDDDVDCTMTekrilalARKHPYLTQLYCCFQTKDR----LFFVME 487
Cdd:cd14172    10 QVLGLGVNGKVLECFHRRTGQKCALKLLY-DSPKARREVEHHWR-------ASGGPHIVHILDVYENMHHgkrcLLIIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKEGILNGV 562
Cdd:cd14172    82 CMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL------YPVW--LSKEA 634
Cdd:cd14172   162 LQTP-CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRMgqygfpNPEWaeVSEEA 240
                         250
                  ....*....|....*.
gi 1958782016 635 VSILKAFMTKNPHKRL 650
Cdd:cd14172   241 KQLIRHLLKTDPTERM 256
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
407-635 1.22e-22

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: 98.03  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDDDVDctmtEKRILaLARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05113     5 DLTFLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSMSEDEFIE----EAKVM-MNLSHEKLVQLYGVCTKQRPIFIIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFDEPRSRF-YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd05113    79 EYMANGCLLNYLREMRKRFQTQQLLeMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 566 TFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLYPVWLSKEAV 635
Cdd:cd05113   159 VGSKFPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGLRLYRPHLASEKV 230
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
413-608 1.61e-22

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: 97.46  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGkdEVYAVKVLKkdvilQDDDVDCTMTEKRILALAR-----KHPYLTQLY-CCFQTKdRLFFVM 486
Cdd:cd14061     1 VIGVGGFGKVYRGIWRG--EEVAVKAAR-----QDPDEDISVTLENVRQEARlfwmlRHPNIIALRgVCLQPP-NLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG---VIYRDLKLDNILLD--AEGH------CKLADFGMCK 555
Cdd:cd14061    73 EYARGGALN-RVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILeaIENEdlenktLKITDFGLAR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 556 EgiLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE 608
Cdd:cd14061   152 E--WHKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYK 202
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
406-649 3.44e-22

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: 97.23  E-value: 3.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLE--LDESKFNQIIMELDILHKAVS-PYIVDFYGAFFIEGAVYMC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGD---LMFQIQRSRKFDEPRSRFYAAEVTSALMFL-HQHGVIYRDLKLDNILLDAEGHCKLADFGMckEGILNG 561
Cdd:cd06622    78 MEYMDAGSldkLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGV--SGNLVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEIL------QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLF---ESILHDD-VLYPVWLS 631
Cdd:cd06622   156 SLAKTNIGCQSYMAPERIksggpnQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaqlSAIVDGDpPTLPSGYS 235
                         250
                  ....*....|....*...
gi 1958782016 632 KEAVSILKAFMTKNPHKR 649
Cdd:cd06622   236 DDAQDFVAKCLNKIPNRR 253
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
434-620 4.61e-22

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: 97.01  E-value: 4.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 434 YAVKVLKKDvilQDDDVDctmtEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYA 513
Cdd:cd14177    32 FAVKIIDKS---KRDPSE----EIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQKFFSEREASAVL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 514 AEVTSALMFLHQHGVIYRDLKLDNIL-LDAEGHC---KLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVD 589
Cdd:cd14177   105 YTITKTVDYLHCQGVVHRDLKPSNILyMDDSANAdsiRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMRQGYDAACD 184
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958782016 590 WWALGVLMYEMMAGQPPFeADNEDDLFESIL 620
Cdd:cd14177   185 IWSLGVLLYTMLAGYTPF-ANGPNDTPEEIL 214
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
408-649 4.74e-22

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: 95.84  E-value: 4.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdctmtEKRILALARK------HPYLTQLYCCFQTKDR 481
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKD-------RKRKLEEVERheklgeHPNCVRFIKAWEEKGI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVnggDLMFQIQRSRKFDEPRSRFYA--AEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL 559
Cdd:cd14050    76 LYIQTELC---DTSLQQYCEETHSLPESEVWNilLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTFcGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAG-QPPFEADNEDDLFESILHDDVLYPvwLSKEAVSIL 638
Cdd:cd14050   153 EDIHDAQE-GDPRYMAPELLQG-SFTKAADIFSLGITILELACNlELPSGGDGWHQLRQGYLPEEFTAG--LSPELRSII 228
                         250
                  ....*....|.
gi 1958782016 639 KAFMTKNPHKR 649
Cdd:cd14050   229 KLMMDPDPERR 239
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
242-292 4.85e-22

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 89.65  E-value: 4.85e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20796     1 PHTFVVHTYTKPTVCQHCKKLLKGLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
414-649 5.52e-22

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: 96.20  E-value: 5.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdctMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14113    15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQ-----VTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLD---AEGHCKLADFGMCKEgiLNgvtTTTFC-- 568
Cdd:cd14113    90 LLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFGDAVQ--LN---TTYYIhq 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 --GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAFM 642
Cdd:cd14113   165 llGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLL 244

                  ....*..
gi 1958782016 643 TKNPHKR 649
Cdd:cd14113   245 QMDPAKR 251
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
408-602 6.11e-22

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: 96.34  E-value: 6.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVM-LAELKGKDEVYAVKVLKKDV--------ILQDDDVDCTMTEKrilalarKHPYLTQLYCCFQT 478
Cdd:cd14052     2 FANVELIGSGEFSQVYkVSERVPTGKVYAVKKLKPNYagakdrlrRLEEVSILRELTLD-------GHDNIVQLIDSWEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDRLFFVMEYVNGGDLMF---QIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC- 554
Cdd:cd14052    75 HGHLYIQTELCENGSLDVflsELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAt 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 555 ----KEGILNGvttttfcGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA 602
Cdd:cd14052   155 vwplIRGIERE-------GDREYIAPEILSEHMYDKPADIFSLGLILLEAAA 199
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
412-607 6.16e-22

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: 96.30  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDR--LFFVMEY 488
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNlQHERIVQYYGCLRDRAEktLTIFMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG---ILNGVTTT 565
Cdd:cd06651    93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqtiCMSGTGIR 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 566 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06651   173 SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
411-649 6.34e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 100.25  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAE---LkgkDEVYAVKVLKKDviLQDDDvdcTMTEKRI---LALAR-KHPYLTQLYCCFQTKDRLF 483
Cdd:NF033483   12 GERIGRGGMAEVYLAKdtrL---DRDVAVKVLRPD--LARDP---EFVARFRreaQSAASlSHPNIVSVYDVGEDGGIPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFgmckeGI---LN 560
Cdd:NF033483   84 IVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF-----GIaraLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTT---TFCGTPDYIAPEilQ-ELEY-GPSVDWWALGVLMYEMMAGQPPFEAD----------NED-----DLFESIl 620
Cdd:NF033483  159 STTMTqtnSVLGTVHYLSPE--QaRGGTvDARSDIYSLGIVLYEMLTGRPPFDGDspvsvaykhvQEDppppsELNPGI- 235
                         250       260
                  ....*....|....*....|....*....
gi 1958782016 621 hddvlyPVWLskEAVsILKAfMTKNPHKR 649
Cdd:NF033483  236 ------PQSL--DAV-VLKA-TAKDPDDR 254
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
406-616 8.20e-22

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: 96.22  E-value: 8.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKdvilQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRLF 483
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKD----SEENEEVKETTLRELKMLRtlKQENIVELKEAFRRRGKLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYV--NGGDLMFQIQRSRKFDEPRSRFYaaEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK---EGi 558
Cdd:cd07848    77 LVFEYVekNMLELLEEMPNGVPPEKVRSYIY--QLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARnlsEG- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 559 lNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE-DDLF 616
Cdd:cd07848   154 -SNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEiDQLF 211
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
407-670 8.56e-22

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: 96.67  E-value: 8.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilQDDDVDCT-MTEKRILaLARKHPYLTQLYCCFQTK--DRLF 483
Cdd:cd07845     8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISsLREITLL-LNLRHPNIVELKEVVVGKhlDSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGgDLMFQIQR-SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegilngv 562
Cdd:cd07845    85 LVMEYCEQ-DLASLLDNmPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLAR------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCG--TPD-----YIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVLYP-- 627
Cdd:cd07845   157 TYGLPAKpmTPKvvtlwYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQllgtpNESIWPgf 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 628 -----------------------VWLSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFFKE 670
Cdd:cd07845   237 sdlplvgkftlpkqpynnlkhkfPWLSEAGLRLLNFLLMYDPKKRA------TAEEAL-ESSYFKE 295
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
414-607 9.49e-22

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: 95.98  E-value: 9.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQD-------DDVDCTMTEK--RILAlARKHPYLTQLyccfQTKDRL-F 483
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDknrerwcLEVQIMKKLNhpNVVS-ARDVPPELEK----LSPNDLpL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDL---MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH---CKLADFGMCKEg 557
Cdd:cd13989    76 LAMEYCSGGDLrkvLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKE- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd13989   155 LDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
407-649 1.08e-21

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: 95.48  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDvDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06646    10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIK----LEPGD-DFSLIQQEIFMVKEcKHCNIVAYFGSYLSREKLWIC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd06646    85 MEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 TFCGTPDYIAPEIL---QELEYGPSVDWWALGVLMYEMMAGQPP-FEADNEDDLFesILHDDVLYPVWLSKEAV------ 635
Cdd:cd06646   165 SFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALF--LMSKSNFQPPKLKDKTKwsstfh 242
                         250
                  ....*....|....
gi 1958782016 636 SILKAFMTKNPHKR 649
Cdd:cd06646   243 NFVKISLTKNPKKR 256
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
414-607 1.46e-21

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: 95.41  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDC-------TMTEKRILAlARKHPYLTQLyccFQTKDRLFFVM 486
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCleiqimkRLNHPNVVA-ARDVPEGLQK---LAPNDLPLLAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDL---MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDaEG-----HcKLADFGMCKEgI 558
Cdd:cd14038    78 EYCQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQ-QGeqrliH-KIIDLGYAKE-L 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 559 LNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd14038   155 DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
410-607 1.94e-21

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: 94.21  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMlaelKGKDEVYAVKVlkKDVILQDDDVDcTMTEKRILALAR-----KHPYLTQLYCCFQTKDR--L 482
Cdd:cd13983     5 FNEVLGRGSFKTVY----RAFDTEEGIEV--AWNEIKLRKLP-KAERQRFKQEIEilkslKHPNIIKFYDSWESKSKkeV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNILLD-AEGHCKLADFGMCKegIL 559
Cdd:cd13983    78 IFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLAT--LL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 560 NGVTTTTFCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd13983   156 RQSFAKSVIGTPEFMAPEMYEE-HYDEKVDIYAFGMCLLEMATGEYPY 202
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
407-609 3.29e-21

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: 93.94  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGkdEVYAVKVLKKDvilQDDDVDCTM----TEKRILALArKHPYLTQLYCCFQTKDRL 482
Cdd:cd14147     4 ELRLEEVIGIGGFGKVYRGSWRG--ELVAVKAARQD---PDEDISVTAesvrQEARLFAML-AHPNIIALKAVCLEEPNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQrSRKFDEPRSRFYAAEVTSALMFLHQHG---VIYRDLKLDNILL--DAEGHC------KLADF 551
Cdd:cd14147    78 CLVMEYAAGGPLSRALA-GRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLlqPIENDDmehktlKITDF 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 552 GMCKEgiLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEA 609
Cdd:cd14147   157 GLARE--WHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
406-650 4.59e-21

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: 93.48  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKK--------DVILQDDDVDCTMTeKRILalarkHPYLTQLYCCFQ 477
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqsrasrrGVSREEIEREVSIL-RQVL-----HPNIITLHDVYE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 478 TKDRLFFVMEYVNGGDLM-FQIQRSRKFDEPRSRFyAAEVTSALMFLHQHGVIYRDLKLDNI-LLDAEG---HCKLADFG 552
Cdd:cd14196    79 NRTDVVLILELVSGGELFdFLAQKESLSEEEATSF-IKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 553 MCKEgILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-----HDDVLYP 627
Cdd:cd14196   158 LAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITavsydFDEEFFS 236
                         250       260
                  ....*....|....*....|...
gi 1958782016 628 vWLSKEAVSILKAFMTKNPHKRL 650
Cdd:cd14196   237 -HTSELAKDFIRKLLVKETRKRL 258
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
413-669 4.87e-21

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; 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 three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 93.38  E-value: 4.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARK------HPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14101     7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLPGVNPVPNEVALLQSvgggpgHRGVIRLLDWFEIPEGFLLVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EY-VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE-GHCKLADFGmcKEGILNGVTT 564
Cdd:cd14101    87 ERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRtGDIKLIDFG--SGATLKDSMY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEddlfesILHDDVLYPVWLSKEAVSILKAFMT 643
Cdd:cd14101   165 TDFDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFNKRVSNDCRSLIRSCLA 238
                         250       260
                  ....*....|....*....|....*.
gi 1958782016 644 KNPHKRLGCvaaqngeDAIKQHPFFK 669
Cdd:cd14101   239 YNPSDRPSL-------EQILLHPWMM 257
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
413-649 5.35e-21

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: 93.10  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALaRKHPY----LTQLYCCFQTKDRLFFVMEY 488
Cdd:cd14102     7 VLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLL-KKVGSgfrgVIKLLDWYERPDGFLIVMER 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VN-GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE-GHCKLADFGmcKEGILNGVTTTT 566
Cdd:cd14102    86 PEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRtGELKLIDFG--SGALLKDTVYTD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADneddlfESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd14102   164 FDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQD------EEILRGRLYFRRRVSPECQQLIKWCLSLR 237

                  ....
gi 1958782016 646 PHKR 649
Cdd:cd14102   238 PSDR 241
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
414-636 5.50e-21

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK 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: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 93.54  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLA-ELKGKDEVyAVKV--LKKDvILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQT-KDRLFFVME 487
Cdd:cd13990     8 LGKGGFSEVYKAfDLVEQRYV-ACKIhqLNKD-WSEEKKQNYIKHALREYEIHKslDHPRIVKLYDVFEIdTDSFCTVLE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQH--GVIYRDLKLDNILLD---AEGHCKLADFGMCK-----EG 557
Cdd:cd13990    86 YCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIkpPIIHYDLKPGNILLHsgnVSGEIKITDFGLSKimddeSY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVT-TTTFCGTPDYIAPEILQELEYGPS----VDWWALGVLMYEMMAGQPPFEAD--NEDDLFE-SILH-DDVLYPv 628
Cdd:cd13990   166 NSDGMElTSQGAGTYWYLPPECFVVGKTPPKisskVDVWSVGVIFYQMLYGRKPFGHNqsQEAILEEnTILKaTEVEFP- 244

                  ....*...
gi 1958782016 629 wlSKEAVS 636
Cdd:cd13990   245 --SKPVVS 250
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
408-671 5.60e-21

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: 94.51  E-value: 5.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKdviLQDDDVDCtmteKRIL---ALAR--KHPYLTQLYCCFQTKDR- 481
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISN---VFDDLIDA----KRILreiKILRhlKHENIIGLLDILRPPSPe 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 ----LFFVMEYVnGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK-- 555
Cdd:cd07834    75 efndVYIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARgv 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EGILNGVTTTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-------DDVLYP 627
Cdd:cd07834   154 DPDEDKGFLTEYVVTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEvlgtpseEDLKFI 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 628 vwLSKEAVSILKAFMTK--------------------------NPHKRLgcvaaqNGEDAIkQHPFFKEI 671
Cdd:cd07834   234 --SSEKARNYLKSLPKKpkkplsevfpgaspeaidllekmlvfNPKKRI------TADEAL-AHPYLAQL 294
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
412-650 6.92e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 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: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 93.95  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvilqdddvDCTMTEKRILA--LARKHPYLTQLY----CCFQTKDRLFFV 485
Cdd:cd14170     8 QVLGLGINGKVLQIFNKRTQEKFALKMLQ----------DCPKARREVELhwRASQCPHIVRIVdvyeNLYAGRKCLLIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQR--SRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE---GHCKLADFGMCKEGILN 560
Cdd:cd14170    78 MECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GvTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN----EDDLFESILHDDVLYP--VW--LSK 632
Cdd:cd14170   158 N-SLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPnpEWseVSE 236
                         250
                  ....*....|....*...
gi 1958782016 633 EAVSILKAFMTKNPHKRL 650
Cdd:cd14170   237 EVKMLIRNLLKTEPTQRM 254
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
407-668 7.95e-21

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: 93.25  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMlaelKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd07861     1 DYTKIEKIGEGTYGVVY----KGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKelQHPNIVCLEDVLMQENRLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGgDL---MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE-GILN 560
Cdd:cd07861    77 VFEFLSM-DLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAfGIPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 561 GVTTTTFCgTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNE-DDLF-----------------ESILH 621
Cdd:cd07861   156 RVYTHEVV-TLWYRAPEVLlGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEiDQLFrifrilgtptediwpgvTSLPD 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 622 DDVLYPVW-----------LSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIKqHPFF 668
Cdd:cd07861   235 YKNTFPKWkkgslrtavknLDEDGLDLLEKMLIYDPAKRI------SAKKALV-HPYF 285
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
414-650 8.59e-21

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: 93.95  E-value: 8.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNG-G 492
Cdd:cd06633    29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQ-QLKHPNTIEYKGCYLKDHTAWLVMEYCLGsA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRsrkfdEPRSRFYAAEVT----SALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilnGVTTTTFC 568
Cdd:cd06633   108 SDLLEVHK-----KPLQEVEIAAIThgalQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASI----ASPANSFV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 569 GTPDYIAPEI---LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVlyPVWLSKEAVSILKAF---- 641
Cdd:cd06633   179 GTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDS--PTLQSNEWTDSFRGFvdyc 256

                  ....*....
gi 1958782016 642 MTKNPHKRL 650
Cdd:cd06633   257 LQKIPQERP 265
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
411-649 9.37e-21

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: 92.89  E-value: 9.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAElkgkdEVYAVKVLKKDVILQDDDvdcTMTEKRILALAR-----KHPYLTQLYCCFQTKD-RLFF 484
Cdd:cd06620    10 LKDLGAGNGGSVSKVL-----HIPTGTIMAKKVIHIDAK---SSVRKQILRELQilhecHSPYIVSFYGAFLNENnNIII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLH-QHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVT 563
Cdd:cd06620    82 CMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGE-LINSIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTtFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNED-----------DLFESILHD-------DVL 625
Cdd:cd06620   161 DT-FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmgilDLLQRIVNEppprlpkDRI 239
                         250       260
                  ....*....|....*....|....
gi 1958782016 626 YPvwlsKEAVSILKAFMTKNPHKR 649
Cdd:cd06620   240 FP----KDLRDFVDRCLLKDPRER 259
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
414-650 2.76e-20

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: 91.22  E-value: 2.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDD-DVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd14195    13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrGVSREEIEREVNILREiQHPNIITLHDIFENKTDVVLILELVSG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG----HCKLADFGMCKEgILNGVTTTTF 567
Cdd:cd14195    93 GELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHK-IEAGNEFKNI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL---HD-DVLYPVWLSKEAVSILKAFMT 643
Cdd:cd14195   172 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISavnYDfDEEYFSNTSELAKDFIRRLLV 251

                  ....*..
gi 1958782016 644 KNPHKRL 650
Cdd:cd14195   252 KDPKKRM 258
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
412-611 2.78e-20

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: 90.82  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdctMTEK---RILALARK--HPYLTQLYCCFQTKD-RLFFV 485
Cdd:cd14163     6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEE------FIQRflpRELQIVERldHKNIIHVYEMLESADgKIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEgHCKLADFGMCKEGILNGVT-T 564
Cdd:cd14163    80 MELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLPKGGRElS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 565 TTFCGTPDYIAPEILQELEYGPSV-DWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd14163   159 QTFCGSTAYAAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPFDDTD 206
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
243-295 3.08e-20

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 84.42  E-value: 3.08e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
408-649 3.15e-20

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: 90.75  E-value: 3.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIP----YKPEDKQLVLREYQVLRRLS-HPRIAQLHSAYLSPRHLVLIEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTF 567
Cdd:cd14110    80 LCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGtpDYI---APEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV----LYPvWLSKEAVSILKA 640
Cdd:cd14110   160 KG--DYVetmAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVqlsrCYA-GLSGGAVNFLKS 236

                  ....*....
gi 1958782016 641 FMTKNPHKR 649
Cdd:cd14110   237 TLCAKPWGR 245
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
407-649 3.44e-20

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: 90.69  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDDdvdctMTEKRILALARKHPYLTQLY-CCFQTKDrLFFV 485
Cdd:cd05114     5 ELTFMKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEED-----FIEEAKVMMKLTHPKLVQLYgVCTQQKP-IYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLM-FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTT 564
Cdd:cd05114    78 TEFMENGCLLnYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLY-PVWLSKEAVSILKAF 641
Cdd:cd05114   158 SSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGHRLYrPKLASKSVYEVMYSC 237

                  ....*...
gi 1958782016 642 MTKNPHKR 649
Cdd:cd05114   238 WHEKPEGR 245
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
242-292 3.60e-20

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 84.28  E-value: 3.60e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20795     3 PHSLFVHSYKSPTFCDFCGEMLFGLVRQGLKCEGCGLNFHKRCAYKIPNNC 53
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
414-608 3.82e-20

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: 90.25  E-value: 3.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGkdEVYAVKVLKKdviLQDDDVdctmteKRILALarKHPYLTQL---------YCcfqtkdrlfF 484
Cdd:cd14059     1 LGSGAQGAVFLGKFRG--EEVAVKKVRD---EKETDI------KHLRKL--NHPNIIKFkgvctqapcYC---------I 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGVTT 564
Cdd:cd14059    59 LMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKE--LSEKST 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 565 -TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE 608
Cdd:cd14059   137 kMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYK 181
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
483-650 3.86e-20

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 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: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 90.32  E-value: 3.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYvngGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd14024    63 FFSRHY---GDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGD 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 --TTTTFCGTPDYIAPEILQELE--YGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSIL 638
Cdd:cd14024   140 ddSLTDKHGCPAYVGPEILSSRRsySGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLV 219
                         170
                  ....*....|..
gi 1958782016 639 KAFMTKNPHKRL 650
Cdd:cd14024   220 SCMLRRSPAERL 231
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
413-608 3.97e-20

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: 91.14  E-value: 3.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDevYAVKVLKK-----------DVILQDDDVD------CTMTEKRILALARKHPYLTQLY-C 474
Cdd:cd14000     1 LLGDGGFGSVYRASYKGEP--VAVKIFNKhtssnfanvpaDTMLRHLRATdamknfRLLRQELTVLSHLHHPSIVYLLgI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 475 CFQTkdrLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFY----AAEVTSALMFLHQHGVIYRDLKLDNILL-----DAEGH 545
Cdd:cd14000    79 GIHP---LMLVLELAPLGSLDHLLQQDSRSFASLGRTLqqriALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 546 CKLADFGM----CKEGILngvtttTFCGTPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPFE 608
Cdd:cd14000   156 IKIADYGIsrqcCRMGAK------GSEGTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMV 217
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
408-607 4.32e-20

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: 90.84  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTK------DR 481
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKsppghdDQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSR--KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL 559
Cdd:cd06636    94 LWLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 560 NGVTTTTFCGTPDYIAPEILQ-----ELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06636   174 TVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 226
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
407-680 4.40e-20

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: 91.09  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVdcTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd06619     2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQ--IMSELEILYKC-DSPYIIGFYGAFFVENRISICT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLmfqiQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVTTTt 566
Cdd:cd06619    79 EFMDGGSL----DVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQ-LVNSIAKT- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNED-------DLFESILHDD--VLYPVWLSKEAVSI 637
Cdd:cd06619   153 YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNqgslmplQLLQCIVDEDppVLPVGQFSEKFVHF 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 638 LKAFMTKNPHKRLgcvaaqnGEDAIKQHPFFKEID---------WVL--LEQKK 680
Cdd:cd06619   233 ITQCMRKQPKERP-------APENLMDHPFIVQYNdgnaevvsmWVCraLEERR 279
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
408-670 6.03e-20

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin 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: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 90.30  E-value: 6.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVK----VKGADQVLVKKEISILNIAR-HRNILRLHESFESHEELVMIFE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE--GHCKLADFGMCKEgILNGVTT 564
Cdd:cd14104    77 FISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQ-LKPGDKF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-----DDVLYPVwLSKEAVSILK 639
Cdd:cd14104   156 RLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNaeyafDDEAFKN-ISIEALDFVD 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 640 AFMTKNPHKRLGCVAAQNgedaikqHPFFKE 670
Cdd:cd14104   235 RLLVKERKSRMTAQEALN-------HPWLKQ 258
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
406-668 6.13e-20

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: 89.97  E-value: 6.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELK-------GKDEVYAVKVLKKDV----ILQdddvdctmtEKRILALARKHPYLTQLYC 474
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKlhdlydrNKGRLVALKHIYPTSspsrILN---------ELECLERLGGSNNVSGLIT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 475 CFQTKDRLFFVMEYVNGGDlmFQiQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE-GHCKLADFGM 553
Cdd:cd14019    72 AFRNEDQVVAVLPYIEHDD--FR-DFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 554 CkEGILNGVTTTTFC-GTPDYIAPEILqeLEY---GPSVDWWALGVLMYEMMAGQ-PPF-EADNEDDLFE--SILHDDVL 625
Cdd:cd14019   149 A-QREEDRPEQRAPRaGTRGFRAPEVL--FKCphqTTAIDIWSAGVILLSILSGRfPFFfSSDDIDALAEiaTIFGSDEA 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 626 YpvwlskeavSILKAFMTKNPHKRLgcvaaqNGEDAIKqHPFF 668
Cdd:cd14019   226 Y---------DLLDKLLELDPSKRI------TAEEALK-HPFF 252
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
406-668 6.69e-20

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: 90.66  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKvlKKDVILQDDDVDCT-MTEKRILALARKHPYLTQLYCCFQT----KD 480
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALK--KTRLEMEEEGVPSTaLREVSLLQMLSQSIYIVRLLDVEHVeengKP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGgDLMFQIQRSRK-----FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLD-AEGHCKLADFGMC 554
Cdd:cd07837    79 LLYLVFEYLDT-DLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLGLG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KEGILNGVTTTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEddlFESILH------------ 621
Cdd:cd07837   158 RAFTIPIKSYTHEIVTLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSE---LQQLLHifrllgtpneev 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 622 --------DDVLYPVW-----------LSKEAVSILKAFMTKNPHKRLGCVAAQngedaikQHPFF 668
Cdd:cd07837   235 wpgvsklrDWHEYPQWkpqdlsravpdLEPEGVDLLTKMLAYDPAKRISAKAAL-------QHPYF 293
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
409-615 6.91e-20

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: 90.62  E-value: 6.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIKV--LGKGSFGKVmlaeLKGKDEVYAVKVLKKDVILqDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd07836     1 NFKQLekLGEGTYATV----YKGRNRTTGEIVALKEIHL-DAEEGTPSTAIREISLMKelKHENIVRLHDVIHTENKLML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGgDL---MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNG 561
Cdd:cd07836    76 VFEYMDK-DLkkyMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARA---FG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 562 VTTTTFCG---TPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPFEA-DNEDDL 615
Cdd:cd07836   152 IPVNTFSNevvTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGtNNEDQL 210
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
413-607 6.93e-20

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: 90.10  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDevYAVKVLKKDvilQDDDV----DCTMTEKRILALARkHPYLTQLY-CCFQtKDRLFFVME 487
Cdd:cd14146     1 IIGVGGFGKVYRATWKGQE--VAVKAARQD---PDEDIkataESVRQEAKLFSMLR-HPNIIKLEgVCLE-EPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRF---------YAAEVTSALMFLHQHGV---IYRDLKLDNILL----DAEGHC----K 547
Cdd:cd14146    74 FARGGTLNRALAAANAAPGPRRARripphilvnWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLlekiEHDDICnktlK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 548 LADFGMCKEgiLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd14146   154 ITDFGLARE--WHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
465-651 9.31e-20

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: 89.34  E-value: 9.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 465 KHPYLTQLYC--CFQTKD----RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNI 538
Cdd:cd14012    56 RHPNLVSYLAfsIERRGRsdgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 539 LLDA---EGHCKLADFGMCKE--GILNGVTTTTFCGTPdYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPFEadne 612
Cdd:cd14012   136 LLDRdagTGIVKLTDYSLGKTllDMCSRGSLDEFKQTY-WLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGLDVLE---- 210
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958782016 613 ddlfESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLG 651
Cdd:cd14012   211 ----KYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPT 245
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
414-607 1.68e-19

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: 89.59  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCtmtekRILALARKHPYLTQLYCC-------FQTKDRLFFVM 486
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWC-----HEIQIMKKLNHPNVVKACdvpeemnFLVNDVPLLAM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRK---FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG----HcKLADFGMCKEgIL 559
Cdd:cd14039    76 EYCSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivH-KIIDLGYAKD-LD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 560 NGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd14039   154 QGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
408-607 1.84e-19

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: 89.39  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTK------DR 481
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKnppgmdDQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSR--KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL 559
Cdd:cd06637    84 LWLVMEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 560 NGVTTTTFCGTPDYIAPEILQ-----ELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06637   164 TVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
405-610 2.19e-19

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: 88.55  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAvkvLKKDVILQDDDV----DCTmteKRILALAR-KHPYLTQLYCCFQTK 479
Cdd:cd08228     1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVA---LKKVQIFEMMDAkarqDCV---KEIDLLKQlNHPNVIKYLDSFIED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQI---QRSRKFDEPRSRF-YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK 555
Cdd:cd08228    75 NELNIVLELADAGDLSQMIkyfKKQKRLIPERTVWkYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 556 EGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEAD 610
Cdd:cd08228   155 FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
414-650 3.30e-19

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: 88.15  E-value: 3.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVI------LQDDDVDctmTEKRILALARkHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd14194    13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIE---REVSILKEIQ-HPNVITLHEVYENKTDVILILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNI-LLD---AEGHCKLADFGMCKEgILNGVT 563
Cdd:cd14194    89 LVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDrnvPKPRIKIIDFGLAHK-IDFGNE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAF-- 641
Cdd:cd14194   168 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFir 247
                         250
                  ....*....|.
gi 1958782016 642 --MTKNPHKRL 650
Cdd:cd14194   248 rlLVKDPKKRM 258
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
397-649 4.45e-19

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: 88.20  E-value: 4.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 397 QGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKD-------VILQDDDV-----DCtmtekrilalar 464
Cdd:cd06618     6 DGKKYKADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSgnkeenkRILMDLDVvlkshDC------------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 465 khPYLTQLYCCFQTKDRLFFVMEyvnggdLMfqiqrSRKFDEPRSRFY-----------AAEVTSALMFLHQ-HGVIYRD 532
Cdd:cd06618    74 --PYIVKCYGYFITDSDVFICME------LM-----STCLDKLLKRIQgpipedilgkmTVSIVKALHYLKEkHGVIHRD 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 533 LKLDNILLDAEGHCKLADFGMCKEgILNGVTTTTFCGTPDYIAPEIL---QELEYGPSVDWWALGVLMYEMMAGQPPFEA 609
Cdd:cd06618   141 VKPSNILLDESGNVKLCDFGISGR-LVDSKAKTRSAGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYRN 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 610 DNED-DLFESILHDD--VLYP-VWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd06618   220 CKTEfEVLTKILNEEppSLPPnEGFSPDFCSFVDLCLTKDHRYR 263
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
406-635 4.71e-19

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: 87.31  E-value: 4.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDDDVDctmtEKRILaLARKHPYLTQLY-CCFQtKDRLFF 484
Cdd:cd05112     4 SELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEEDFIE----EAEVM-MKLSHPKLVQLYgVCLE-QAPICL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd05112    77 VFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYT 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 564 TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLYPVWLSKEAV 635
Cdd:cd05112   157 SSTGTKFPvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGFRLYKPRLASTHV 230
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
408-649 4.72e-19

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: 87.51  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLK----------KDVIlqdddvdctmteKRILALAR-KHPYLTQLYCCF 476
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSysgkqstekwQDII------------KEVKFLRQlRHPNTIEYKGCY 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 477 QTKDRLFFVMEYVNG--GDLMFQIQRSRKFDEprsrfYAA---EVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADF 551
Cdd:cd06607    71 LREHTAWLVMEYCLGsaSDIVEVHKKPLQEVE-----IAAichGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 552 G----MCKegilngvtTTTFCGTPDYIAPEI---LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD- 623
Cdd:cd06607   146 GsaslVCP--------ANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDs 217
                         250       260
                  ....*....|....*....|....*..
gi 1958782016 624 -VLYPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd06607   218 pTLSSGEWSDDFRNFVDSCLQKIPQDR 244
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
410-600 6.43e-19

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: 87.44  E-value: 6.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELK----GKDEVYAVKVLkkdvilQDDDVDCTMT--EKRILALAR-KHPYLTQL-YCCFQTKDR 481
Cdd:cd05038     8 FIKQLGEGHFGSVELCRYDplgdNTGEQVAVKSL------QPSGEEQHMSdfKREIEILRTlDHEYIVKYkGVCESPGRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 -LFFVMEYVNGGDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegIL 559
Cdd:cd05038    82 sLRLIMEYLPSGSLRDYLQRHRdQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK--VL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 560 NGVTTTTFCGTPD-----YIAPEILQELEYGPSVDWWALGVLMYEM 600
Cdd:cd05038   160 PEDKEYYYVKEPGespifWYAPECLRESRFSSASDVWSFGVTLYEL 205
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
408-607 6.87e-19

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: 88.18  E-value: 6.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd06635    27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRI-KHPNSIEYKGCYLREHTAWLVME 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGG--DLMfQIQRsrkfdEPRSRFYAAEVT----SALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilnG 561
Cdd:cd06635   106 YCLGSasDLL-EVHK-----KPLQEIEIAAIThgalQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASI----A 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 562 VTTTTFCGTPDYIAPEI---LQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06635   176 SPANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPL 224
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
403-607 7.33e-19

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: 86.96  E-value: 7.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 403 LGLDEFNFIKVLGKGSFGKVMLAELKGKDevYAVKVLKKDVILQdddvdCTMTEKRILALARkHPYLTQLY-CCFQTKDR 481
Cdd:cd05082     3 LNMKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCIKNDATAQ-----AFLAEASVMTQLR-HSNLVQLLgVIVEEKGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIqRSRK---FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGi 558
Cdd:cd05082    75 LYIVTEYMAKGSLVDYL-RSRGrsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEA- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 559 lnGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05082   153 --SSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
408-607 1.37e-18

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: 87.00  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd06634    17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLR-HPNTIEYRGCYLREHTAWLVME 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGG--DLMfQIQRsrkfdEPRSRFYAAEVT----SALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGmcKEGILng 561
Cdd:cd06634    96 YCLGSasDLL-EVHK-----KPLQEVEIAAIThgalQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG--SASIM-- 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 562 VTTTTFCGTPDYIAPEI---LQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd06634   166 APANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPL 214
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
406-668 1.43e-18

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: 86.89  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilqDDDVDCTMTEKR---ILaLARKHPyltqlyCCFQTK--- 479
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKME----KEKEGFPITSLReinIL-LKLQHP------NIVTVKevv 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 -----DRLFFVMEYVNGG--DLMfqiqrsrkfDEPRSRFYAAEVT-------SALMFLHQHGVIYRDLKLDNILLDAEGH 545
Cdd:cd07843    74 vgsnlDKIYMVMEYVEHDlkSLM---------ETMKQPFLQSEVKclmlqllSGVAHLHDNWILHRDLKTSNLLLNNRGI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 546 CKLADFGMCKEgilngvttttfCGTPD-----------YIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNED 613
Cdd:cd07843   145 LKICDFGLARE-----------YGSPLkpytqlvvtlwYRAPELLlGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEI 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 614 DLFESILH-----DDVLYPVW---------------------------LSKEAVSILKAFMTKNPHKRLGCvaaqngEDA 661
Cdd:cd07843   214 DQLNKIFKllgtpTEKIWPGFselpgakkktftkypynqlrkkfpalsLSDNGFDLLNRLLTYDPAKRISA------EDA 287

                  ....*..
gi 1958782016 662 IKqHPFF 668
Cdd:cd07843   288 LK-HPYF 293
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
409-608 1.47e-18

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: 86.18  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIKVLGKGSFGKVMLAELKGKDEVYAVKvlkkDVILQDDDVDCTM-TEKRILALARKHPYLTQLYCCFQTKDR-----L 482
Cdd:cd14037     6 TIEKYLAEGGFAHVYLVKTSNGGNRAALK----RVYVNDEHDLNVCkREIEIMKRLSGHKNIVGYIDSSANRSGngvyeV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGG---DLMFQiQRSRKFDEPRSRFYAAEVTSALMFLH--QHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG 557
Cdd:cd14037    82 LLLMEYCKGGgviDLMNQ-RLQTGLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYKLCDFGSATTK 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 558 ILNGVTTTTFC---------GTPDYIAPEIL---QELEYGPSVDWWALGVLMYEMMAGQPPFE 608
Cdd:cd14037   161 ILPPQTKQGVTyveedikkyTTLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPFE 223
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
405-670 1.47e-18

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: 87.61  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAvkvLKK--DVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTK-DR 481
Cdd:cd07852     6 LRRYEILKKLGKGAYGIVWKAIDKKTGEVVA---LKKifDAFRNATDAQRTFREIMFLQELNDHPNIIKLLNVIRAEnDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 -LFFVMEYVNGgDLMFQIqRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK----- 555
Cdd:cd07852    83 dIYLVFEYMET-DLHAVI-RANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARslsql 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 -EGILNGVTTttfcgtpDYIA------PEILqeL---EYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL----- 620
Cdd:cd07852   161 eEDDENPVLT-------DYVAtrwyraPEIL--LgstRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIevigr 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 621 --HDDV-------------------------LYPVwLSKEAVSILKAFMTKNPHKRLGCvaaqngEDAIkQHPFFKE 670
Cdd:cd07852   232 psAEDIesiqspfaatmleslppsrpksldeLFPK-ASPDALDLLKKLLVFNPNKRLTA------EEAL-RHPYVAQ 300
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
406-615 1.47e-18

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: 87.11  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLK---KDVILQDddvdcTMTEKRILALARKhPYLTQLYCCFQTKDRL 482
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleiKPAIRNQ-----IIRELKVLHECNS-PYIVGFYGAFYSDGEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRKFDEPrsrfYAAEVTSA----LMFLHQ-HGVIYRDLKLDNILLDAEGHCKLADFGMckEG 557
Cdd:cd06615    75 SICMEHMDGGSLDQVLKKAGRIPEN----ILGKISIAvlrgLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGV--SG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 558 ILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDL 615
Cdd:cd06615   149 QLIDSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKEL 206
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
424-650 1.56e-18

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 86.69  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 424 LAELKGKDEVYAVKVLKKDVILQD--DDVDCTM---TEKRILALARKHPYLTQLYCCFQ------------------TKD 480
Cdd:cd13974    16 LARKEGTDDFYTLKILTLEEKGEEtqEDRQGKMllhTEYSLLSLLHDQDGVVHHHGLFQdraceikedkssnvytgrVRK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVM-------------EYVNggdLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHck 547
Cdd:cd13974    96 RLCLVLdclcahdfsdktaDLIN---LQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 548 ladfgmckegilnGVTTTTFC----------------GTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEAD 610
Cdd:cd13974   171 -------------KITITNFClgkhlvseddllkdqrGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 611 NEDDLFESILHDDVLYPV--WLSKEAVSILKAFMTKNPHKRL 650
Cdd:cd13974   238 IPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRL 279
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
407-607 1.59e-18

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: 86.25  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAeLKGKDEVyAVKVLKKDvilQDDDVDCTM----TEKRILALArKHPYLTQLY-CCFQTKDr 481
Cdd:cd14145     7 ELVLEEIIGIGGFGKVYRA-IWIGDEV-AVKAARHD---PDEDISQTIenvrQEAKLFAML-KHPNIIALRgVCLKEPN- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG---VIYRDLKLDNILLD--------AEGHCKLAD 550
Cdd:cd14145    80 LCLVMEFARGGPLN-RVLSGKRIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILILekvengdlSNKILKITD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 551 FGMCKEgiLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd14145   159 FGLARE--WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
408-649 2.00e-18

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: 86.20  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAvkvLKKDVILQDDDVDCTMTEKRILALARkHPYLTQL--YCCFQTKD---RL 482
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYA---LKKILCHSKEDVKEAMREIENYRLFN-HPNILRLldSQIVKEAGgkkEV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRK----FDEPRSRFYAAEVTSALMFLHQH---GVIYRDLKLDNILLDAEGHCKLADFGMC- 554
Cdd:cd13986    78 YLLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGSMn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 ---------KEGILNGVTTTTFCgTPDYIAPEiLQELEYG----PSVDWWALGVLMYEMMAGQPPFEADNE--DDLFESI 619
Cdd:cd13986   158 parieiegrREALALQDWAAEHC-TMPYRAPE-LFDVKSHctidEKTDIWSLGCTLYALMYGESPFERIFQkgDSLALAV 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958782016 620 LHDDVLYPV--WLSKEAVSILKAFMTKNPHKR 649
Cdd:cd13986   236 LSGNYSFPDnsRYSEELHQLVKSMLVVNPAER 267
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
405-671 2.09e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 86.41  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVmlaeLKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRL 482
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVV----YKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKemQHGNIVRLQDVVHSEKRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGgDLMFQIQRSRKFDE-PRS-RFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC-KLADFGMCKEgil 559
Cdd:PLN00009   77 YLVFEYLDL-DLKKHMDSSPDFAKnPRLiKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNAlKLADFGLARA--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTFCG---TPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE-DDLFE----------------S 618
Cdd:PLN00009  153 FGIPVRTFTHevvTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEiDELFKifrilgtpneetwpgvT 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 619 ILHD-DVLYPVW-----------LSKEAVSILKAFMTKNPHKRLGCVAAQngedaikQHPFFKEI 671
Cdd:PLN00009  233 SLPDyKSAFPKWppkdlatvvptLEPAGVDLLSKMLRLDPSKRITARAAL-------EHEYFKDL 290
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
407-619 2.42e-18

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: 85.56  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKkdvilQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05148     7 EFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILK-----SDDLLKQQDFQKEVQALKRlRHKHLISLFAVCSVGEPVYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRS--RKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGVT 563
Cdd:cd05148    81 TELMEKGSLLAFLRSPegQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARL-IKEDVY 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 564 TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05148   160 LSSDKKIPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQI 217
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
243-292 2.43e-18

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 78.91  E-value: 2.43e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVaPNC 292
Cdd:cd20817     1 HSFQEHTFKKPTFCDVCKELLVGLSKQGLRCKNCKMNVHHKCQEGV-PDC 49
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
374-671 2.61e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 88.17  E-value: 2.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 374 EEHRASSSTDGQlasPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCT 453
Cdd:PTZ00036   37 EEERSHNNNAGE---DEDEEKMIDNDINRSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIM 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 454 MTEKRILALARKHPYLTQlycCFQTKDRLFF---VMEYVNggdlmfqiQRSRKFDEPRSR-----------FYAAEVTSA 519
Cdd:PTZ00036  114 KNLNHINIIFLKDYYYTE---CFKKNEKNIFlnvVMEFIP--------QTVHKYMKHYARnnhalplflvkLYSYQLCRA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 520 LMFLHQHGVIYRDLKLDNILLDAEGHC-KLADFGMCKEgILNGVTTTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLM 597
Cdd:PTZ00036  183 LAYIHSKFICHRDLKPQNLLIDPNTHTlKLCDFGSAKN-LLAGQRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCII 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 598 YEMMAGQPPFEADNEDDLFESIL-----------------HDDVLYPVWLSK------------EAVSILKAFMTKNPHK 648
Cdd:PTZ00036  262 AEMILGYPIFSGQSSVDQLVRIIqvlgtptedqlkemnpnYADIKFPDVKPKdlkkvfpkgtpdDAINFISQFLKYEPLK 341
                         330       340
                  ....*....|....*....|...
gi 1958782016 649 RLGCVAAQngedaikQHPFFKEI 671
Cdd:PTZ00036  342 RLNPIEAL-------ADPFFDDL 357
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
242-302 2.84e-18

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 79.70  E-value: 2.84e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC-GVDARGIAKV 302
Cdd:cd20841    10 PHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCsGVRKRRLSNV 71
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
413-656 2.85e-18

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: 85.04  E-value: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMlaelKG--KDEVYAVKVLKKDvilQDDDVDCTM----TEKRILALARkHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14148     1 IIGVGGFGKVY----KGlwRGEEVAVKAARQD---PDEDIAVTAenvrQEARLFWMLQ-HPNIIALRGVCLNPPHLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG---VIYRDLKLDNILL--DAEGH------CKLADFGMCK 555
Cdd:cd14148    73 EYARGGALN-RALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILIlePIENDdlsgktLKITDFGLAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgiLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEadnEDDLFEsilhddVLYPVWLSKEAV 635
Cdd:cd14148   152 E--WHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR---EIDALA------VAYGVAMNKLTL 220
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958782016 636 SI-----------LKAFMTKNPHKR--LGCVAAQ 656
Cdd:cd14148   221 PIpstcpepfarlLEECWDPDPHGRpdFGSILKR 254
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
412-608 3.20e-18

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: 84.64  E-value: 3.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVyAVKVLKKDvilqdddvdcTMTEKRILALAR-----KHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLKPG----------TMSPEAFLQEAQimkklRHDKLVQLYAVCSDEEPIYIVT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLM--FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG---MCKEGILNG 561
Cdd:cd05034    70 ELMSKGSLLdyLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGlarLIEDDEYTA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 562 VTTTTFcgtP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFE 608
Cdd:cd05034   150 REGAKF---PiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYP 195
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
405-610 4.09e-18

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: 85.47  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKK-DVILQDDDVDCTmteKRILALAR-KHPYLTQLYCCFQTKDRL 482
Cdd:cd08229    23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDAKARADCI---KEIDLLKQlNHPNVIKYYASFIEDNEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRK----FDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGI 558
Cdd:cd08229   100 NIVLELADAGDLSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 559 LNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEAD 610
Cdd:cd08229   180 SKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
414-607 4.33e-18

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: 84.50  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKdeVYAVKVLKKDVILQDDDVDCTMTEKRILAlARKHPYLTQLY-CCFQTKDRLFFVMEYVNGG 492
Cdd:cd14064     1 IGSGSFGKVYKGRCRNK--IVAIKRYRANTYCSKSDVDMFCREVSILC-RLNHPCVIQFVgACLDDPSQFAIVTQYVSGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRF-YAAEVTSALMFLHQ--HGVIYRDLKLDNILLDAEGHCKLADFG----MCKegiLNGVTTT 565
Cdd:cd14064    78 SLFSLLHEQKRVIDLQSKLiIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGesrfLQS---LDEDNMT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 566 TFCGTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd14064   155 KQPGNLRWMAPEVFtQCTRYSIKADVFSYALCLWELLTGEIPF 197
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
382-667 5.07e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 86.03  E-value: 5.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 382 TDGQLASPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMT-EKRIL 460
Cdd:PLN00034   50 PSSSSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN---HEDTVRRQICrEIEIL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 461 ALArKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLmfqiQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL 540
Cdd:PLN00034  127 RDV-NHPNVVKCHDMFDHNGEIQVLLEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 541 DAEGHCKLADFGMCKegILNgvTTTTFC----GTPDYIAPE-ILQELEYGP----SVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:PLN00034  202 NSAKNVKIADFGVSR--ILA--QTMDPCnssvGTIAYMSPErINTDLNHGAydgyAGDIWSLGVSILEFYLGRFPFGVGR 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 612 EDD---LFESI-LHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGcvAAQngedaIKQHPF 667
Cdd:PLN00034  278 QGDwasLMCAIcMSQPPEAPATASREFRHFISCCLQREPAKRWS--AMQ-----LLQHPF 330
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
170-220 5.78e-18

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 77.87  E-value: 5.78e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWG-LGKQGLKCSWCKLNVHKRCHEKVPPEC 50
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
408-649 6.01e-18

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: 84.10  E-value: 6.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVL-----KKDVILQDDDVDCTMTEKRILALarKHPYLTQLYccfqtkdrL 482
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqaeEKQGVLQEYEILKSLHHERIMAL--HEAYITPRY--------L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE-GILNG 561
Cdd:cd14111    75 VLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSfNPLSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEaDNEDDLFESILHDD-----VLYPVwLSKEAVS 636
Cdd:cd14111   155 RQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE-DQDPQETEAKILVAkfdafKLYPN-VSQSASL 232
                         250
                  ....*....|...
gi 1958782016 637 ILKAFMTKNPHKR 649
Cdd:cd14111   233 FLKKVLSSYPWSR 245
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
406-623 6.02e-18

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: 85.49  E-value: 6.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqdddvDCTMTEKRILALARKH----PYLTQLYCCFQTKDR 481
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEI-------KPAIRNQIIRELQVLHecnsPYIVGFYGAFYSDGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQ-HGVIYRDLKLDNILLDAEGHCKLADFGMckEGILN 560
Cdd:cd06650    78 ISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGV--SGQLI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 561 GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQ---PPFEADNEDDLFESILHDD 623
Cdd:cd06650   156 DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRypiPPPDAKELELMFGCQVEGD 221
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
414-668 6.50e-18

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: 84.63  E-value: 6.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMlaelKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARK-----HPYLTQLY--CCFQTKDR---LF 483
Cdd:cd07863     8 IGVGAYGTVY----KARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRleafdHPNIVRLMdvCATSRTDRetkVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGgDLMFQIQRSRKFDEP--RSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK----EG 557
Cdd:cd07863    84 LVFEHVDQ-DLRTYLDKVPPPGLPaeTIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARiyscQM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTFcgtpdYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL-------HDDVLYPVWL 630
Cdd:cd07863   163 ALTPVVVTLW-----YRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFdliglppEDDWPRDVTL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 631 SKEAVS--------------------ILKAFMTKNPHKRLGCVAAQngedaikQHPFF 668
Cdd:cd07863   238 PRGAFSprgprpvqsvvpeieesgaqLLLEMLTFNPHKRISAFRAL-------QHPFF 288
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
407-620 6.88e-18

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: 84.70  E-value: 6.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLA-ELKGKDEVYAVKVLKkdviLQDDDVDCTMTEKRILALAR-----KHPYLTQLY--CCFQT 478
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKArDLKNGGRFVALKRVR----VQTGEEGMPLSTIREVAVLRhletfEHPNVVRLFdvCTVSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDR---LFFVMEYVNGgDLMFQIQRSRKFDEPRSRF--YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM 553
Cdd:cd07862    78 TDRetkLTLVFEHVDQ-DLTTYLDKVPEPGVPTETIkdMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 554 CKEGILNgVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd07862   157 ARIYSFQ-MALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKIL 222
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
406-670 8.11e-18

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: 85.42  E-value: 8.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKK---DVIlqddDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRL 482
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfqSAI----HAKRTYRELRLLKHMK-HENVIGLLDVFTPASSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 ------FFVMEYVnGGDLmFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKe 556
Cdd:cd07851    90 edfqdvYLVTHLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 giLNGVTTTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH------DDVL---- 625
Cdd:cd07851   167 --HTDDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNlvgtpdEELLkkis 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 626 ----------YPV-----------WLSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFFKE 670
Cdd:cd07851   245 sesarnyiqsLPQmpkkdfkevfsGANPLAIDLLEKMLVLDPDKRI------TAAEAL-AHPYLAE 303
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
405-668 8.68e-18

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: 84.67  E-value: 8.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAvkvLKKdvILQDDDVD----CTMTEKRILALArKHPYLTQLYCCF---- 476
Cdd:cd07866     7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVA---LKK--ILMHNEKDgfpiTALREIKILKKL-KHPNVVPLIDMAverp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 477 --QTKDR--LFFVMEYVNGgDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADF 551
Cdd:cd07866    81 dkSKRKRgsVYMVTPYMDH-DLSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 552 GMC--------KEGILNGVTTTTFCG---TPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI 619
Cdd:cd07866   160 GLArpydgpppNPKGGGGGGTRKYTNlvvTRWYRPPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLI 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 620 LH-----DDVLYPVW-------------------------LSKEAVSILKAFMTKNPHKRLGCVAAqngedaiKQHPFF 668
Cdd:cd07866   240 FKlcgtpTEETWPGWrslpgcegvhsftnyprtleerfgkLGPEGLDLLSKLLSLDPYKRLTASDA-------LEHPYF 311
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
243-292 1.19e-17

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 76.79  E-value: 1.19e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
239-292 1.30e-17

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 77.71  E-value: 1.30e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 239 VNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20843     8 VKVPHTFVIHSYTRPTVCQFCKKLLKGLFRQGLQCKDCKFNCHKRCATRVPNDC 61
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
239-292 1.30e-17

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 78.52  E-value: 1.30e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 239 VNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20842    31 VKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCKFNCHKRCAPKVPNNC 84
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
242-302 1.49e-17

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 77.37  E-value: 1.49e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC-GVDARGIAKV 302
Cdd:cd20839     7 PHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCsGVRKRRLSNV 68
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
407-607 1.50e-17

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: 82.78  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDevYAVKVLKKDVILQDDDVD--CTMTEKRilalarkHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05039     7 DLKLGELIGKGEFGDVMLGDYRGQK--VAVKCLKDDSTAAQAFLAeaSVMTTLR-------HPNLVQLLGVVLEGNGLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMfqiqrsrkfDEPRSR-----------FYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM 553
Cdd:cd05039    78 VTEYMAKGSLV---------DYLRSRgravitrkdqlGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 554 CKEGILNgVTTTTFcgtP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05039   149 AKEASSN-QDGGKL---PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
466-668 1.54e-17

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: 82.94  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 466 HPYLTQLYCCFQTKDRLFFVMEYVNGG--DLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLdA 542
Cdd:cd14109    55 HPNIVQMHDAYDDEKLAVTVIDNLASTieLVRDNLLPGKdYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-Q 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 543 EGHCKLADFGMCKEgILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH- 621
Cdd:cd14109   134 DDKLKLADFGQSRR-LLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSg 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 622 -----DDVLYPVwlSKEAVSILKAFMTKNPHKRLGCVAAQNgedaikqHPFF 668
Cdd:cd14109   213 kwsfdSSPLGNI--SDDARDFIKKLLVYIPESRLTVDEALN-------HPWF 255
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
406-619 1.59e-17

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: 83.17  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVIlqddDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd05072     7 ESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM----SVQAFLEEANLMK-TLQHDKLVRLYAVVTKEEPIYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLM--FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd05072    81 TEYMAKGSLLdfLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 564 TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05072   161 AREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSAL 218
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
414-622 2.71e-17

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: 82.93  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDevYAVKVLKKDVILQDDDVDCTMtEKRILALAR-KHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14158    23 LGEGGFGVVFKGYINDKN--VAVKKLAAMVDISTEDLTKQF-EQEIQVMAKcQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIqrSRKFDEP----RSRFYAAEVTS-ALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT--TT 565
Cdd:cd14158   100 SLLDRL--ACLNDTPplswHMRCKIAQGTAnGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTimTE 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 566 TFCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD 622
Cdd:cd14158   178 RIVGTTAYMAPEALRG-EITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIKEE 233
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
412-607 3.26e-17

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: 81.98  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVyAVKVLKKDvILQDDDVDcTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNG 491
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDKTPV-AVKTCKED-LPQELKIK-FLSEARILK-QYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRkfDEPRSR---FYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFC 568
Cdd:cd05085    78 GDFLSFLRKKK--DELKTKqlvKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 569 GTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05085   156 QIPiKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPY 196
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
405-667 3.28e-17

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: 82.93  E-value: 3.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAvkvLKKdVILQDDDVDCTMT---EKRIL------ALARKHPYLT--QLY 473
Cdd:cd07864     6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVA---LKK-VRLDNEKEGFPITairEIKILrqlnhrSVVNLKEIVTdkQDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 474 CCFQTKDRLFF-VMEYVNGgDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADF 551
Cdd:cd07864    82 LDFKKDKGAFYlVFEYMDH-DLMGLLESGLvHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 552 GMC-------KEGILNGVTTTTfcgtpdYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-- 621
Cdd:cd07864   161 GLArlynseeSRPYTNKVITLW------YRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRlc 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 622 ---------DDVLYPVW-------------------LSKEAVSILKAFMTKNPHKRlgCVAaqngEDAIkQHPF 667
Cdd:cd07864   235 gspcpavwpDVIKLPYFntmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKR--CTA----EQAL-NSPW 301
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
412-614 3.31e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 83.27  E-value: 3.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQD--------DDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDR 481
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDvtkdrqlvGMCGIHFTTLRELKIMNeiKHENIMGLVDVYVEGDF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGgDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG 561
Cdd:PTZ00024   95 INLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPP 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 562 VTTTTFCG---------TPD-----YIAPEILQELE-YGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:PTZ00024  174 YSDTLSKDetmqrreemTSKvvtlwYRAPELLMGAEkYHFAVDMWSVGCIFAELLTGKPLFPGENEID 241
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
411-607 3.33e-17

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: 82.70  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd07870     5 LEKLGEGSYATVYKGISRINGQLVALKVISMKT---EEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGT 570
Cdd:cd07870    82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVVT 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958782016 571 PDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd07870   162 LWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAF 199
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
242-292 3.68e-17

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 75.74  E-value: 3.68e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20792     1 GHKFVATFFKQPTFCSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKC 51
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
414-599 4.08e-17

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: 81.72  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDDDVDCTMTEKRILaLARKHPYLTQLY-CCFQtKDRLFFVMEYVNGG 492
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTCRET--LPPDLKRKFLQEARIL-KQYDHPNIVKLIgVCVQ-KQPIMIVMELVPGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSA-LMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGilNGVTTTTFCGTP 571
Cdd:cd05041    79 SLLTFLRKKGARLTVKQLLQMCLDAAAgMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREE--EDGEYTVSDGLK 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958782016 572 D----YIAPEILQELEYGPSVDWWALGVLMYE 599
Cdd:cd05041   157 QipikWTAPEALNYGRYTSESDVWSFGILLWE 188
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
413-649 5.29e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 81.17  E-value: 5.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDV-DCTMTEKRILALAR---KHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd14100     7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELpNGTRVPMEIVLLKKvgsGFRGVIRLLDWFERPDSFVLVLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNG-GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLD-AEGHCKLADFGmcKEGILNGVTTTT 566
Cdd:cd14100    87 PEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFG--SGALLKDTVYTD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTPDYIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADneddlfESILHDDVLYPVWLSKEAVSILKAFMTKN 645
Cdd:cd14100   165 FDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHD------EEIIRGQVFFRQRVSSECQHLIKWCLALR 238

                  ....
gi 1958782016 646 PHKR 649
Cdd:cd14100   239 PSDR 242
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
415-608 6.04e-17

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: 80.77  E-value: 6.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 415 GKGSFGKVMLAELKGKDEVYAVKVLKKdvilqdddvdcTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVMEYVNGGDL 494
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLK-----------IEKEAEILSVL-SHRNIIQFYGAILEAPNYGIVTEYASYGSL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 495 M--FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG---VIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVTTTTFCG 569
Cdd:cd14060    70 FdyLNSNESEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTTHMSLVG 147
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958782016 570 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE 608
Cdd:cd14060   148 TFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFK 186
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
406-686 6.36e-17

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: 82.41  E-value: 6.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKK--DVILQDDDvdcTMTEKRILaLARKHPYLTQLYCCFQTK---- 479
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNafDVVTTAKR---TLRELKIL-RHFKHDNIIAIRDILRPKvpya 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 --DRLFFVMEYVNGgDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEG 557
Cdd:cd07855    81 dfKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNGVTTTTF----CGTPDYIAPEILQEL-EYGPSVDWWALGVLMYEM---------------------MAGQPPFE--- 608
Cdd:cd07855   160 CTSPEEHKYFmteyVATRWYRAPELMLSLpEYTQAIDMWSVGCIFAEMlgrrqlfpgknyvhqlqliltVLGTPSQAvin 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 609 ---ADNEDDLFESILHD-----DVLYPVwLSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFFKEIDWVLLEQKK 680
Cdd:cd07855   240 aigADRVRRYIQNLPNKqpvpwETLYPK-ADQQALDLLSQMLRFDPSERI------TVAEAL-QHPFLAKYHDPDDEPDC 311

                  ....*.
gi 1958782016 681 iKPPFK 686
Cdd:cd07855   312 -APPFD 316
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
411-668 8.12e-17

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: 81.27  E-value: 8.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd07844     5 LDKLGEGSYATVYKGRSKLTGQLVALKEIR---LEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GgDLMFQIQRSRKFDEPRS-RFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNGVTTTTFCG 569
Cdd:cd07844    82 T-DLKQYMDDCGGGLSMHNvRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA---KSVPSKTYSN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 ---TPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPF--EADNEDDL---FES-----------ILHDDVLYPVW 629
Cdd:cd07844   158 evvTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFpgSTDVEDQLhkiFRVlgtpteetwpgVSSNPEFKPYS 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 630 LSK-----------------EAVSILKAFMTKNPHKRLGcvaaqnGEDAIKqHPFF 668
Cdd:cd07844   238 FPFypprplinhaprldripHGEELALKFLQYEPKKRIS------AAEAMK-HPYF 286
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
411-619 8.47e-17

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: 80.97  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDE-----VYAVKVLKKdvilqDDDVDCTMTEKRILALARK--HPYLTQLYCCFQTKDRLF 483
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAKGIEEeggetLVLVKALQK-----TKDENLQSEFRRELDMFRKlsHKNVVRLLGLCREAEPHY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSR---------FYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC 554
Cdd:cd05046    85 MILEYTDLGDLKQFLRATKSKDEKLKPpplstkqkvALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLS 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 555 KEgilngVTTTTFCGTPD------YIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05046   165 KD-----VYNSEYYKLRNaliplrWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRL 231
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
414-668 8.58e-17

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: 81.33  E-value: 8.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKvlkkDVILQDDDVDCTMTEKRILALAR--KHPYLTQLYCCFQTKDRLFFVMEYVNg 491
Cdd:cd07839     8 IGEGTYGTVFKAKNRETHEIVALK----RVRLDDDDEGVPSSALREICLLKelKHKNIVRLYDVLHSDKKLTLVFEYCD- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 gdlmfqiQRSRKF--------DEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNGVT 563
Cdd:cd07839    83 -------QDLKKYfdscngdiDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA---FGIP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCG---TPDYIAPEILQELE-YGPSVDWWALGVLMYEMM-AGQPPFEADNEDDLFESI-----------------LH 621
Cdd:cd07839   153 VRCYSAevvTLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIfrllgtpteeswpgvskLP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 622 DDVLYPVW------------LSKEAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFF 668
Cdd:cd07839   233 DYKPYPMYpattslvnvvpkLNSTGRDLLQNLLVCNPVQRI------SAEEAL-QHPYF 284
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
407-601 1.00e-16

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: 81.83  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilqDDDVDCTMTEKRIL-ALARKHPYLTQLYCCFQTKDRLF-- 483
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNA---PENVELALREFWALsSIQRQHPNVIQLEECVLQRDGLAqr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 ----------------------------------FVMEYVNGGDlMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVI 529
Cdd:cd13977    78 mshgssksdlylllvetslkgercfdprsacylwFVMEFCDGGD-MNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 530 YRDLKLDNILLD---AEGHCKLADFGM---CKEGILNGVTT--------TTFCGTPDYIAPEILqELEYGPSVDWWALGV 595
Cdd:cd13977   157 HRDLKPDNILIShkrGEPILKVADFGLskvCSGSGLNPEEPanvnkhflSSACGSDFYMAPEVW-EGHYTAKADIFALGI 235

                  ....*.
gi 1958782016 596 LMYEMM 601
Cdd:cd13977   236 IIWAMV 241
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
406-607 1.02e-16

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: 80.70  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDvilqdddvdcTMTEKRILALAR-----KHPYLTQLYCCFqTKD 480
Cdd:cd05067     7 ETLKLVERLGAGQFGEVWMGYYNGHTKV-AIKSLKQG----------SMSPDAFLAEANlmkqlQHQRLVRLYAVV-TQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRF--YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGI 558
Cdd:cd05067    75 PIYIITEYMENGSLVDFLKTPSGIKLTINKLldMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 559 LNGVTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05067   155 DNEYTAREGAKFPiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPY 205
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
513-619 1.87e-16

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: 79.84  E-value: 1.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 513 AAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK-EGILNGvtttTFCGTPDYIAPEILQElEYGPSVDWW 591
Cdd:cd13975   108 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFSG-KYDNSVDVY 182
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958782016 592 ALGVLMYEMMAGQ----PPFE-ADNEDDLFESI 619
Cdd:cd13975   183 AFGILFWYLCAGHvklpEAFEqCASKDHLWNNV 215
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
242-292 1.92e-16

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 73.69  E-value: 1.92e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20798     1 PHTLAEHNYKKPTVCKVCDKLLVGLVRQGLKCRDCGVNVHKKCASLLPSNC 51
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
242-293 2.46e-16

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 73.12  E-value: 2.46e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCG 293
Cdd:cd20824     1 PHNFKPHSFSIPTKCDYCGEKIWGLSKKGLSCKDCGFNCHIKCELKVPPECP 52
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
405-601 2.47e-16

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: 79.92  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVK-VLKKDVILQDDDVdctMTEKRILALArKHPYLTQLYCC-------- 475
Cdd:cd14048     5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKrIRLPNNELAREKV---LREVRALAKL-DHPGIVRYFNAwlerppeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 476 FQTKDR---LFFVMEYVNGGDLMFQIQRsRKFDEPRSRFYA----AEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKL 548
Cdd:cd14048    81 WQEKMDevyLYIQMQLCRKENLKDWMNR-RCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 549 ADFGMC--------KEGILN----GVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMM 601
Cdd:cd14048   160 GDFGLVtamdqgepEQTVLTpmpaYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
406-649 2.62e-16

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: 79.50  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFgKVMLAELKGKDEVYAVKVLKkdVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14112     3 GRFSFGSEIFRGRF-SVIVKAVDSTTETDAHCAVK--IFEVSDEASEAVREFESLRTLQ-HENVQRLIAAFKPSNFAYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGgDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDA--EGHCKLADFGMCKEgiLNGVT 563
Cdd:cd14112    79 MEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSvrSWQVKLVDFGRAQK--VSKLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFCGTPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPF--EADNEDDLFESILH---DDVLYPVWLSKEAVSI 637
Cdd:cd14112   156 KVPVDGDTDWASPEFHNpETPITVQSDIWGLGVLTFCLLSGFHPFtsEYDDEEETKENVIFvkcRPNLIFVEATQEALRF 235
                         250
                  ....*....|..
gi 1958782016 638 LKAFMTKNPHKR 649
Cdd:cd14112   236 ATWALKKSPTRR 247
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
492-650 2.78e-16

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 79.01  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTF--CG 569
Cdd:cd13976    69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGEDDSLSdkHG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 570 TPDYIAPEIL--QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPH 647
Cdd:cd13976   149 CPAYVSPEILnsGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPS 228

                  ...
gi 1958782016 648 KRL 650
Cdd:cd13976   229 ERL 231
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
242-294 2.84e-16

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 73.28  E-value: 2.84e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGV 294
Cdd:cd20797     3 PHVVEVEQYMTPTFCDYCGEMLTGLMKQGVKCKNCRCNFHKRCANAPRNNCAA 55
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
410-607 3.05e-16

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: 79.37  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDvilqdddvdcTMTEKRILALAR-----KHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05068    12 LLRKLGSGQFGEVWEGLWNNTTPV-AVKTLKPG----------TMDPEDFLREAQimkklRHPKLIQLYAVCTLEEPIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRS-RKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK----EGIL 559
Cdd:cd05068    81 ITELMKHGSLLEYLQGKgRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARvikvEDEY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTFcgtP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05068   161 EAREGAKF---PiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPY 207
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
410-607 3.07e-16

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: 80.05  E-value: 3.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKV--LGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd07873     4 YIKLdkLGEGTYATVYKGRSKLTDNLVALKEIRLE---HEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTF 567
Cdd:cd07873    81 YLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 568 CGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd07873   161 VVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLF 201
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
406-668 3.48e-16

Catalytic kinase domain, first 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: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 78.79  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVlkkdVILQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKF----IPVRAKKKTSARRELALLA-ELDHKSIVRFHDAFEKRRVVIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGgDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL--DAEGHCKLADFGMCKEGILNgvt 563
Cdd:cd14108    77 TELCHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPN--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFC--GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSI 637
Cdd:cd14108   153 EPQYCkyGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEesmfKDLCREAKGF 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958782016 638 LKAFMTKNphkRLGCVAAQNGEdaikqHPFF 668
Cdd:cd14108   233 IIKVLVSD---RLRPDAEETLE-----HPWF 255
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
485-672 4.05e-16

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: 79.08  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRKFDEPRSRFYAaEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTT 564
Cdd:cd14027    69 VMEYMEKGNLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTK 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 TTFC-------------GTPDYIAPEILQELEYGPS--VDWWALGVLMYEMMAGQPPFE-ADNEDDLFESILH----DDV 624
Cdd:cd14027   148 EEHNeqrevdgtakknaGTLYYMAPEHLNDVNAKPTekSDVYSFAIVLWAIFANKEPYEnAINEDQIIMCIKSgnrpDVD 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 625 LYPVWLSKEAVSILKAFMTKNPHKRlgcvaaqngedaikqhPFFKEID 672
Cdd:cd14027   228 DITEYCPREIIDLMKLCWEANPEAR----------------PTFPGIE 259
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
414-607 4.25e-16

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: 79.28  E-value: 4.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVmlaeLKGKDEVYAVKVLKKDVILQDDD-VDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYV--- 489
Cdd:cd07871    13 LGEGTYATV----FKGRSKLTENLVALKEIRLEHEEgAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLdsd 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 ------NGGDLMfqiqrsrkfDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNGVT 563
Cdd:cd07871    89 lkqyldNCGNLM---------SMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA---KSVP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958782016 564 TTTFCG---TPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd07871   157 TKTYSNevvTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMF 204
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
242-292 4.39e-16

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 73.17  E-value: 4.39e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20840    10 PHALNVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNC 60
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
242-292 4.97e-16

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 72.45  E-value: 4.97e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20827     1 PHRFEKHNFTTPTYCDYCSSLLWGLVKTGMRCADCGYSCHEKCLEHVPKNC 51
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
405-612 5.58e-16

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: 78.70  E-value: 5.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVK--VLKKDVIlqdDDVDCTMTEKRILAlARKHPYLTQLYCCFqtkdrl 482
Cdd:cd14049     5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKkiLIKKVTK---RDCMKVLREVKVLA-GLQHPNIVGYHTAW------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 ffvMEYVNggdLMFQIQ--------------RSRKFDEPRSR-----FYAAEVTSALM--------FLHQHGVIYRDLKL 535
Cdd:cd14049    75 ---MEHVQ---LMLYIQmqlcelslwdwiveRNKRPCEEEFKsapytPVDVDVTTKILqqllegvtYIHSMGIVHRDLKP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 536 DNILLDAEG-HCKLADFGM-CKEGI-----------LNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA 602
Cdd:cd14049   149 RNIFLHGSDiHVRIGDFGLaCPDILqdgndsttmsrLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ 228
                         250
                  ....*....|
gi 1958782016 603 gqpPFEADNE 612
Cdd:cd14049   229 ---PFGTEME 235
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
408-667 5.74e-16

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: 79.76  E-value: 5.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKG--KDEVYAVK----VLKKDVILQDddvdcTMTEKRILALARKHPYLTQLY---CCFQT 478
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAEtsEEETVAIKkitnVFSKKILAKR-----ALRELKLLRHFRGHKNITCLYdmdIVFPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--- 555
Cdd:cd07857    77 NFNELYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARgfs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 ------EGILNGVTTTTFcgtpdYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH------D 622
Cdd:cd07857   157 enpgenAGFMTEYVATRW-----YRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQvlgtpdE 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 623 DVL-----------------YP----VWL----SKEAVSILKAFMTKNPHKRLGCvaaqngEDAIkQHPF 667
Cdd:cd07857   232 ETLsrigspkaqnyirslpnIPkkpfESIfpnaNPLALDLLEKLLAFDPTKRISV------EEAL-EHPY 294
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
406-616 6.02e-16

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: 79.71  E-value: 6.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVilQDDDVDCTMTEKRILALARKhPYLTQLYCCFQTKDRLFFV 485
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEI--KPAIRNQIIRELQVLHECNS-PYIVGFYGAFYSDGEISIC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQ-HGVIYRDLKLDNILLDAEGHCKLADFGMckEGILNGVTT 564
Cdd:cd06649    82 MEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREkHQIMHRDVKPSNILVNSRGEIKLCDFGV--SGQLIDSMA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 565 TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQ---PPFEADNEDDLF 616
Cdd:cd06649   160 NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRypiPPPDAKELEAIF 214
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
242-292 6.70e-16

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 71.96  E-value: 6.70e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20806     1 PHNFKVHTFKGPHWCDYCGNFMWGLIAQGVKCEDCGFNAHKQCSKLVPHDC 51
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
406-619 8.12e-16

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: 78.19  E-value: 8.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDDDVDCTMTEKRIlalarKHPYLTQLYCCFqTKDRLFFV 485
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSPESFLEEAQIMKKL-----KHDKLVQLYAVV-SEEPIYIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQ--RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVT 563
Cdd:cd05070    82 TEYMSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 564 TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05070   162 ARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 219
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
411-608 8.52e-16

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: 78.42  E-value: 8.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd14026     2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKAR-FSYILPILGICNEPEFLGIVTEYMT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFDE---PRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNILLDAEGHCKLADFGMCKEGILN----- 560
Cdd:cd14026    81 NGSLNELLHEKDIYPDvawPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSisqsr 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 561 GVTTTTFCGTPDYIAPEilqelEYGPSV--------DWWALGVLMYEMMAGQPPFE 608
Cdd:cd14026   161 SSKSAPEGGTIIYMPPE-----EYEPSQkrrasvkhDIYSYAIIMWEVLSRKIPFE 211
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
407-620 8.68e-16

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: 78.42  E-value: 8.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVY---AVKVLKKDVILQDDDVDCTmtekRILALARK--HPYLTQLYCCF---QT 478
Cdd:cd05074    10 QFTLGRMLGKGEFGSVREAQLKSEDGSFqkvAVKMLKADIFSSSDIEEFL----REAACMKEfdHPNVIKLIGVSlrsRA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDRL---FFVMEYVNGGDLMFQIQRSRKFDEPRS-------RFyAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKL 548
Cdd:cd05074    86 KGRLpipMVILPFMKHGDLHTFLLMSRIGEEPFTlplqtlvRF-MIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCV 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 549 ADFGMCKEgILNGVTTTTFCGTP---DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESIL 620
Cdd:cd05074   165 ADFGLSKK-IYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLI 239
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
406-615 8.78e-16

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: 78.58  E-value: 8.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKkdvILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR---LQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTT 565
Cdd:cd07869    82 FEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 566 TFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEA--DNEDDL 615
Cdd:cd07869   162 NEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmkDIQDQL 214
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
477-668 9.74e-16

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 77.38  E-value: 9.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 477 QTKDRLFFVMEYvngGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 556
Cdd:cd14022    57 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 GILNGV--TTTTFCGTPDYIAPEILQEL-EY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSK 632
Cdd:cd14022   134 YILRGHddSLSDKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSP 213
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958782016 633 EAVSILKAFMTKNPHKRLgcvaaqnGEDAIKQHPFF 668
Cdd:cd14022   214 KAKCLIRSILRREPSERL-------TSQEILDHPWF 242
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
410-615 1.13e-15

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: 78.50  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKV--LGKGSFGKVMLAELKGKDEVYAVKVLKKDvilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd07872     8 YIKLekLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTF 567
Cdd:cd07872    85 YLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNE 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 568 CGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADN-EDDL 615
Cdd:cd07872   165 VVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTvEDEL 214
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
239-292 1.21e-15

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 71.97  E-value: 1.21e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 239 VNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20844     2 VKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCRFNCHKRCASKVPRDC 55
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
243-295 1.41e-15

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 71.15  E-value: 1.41e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVD 295
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVCPVP 53
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
413-603 1.55e-15

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: 76.91  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGKDevYAVKVLKKDVILQdddvdctMTEKRILALAR-KHPYLTQLYCCfQTKDRLFfVMEYVNG 491
Cdd:cd14068     1 LLGDGGFGSVYRAVYRGED--VAVKIFNKHTSFR-------LLRQELVVLSHlHHPSLVALLAA-GTAPRML-VMELAPK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 G--DLMFQiQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL-----DAEGHCKLADFGMCKEGILNGVTT 564
Cdd:cd14068    70 GslDALLQ-QDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKT 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958782016 565 TtfCGTPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAG 603
Cdd:cd14068   149 S--EGTPGFRAPEVARgNVIYNQQADVYSFGLLLYDILTC 186
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
405-619 1.61e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and 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. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 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: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 78.51  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 405 LDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdcTMTEKRILALARKHP-----YLTQLYCCFQTK 479
Cdd:cd14226    12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELMNKHDtenkyYIVRLKRHFMFR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYV--NGGDLM-------FQIQRSRKFdeprsrfyAAEVTSALMFLHQH--GVIYRDLKLDNILLdaeghC-- 546
Cdd:cd14226    88 NHLCLVFELLsyNLYDLLrntnfrgVSLNLTRKF--------AQQLCTALLFLSTPelSIIHCDLKPENILL-----Cnp 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 547 -----KLADFGmckegilngvtTTTFCGTP--DYI------APEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNED 613
Cdd:cd14226   155 krsaiKIIDFG-----------SSCQLGQRiyQYIqsrfyrSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEV 223

                  ....*.
gi 1958782016 614 DLFESI 619
Cdd:cd14226   224 DQMNKI 229
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
410-600 1.78e-15

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: 77.24  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELK----GKDEVYAVKVLKKDVILQDDDVDctmTEKRILAlARKHPYLTQLY-CCFQTKDRLF- 483
Cdd:cd05081     8 YISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRDFQ---REIQILK-ALHSDFIVKYRgVSYGPGRRSLr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMFQIQRSRKFDEPRSRF-YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGV 562
Cdd:cd05081    84 LVMEYLPSGCLRDFLQRHRARLDASRLLlYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAK--LLPLD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 563 TTTTFCGTPD-----YIAPEILQELEYGPSVDWWALGVLMYEM 600
Cdd:cd05081   162 KDYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYEL 204
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
169-223 1.81e-15

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 70.80  E-value: 1.81e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 169 GHKFMATYLRQPTYCSHCRDFIWGVIGkQGYQCQVCTCVVHKRCHELIITKCAGL 223
Cdd:cd20803     1 GHSFRKKTFHKPTYCHHCTDLLWGLLN-QGYQCEVCNFVSHERCLKTVVTPCSSI 54
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
243-292 1.83e-15

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 70.57  E-value: 1.83e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958782016  243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
169-222 3.12e-15

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 70.09  E-value: 3.12e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 169 GHKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20832     1 GHQFVLQHYYQVTFCNHCSGLLWG-IGYQGYQCSDCEFNIHKQCIEVIEESCPG 53
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
408-613 3.68e-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: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELK-GKD-EVYAVKVLKKDVilqDDDVDCTMTEKRILALAR--KHPYLTQLY-CCFQTKDR- 481
Cdd:cd07842     2 YEIEGCIGRGTYGRVYKAKRKnGKDgKEYAIKKFKGDK---EQYTGISQSACREIALLRelKHENVVSLVeVFLEHADKs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGgDLmFQI---QRSRKfdepRSRFYAAEVTSAL-------MFLHQHGVIYRDLKLDNILLDAEGHC----K 547
Cdd:cd07842    79 VYLLFDYAEH-DL-WQIikfHRQAK----RVSIPPSMVKSLLwqilngiHYLHSNWVLHRDLKPANILVMGEGPErgvvK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 548 LADFGM---CKEGI-----LNGVTTTTFcgtpdYIAPEILqeL---EYGPSVDWWALGVLMYEMMAGQPPFEADNED 613
Cdd:cd07842   153 IGDLGLarlFNAPLkpladLDPVVVTIW-----YRAPELL--LgarHYTKAIDIWAIGCIFAELLTLEPIFKGREAK 222
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
406-670 3.83e-15

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: 76.31  E-value: 3.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDD-----DVDCTMTekrilalARKHPYLTQLY-CCFQTK 479
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQkrllmDLDISMR-------SVDCPYTVTFYgALFREG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DrLFFVMEYVNGG-DLMFQ--IQRSRKFDEPRSRFYAAEVTSALMFLH-QHGVIYRDLKLDNILLDAEGHCKLADFGMCK 555
Cdd:cd06617    74 D-VWICMEVMDTSlDKFYKkvYDKGLTIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGISG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgILNGVTTTTFCGTPDYIAPE-ILQELE---YGPSVDWWALGVLMYEMMAGQPPFeaDNEDDLFESI---LHDD--VLY 626
Cdd:cd06617   153 Y-LVDSVAKTIDAGCKPYMAPErINPELNqkgYDVKSDVWSLGITMIELATGRFPY--DSWKTPFQQLkqvVEEPspQLP 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 627 PVWLSKEAVSILKAFMTKNPHKRlgcvaaQNGEDaIKQHPFFKE 670
Cdd:cd06617   230 AEKFSPEFQDFVNKCLKKNYKER------PNYPE-LLQHPFFEL 266
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
414-614 4.14e-15

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: 75.99  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKgKDEVYAVKVLKKDVIlQDDDVDCTmTEKRILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14664     1 IGRGGAGTVYKGVMP-NGTLVAVKRLKGEGT-QGGDHGFQ-AEIQTLGMIR-HRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMfQIQRSR-----KFDEPRSRFYAAEVTSALMFLHQH---GVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVTT- 564
Cdd:cd14664    77 LG-ELLHSRpesqpPLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAK--LMDDKDSh 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 565 --TTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14664   154 vmSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDD 205
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
168-222 6.45e-15

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; 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. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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. 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. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 69.22  E-value: 6.45e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 168 NGHKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20794     1 NGHLFQAKRFNRRAVCAYCSDRIWG-LGRQGYKCINCKLLVHKKCHKLVKVACGQ 54
pknD PRK13184
serine/threonine-protein kinase PknD;
408-607 6.75e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 78.66  E-value: 6.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAElkgkDEVYAVKV-LKKdviLQDDDVDCTMTEKRILALAR-----KHPYLTQLYCCFQTKDR 481
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAY----DPVCSRRVaLKK---IREDLSENPLLKKRFLREAKiaadlIHPGIVPVYSICSDGDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAaEVTSALMFL-------------HQHGVIYRDLKLDNILLDAEGHCKL 548
Cdd:PRK13184   77 VYYTMPYIEGYTLK-SLLKSVWQKESLSKELA-EKTSVGAFLsifhkicatieyvHSKGVLHRDLKPDNILLGLFGEVVI 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 549 ADFGMCK----------------EGILNGVTTT--TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:PRK13184  155 LDWGAAIfkkleeedlldidvdeRNICYSSMTIpgKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
408-556 7.12e-15

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 75.19  E-value: 7.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDV---ILQDddvdctmtEKRILALARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSkhpQLEY--------EAKVYKLLQGGPGIPRLYWFGQEGDYNVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVnGGDL--MFQiQRSRKFDeprsrfyaaeVTSALM----------FLHQHGVIYRDLKLDNILLDAEGHCK---LA 549
Cdd:cd14016    74 VMDLL-GPSLedLFN-KCGRKFS----------LKTVLMladqmisrleYLHSKGYIHRDIKPENFLMGLGKNSNkvyLI 141

                  ....*..
gi 1958782016 550 DFGMCKE 556
Cdd:cd14016   142 DFGLAKK 148
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
408-614 8.37e-15

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK 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: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 75.95  E-value: 8.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDV----ILQdddvdctmTEKRILA-LARKHP---YLTQLYCCFQTK 479
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPsyarQGQ--------IEVSILSrLSQENAdefNFVRAYECFQHK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGdlMFQIQRSRKFDE---PRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC----KLADFG 552
Cdd:cd14211    73 NHTCLVFEMLEQN--LYDFLKQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQpyrvKVIDFG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 553 mcKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14211   151 --SASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYD 210
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
414-683 9.72e-15

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: 74.78  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDevYAVKVLKKDVILQDddvdctmTEKRILALAR-KHPYLTQLY--CCFQTKDRLffVMEYVN 490
Cdd:cd14058     1 VGRGSFGVVCKARWRNQI--VAVKIIESESEKKA-------FEVEVRQLSRvDHPNIIKLYgaCSNQKPVCL--VMEYAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLmfqiQRSRKFDEPRSRFYAAEVTS-------ALMFLHQ---HGVIYRDLKLDNILLDAEGH-CKLADFGMCKEgIL 559
Cdd:cd14058    70 GGSL----YNVLHGKEPKPIYTAAHAMSwalqcakGVAYLHSmkpKALIHRDLKPPNLLLTNGGTvLKICDFGTACD-IS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTfcGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLFESILHDDVLYPvwLSKEAVSIL 638
Cdd:cd14058   145 THMTNNK--GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFdHIGGPAFRIMWAVHNGERPP--LIKNCPKPI 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 639 KAFMT----KNPHKRlgcvaaqngedaikqhPFFKEIDWVLLEQKKIKP 683
Cdd:cd14058   221 ESLMTrcwsKDPEKR----------------PSMKEIVKIMSHLMQFFP 253
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
414-607 1.03e-14

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: 74.69  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVY---AVKVLKKDVILQDddvdctmtEKRILALAR-----KHPYLTQLYCCFQTkDRLFFV 485
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSGKEvevAVKTLKQEHEKAG--------KKEFLREASvmaqlDHPCIVRLIGVCKG-EPLMLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE-GILNGVTT 564
Cdd:cd05060    74 MELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRAlGAGSDYYR 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 565 TTFCGT-P-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05060   154 ATTAGRwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
412-617 1.06e-14

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: 75.77  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDE-------VYAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05099    18 KPLGEGCFGQVVRAEAYGIDKsrpdqtvTVAVKMLKDNA--TDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPLYV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMfQIQRSRK-------FDEPRSR----------FYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCK 547
Cdd:cd05099    96 IVEYAAKGNLR-EFLRARRppgpdytFDITKVPeeqlsfkdlvSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMK 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 548 LADFGMCKeGI--LNGVTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFE 617
Cdd:cd05099   175 IADFGLAR-GVhdIDYYKKTSNGRLPvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFK 247
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
411-615 1.07e-14

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 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: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 75.27  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLK---KDVILQdddvdctmtEKRILALARKHPYLTQLYCCFQTKD--RLFFV 485
Cdd:cd14132    23 IRKIGRGKYSEVFEGINIGNNEKVVIKVLKpvkKKKIKR---------EIKILQNLRGGPNIVKLLDVVKDPQskTPSLI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDL--MFQiqrsrKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH-CKLADFGMCkEGILNGV 562
Cdd:cd14132    94 FEYVNNTDFktLYP-----TLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA-EFYHPGQ 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 563 TTTTFCGTPDYIAPEILQEL-EYGPSVDWWALGVLMYEMMAGQPPFEA--DNEDDL 615
Cdd:cd14132   168 EYNVRVASRYYKGPELLVDYqYYDYSLDMWSLGCMLASMIFRKEPFFHghDNYDQL 223
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
408-602 1.28e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.07  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDddvdcTMTEKRIlalarKHPyltqlyCCFQTKDRLFF--- 484
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGTTLIE-----AMLLQNV-----NHP------SVIRMKDTLVSgai 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 ---VMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIlNG 561
Cdd:PHA03209  132 tcmVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPV-VA 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA 602
Cdd:PHA03209  211 PAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
477-668 1.33e-14

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 73.93  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 477 QTKDRLFFVMEYvngGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 556
Cdd:cd14023    57 DTKAYVFFEKDF---GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 GILNGV--TTTTFCGTPDYIAPEILQEL-EY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSK 632
Cdd:cd14023   134 HIMKGEddALSDKHGCPAYVSPEILNTTgTYsGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSP 213
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958782016 633 EAVSILKAFMTKNPHKRLGCvaaqngeDAIKQHPFF 668
Cdd:cd14023   214 KARCLIRSLLRREPSERLTA-------PEILLHPWF 242
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
391-656 1.39e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 77.86  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  391 ENGEVRqgqakrlgLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALarKHPYLT 470
Cdd:PTZ00266     6 DDGESR--------LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMREL--KHKNIV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  471 QLYCCFQTK--DRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTS----ALMFLHQ-------HGVIYRDLKLDN 537
Cdd:PTZ00266    76 RYIDRFLNKanQKLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRqllhALAYCHNlkdgpngERVLHRDLKPQN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016  538 ILLD----------AEGH-------CKLADFGMCKE-GILNGVTTTTfcGTPDYIAPEIL--QELEYGPSVDWWALGVLM 597
Cdd:PTZ00266   156 IFLStgirhigkitAQANnlngrpiAKIGDFGLSKNiGIESMAHSCV--GTPYYWSPELLlhETKSYDDKSDMWALGCII 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782016  598 YEMMAGQPPF-EADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKR---LGCVAAQ 656
Cdd:PTZ00266   234 YELCSGKTPFhKANNFSQLISELKRGPDLPIKGKSKELNILIKNLLNLSAKERpsaLQCLGYQ 296
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
414-656 1.48e-14

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: 74.23  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVM--LAELKGKDEVYAVKVLKKDvilqDDDV---DCTMTEKRILALArKHPYLTQLYCCFQTKDrLFFVMEY 488
Cdd:cd05116     3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNE----ANDPalkDELLREANVMQQL-DNPYIVRMIGICEAES-WMLVMEM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK-----EGILNGVT 563
Cdd:cd05116    77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKalradENYYKAQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 564 TTTFcgtP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVL-YPVWLSKEAVSILKA 640
Cdd:cd05116   157 HGKW---PvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKGERMeCPAGCPPEMYDLMKL 233
                         250
                  ....*....|....*.
gi 1958782016 641 FMTKNPHKRLGCVAAQ 656
Cdd:cd05116   234 CWTYDVDERPGFAAVE 249
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
412-613 1.60e-14

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: 74.33  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKV---MLAELKGKDEVYAVKVLKKDVilQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd05033    10 KVIGGGEFGEVcsgSLKLPGKKEIDVAIKTLKSGY--SDKQRLDFLTEASIMG-QFDHPNVIRLEGVVTKSRPVMIVTEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDL-MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE-GILNGVTTTT 566
Cdd:cd05033    87 MENGSLdKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRlEDSEATYTTK 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 567 FCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF-EADNED 613
Cdd:cd05033   167 GGKIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYwDMSNQD 216
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
418-668 1.70e-14

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: 74.67  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 418 SFGKVMLAELKGKDEVYAVKVLKKDVIlqdddvdcTMTEKRilalarkHPY-LTQLYCCFQTKDRLFFVME--------- 487
Cdd:cd14011    28 VFEKKQLEEYSKRDREQILELLKRGVK--------QLTRLR-------HPRiLTVQHPLEESRESLAFATEpvfaslanv 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 ---YVNGGDLMFQIQRSRKFDEPRSR-FYaaEVTSALMFLHQH-GVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd14011    93 lgeRDNMPSPPPELQDYKLYDVEIKYgLL--QISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCG-----------TPDYIAPEILQELEYGPSVDWWALGVLMYEMM-AGQPPFEADNEDDLFESIL--HDDVLYPV 628
Cdd:cd14011   171 QFPYFREydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKKNSnqLRQLSLSL 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 629 WLS--KEAVSILKAFMTKNPHKRLgcvaaqNGEDAIKqHPFF 668
Cdd:cd14011   251 LEKvpEELRDHVKTLLNVTPEVRP------DAEQLSK-IPFF 285
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
406-617 1.82e-14

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: 75.05  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDE-------VYAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQT 478
Cdd:cd05101    24 DKLTLGKPLGEGCFGQVVMAEAVGIDKdkpkeavTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 KDRLFFVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALM-----------------FLHQHGVIYRDLKLDNILLD 541
Cdd:cd05101   102 DGPLYVIVEYASKGNLR-EYLRARRPPGMEYSYDINRVPEEQMtfkdlvsctyqlargmeYLASQKCIHRDLAARNVLVT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 542 AEGHCKLADFGMCKEgiLNGV---TTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLF 616
Cdd:cd05101   181 ENNVMKIADFGLARD--INNIdyyKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELF 258

                  .
gi 1958782016 617 E 617
Cdd:cd05101   259 K 259
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
414-609 1.83e-14

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: 73.81  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDDDVDCTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd05084     4 IGRGNFGEVFSGRLRADNTPVAVKSCRET--LPPDLKAKFLQEARILK-QYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRsrkfDEPRSRF-----YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGiLNGVTTTT-- 566
Cdd:cd05084    81 FLTFLRT----EGPRLKVkelirMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREE-EDGVYAATgg 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 567 FCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEA 609
Cdd:cd05084   156 MKQIPvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYAN 200
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
414-612 1.93e-14

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: 74.71  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAvkvLKKdvILQDDDVD----CTMTEKRILALArKHPYLTQLYCCFQTKDR-------- 481
Cdd:cd07865    20 IGQGTFGEVFKARHRKTGQIVA---LKK--VLMENEKEgfpiTALREIKILQLL-KHENVVNLIEICRTKATpynrykgs 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGgDLM-FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC------ 554
Cdd:cd07865    94 IYLVFEFCEH-DLAgLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLArafsla 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 555 KEGILNGVTTTTFcgTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE 612
Cdd:cd07865   173 KNSQPNRYTNRVV--TLWYRPPELlLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTE 229
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
243-284 2.28e-14

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 67.78  E-value: 2.28e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRC 284
Cdd:cd20832     2 HQFVLQHYYQVTFCNHCSGLLWGIGYQGYQCSDCEFNIHKQC 43
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
414-552 2.33e-14

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: 70.55  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKkdvILQDDDVDCTMTEKRILALARKH-PYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGD---DVNNEEGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLmFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG 552
Cdd:cd13968    78 TL-IAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
403-605 2.40e-14

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: 74.38  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 403 LGLDEFNFIKVLGKGSFGKVMLAELKGKDE------VYAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLY-CC 475
Cdd:cd05053     9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLDNkpnevvTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIGKHKNIINLLgAC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 476 FQtKDRLFFVMEYVNGGDLMFQIQRSR------KFDEPRSRF----------YAAEVTSALMFLHQHGVIYRDLKLDNIL 539
Cdd:cd05053    87 TQ-DGPLYVVVEYASKGNLREFLRARRppgeeaSPDDPRVPEeqltqkdlvsFAYQVARGMEYLASKKCIHRDLAARNVL 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 540 LDAEGHCKLADFGMCKE-GILNGVTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMM--AGQP 605
Cdd:cd05053   166 VTEDNVMKIADFGLARDiHHIDYYRKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtlGGSP 235
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
482-617 2.43e-14

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: 74.99  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVnGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EGIL 559
Cdd:cd07880    95 FYLVMPFM-GTDLG-KLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARqtDSEM 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 560 NGVTTTTFcgtpdYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEA-DNEDDLFE 617
Cdd:cd07880   173 TGYVVTRW-----YRAPEvILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGhDHLDQLME 227
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
406-614 2.50e-14

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. 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 HIPK2 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: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 75.13  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKD-VILQDDDVDCTMTEKRILALARKHPYLtQLYCCFQTKDRLFF 484
Cdd:cd14227    15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHpSYARQGQIEVSILARLSTESADDYNFV-RAYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGdlMFQIQRSRKFDEPRSRF---YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGH----CKLADFGMCKEg 557
Cdd:cd14227    94 VFEMLEQN--LYDFLKQNKFSPLPLKYirpILQQVATALMKLKSLGLIHADLKPENIMLVDPSRqpyrVKVIDFGSASH- 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 558 iLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14227   171 -VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYD 226
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
468-613 2.59e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 75.42  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 468 YLTQLYCCFQTKDRLFFVMeyvnggdlMFQIQRSrkfdeprsrfyaaeVTSALMFLHQHGVIYRDLKLDNILLDAEGHCK 547
Cdd:PHA03212  165 YKTDLYCYLAAKRNIAICD--------ILAIERS--------------VLRAIQYLHENRIIHRDIKAENIFINHPGDVC 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 548 LADFGM-CKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPP-FEADNED 613
Cdd:PHA03212  223 LGDFGAaCFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSlFEKDGLD 290
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
407-608 3.22e-14

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: 73.60  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMlaelKG---------KDEVyAVKVLKKDVILQDDDVdcTMTEKRILAlARKHPYLTQLYCCFQ 477
Cdd:cd05057     8 ELEKGKVLGSGAFGTVY----KGvwipegekvKIPV-AIKVLREETGPKANEE--ILDEAYVMA-SVDHPHLVRLLGICL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 478 TKdRLFFVMEYVNGGDLMFQIQRSRkfDEPRSRF---YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC 554
Cdd:cd05057    80 SS-QVQLITQLMPLGCLLDYVRNHR--DNIGSQLllnWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 555 KegILNG---VTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFE 608
Cdd:cd05057   157 K--LLDVdekEYHAEGGKVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYE 213
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
513-658 3.29e-14

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: 73.46  E-value: 3.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 513 AAEVTSALMFLHQHGVIYRDLKLDNIL---LDAEGHC--KLADFGMCKEGILNGVTTTTfcGTPDYIAPEILQELEYGPS 587
Cdd:cd14067   120 AYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHIniKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPRIVYDEK 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 588 VDWWALGVLMYEMMAGQPPFEADNEDDLFESIlhDDVLYPVWLSKEAVSI--LKAFMTK----NPHKR---LGCVAAQNG 658
Cdd:cd14067   198 VDMFSYGMVLYELLSGQRPSLGHHQLQIAKKL--SKGIRPVLGQPEEVQFfrLQALMMEcwdtKPEKRplaCSVVEQMKD 275
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
242-292 3.43e-14

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410358  Cd Length: 52  Bit Score: 67.36  E-value: 3.43e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20808     1 KHNFQETTYFKPTFCDHCTGLLWGLIKQGYKCKDCGINCHKHCKDLVVVEC 51
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
170-220 4.26e-14

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 66.77  E-value: 4.26e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGLF-KQGLKCSDCGLVCHKKCLDKAPSPC 50
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
412-611 5.26e-14

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: 73.66  E-value: 5.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVYAVKVLKkDVILQDDDVDCTMTEKRILALARkHPYLTQLYCCFQTKDR-----LFFVM 486
Cdd:cd07859     6 EVIGKGSYGVVCSAIDTHTGEKVAIKKIN-DVFEHVSDATRILREIKLLRLLR-HPDIVEIKHIMLPPSRrefkdIYVVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVnGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTT-- 564
Cdd:cd07859    84 ELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAif 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 565 -TTFCGTPDYIAPEILQEL--EYGPSVDWWALGVLMYEMMAGQPPFEADN 611
Cdd:cd07859   163 wTDYVATRWYRAPELCGSFfsKYTPAIDIWSIGCIFAEVLTGKPLFPGKN 212
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
414-649 5.39e-14

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, 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. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin 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: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 72.30  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDdvdctMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQ-----AAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAE---GHCKLADFGMCKEgILNGVTTTTFCGT 570
Cdd:cd14115    76 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHRHVHHLLGN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 571 PDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYP----VWLSKEAVSILKAFMTKNP 646
Cdd:cd14115   155 PEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPdeyfGDVSQAARDFINVILQEDP 234

                  ...
gi 1958782016 647 HKR 649
Cdd:cd14115   235 RRR 237
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
412-621 5.48e-14

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: 72.75  E-value: 5.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVyAVKVLKKDVIlqddDVDCTMTEKRILAlARKHPYLTQLYCCFqTKDRLFFVMEYVNG 491
Cdd:cd05073    17 KKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM----SVEAFLAEANVMK-TLQHDKLVKLHAVV-TKEPIYIITEFMAK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 492 GDLM--FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCG 569
Cdd:cd05073    90 GSLLdfLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAK 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 570 TP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILH 621
Cdd:cd05073   170 FPiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALER 223
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
407-649 5.57e-14

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: 72.77  E-value: 5.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGkdEVyAVKVLKKDVILQDDDVdctmTEKRILALARK--HPYLTQLYCCFQTKDRLFF 484
Cdd:cd14063     1 ELEIKEVIGKGRFGRVHRGRWHG--DV-AIKLLNIDYLNEEQLE----AFKEEVAAYKNtrHDNLVLFMGACMDPPHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQI-QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDaEGHCKLADFGMCK-EGILNGV 562
Cdd:cd14063    74 VTSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGLFSlSGLLQPG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTP----DYIAPEILQ----------ELEYGPSVDWWALGVLMYEMMAGQPPFEADNEddlfESIL------HD 622
Cdd:cd14063   153 RREDTLVIPngwlCYLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPFKEQPA----ESIIwqvgcgKK 228
                         250       260
                  ....*....|....*....|....*..
gi 1958782016 623 DVLYPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd14063   229 QSLSQLDIGREVKDILMQCWAYDPEKR 255
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
412-617 6.70e-14

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: 73.52  E-value: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDE-------VYAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05100    18 KPLGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLKDDA--TDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMfQIQRSRK-------FDE---PRSRFY-------AAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCK 547
Cdd:cd05100    96 LVEYASKGNLR-EYLRARRppgmdysFDTcklPEEQLTfkdlvscAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMK 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 548 LADFGMCKE-GILNGVTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFE 617
Cdd:cd05100   175 IADFGLARDvHNIDYYKKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFK 247
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
412-617 7.53e-14

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: 72.74  E-value: 7.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDE-------VYAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFF 484
Cdd:cd05098    19 KPLGEGCFGQVVLAEAIGLDKdkpnrvtKVAVKMLKSDA--TEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSRkfdePRSRFY--------------------AAEVTSALMFLHQHGVIYRDLKLDNILLDAEG 544
Cdd:cd05098    97 IVEYASKGNLREYLQARR----PPGMEYcynpshnpeeqlsskdlvscAYQVARGMEYLASKKCIHRDLAARNVLVTEDN 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 545 HCKLADFGMCKE-GILNGVTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFE 617
Cdd:cd05098   173 VMKIADFGLARDiHHIDYYKKTTNGRLPvKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFK 248
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
406-649 7.56e-14

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: 72.90  E-value: 7.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKG--KDEV---YAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD 480
Cdd:cd05055    35 NNLSFGKTLGAGAFGKVVEATAYGlsKSDAvmkVAVKMLKPTA--HSSEREALMSELKIMSHLGNHENIVNLLGACTIGG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSR-KFDEPRSRF-YAAEVTSALMFLHQHGVIYRDLKLDNILLdAEGH-CKLADFGMCKEg 557
Cdd:cd05055   113 PILVITEYCCYGDLLNFLRRKReSFLTLEDLLsFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKiVKICDFGLARD- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 558 ILNG----VTTTTFCGTpDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHD--DVLYPVWL 630
Cdd:cd05055   191 IMNDsnyvVKGNARLPV-KWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEgyRMAQPEHA 269
                         250
                  ....*....|....*....
gi 1958782016 631 SKEAVSILKAFMTKNPHKR 649
Cdd:cd05055   270 PAEIYDIMKTCWDADPLKR 288
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
414-672 7.61e-14

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: 72.78  E-value: 7.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKV--MLAELKGKdeVYAVKVLKKDVILQDD-----DVDCTMTekrilalARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd06616    14 IGRGAFGTVnkMLHKPSGT--IMAVKRIRSTVDEKEQkrllmDLDVVMR-------SSDCPYIVKFYGALFREGDCWICM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EyvnggdLM-----------FQIQRSRkFDEPRSRFYAAEVTSALMFL-HQHGVIYRDLKLDNILLDAEGHCKLADFGMC 554
Cdd:cd06616    85 E------LMdisldkfykyvYEVLDSV-IPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KEgILNGVTTTTFCGTPDYIAPEILQELE----YGPSVDWWALGVLMYEMMAGQPPFEADNEddLFES----------IL 620
Cdd:cd06616   158 GQ-LVDSIAKTRDAGCRPYMAPERIDPSAsrdgYDVRSDVWSLGITLYEVATGKFPYPKWNS--VFDQltqvvkgdppIL 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 621 HDDVLYPVwlSKEAVSILKAFMTKNPHKRlgcvaaqNGEDAIKQHPFFKEID 672
Cdd:cd06616   235 SNSEEREF--SPSFVNFVNLCLIKDESKR-------PKYKELLKHPFIKMYE 277
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
465-670 7.61e-14

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: 72.45  E-value: 7.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 465 KHPYLTQLYCCFQT----KDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNI 538
Cdd:cd14031    67 QHPNIVRFYDSWESvlkgKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNI 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 539 LLDA-EGHCKLADFGMCKegILNGVTTTTFCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLF 616
Cdd:cd14031   147 FITGpTGSVKIGDLGLAT--LMRTSFAKSVIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIY 223
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 617 ESILHDdvLYPVWLSK----EAVSILKAFMTKNPHKRLGCVAAQNgedaikqHPFFKE 670
Cdd:cd14031   224 RKVTSG--IKPASFNKvtdpEVKEIIEGCIRQNKSERLSIKDLLN-------HAFFAE 272
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
411-605 7.82e-14

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: 72.38  E-value: 7.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKG--KDEVY---AVKvlkkdvILQDDDvdcTMTEKR-ILALAR-----KHPYLTQLYCCFQTK 479
Cdd:cd05032    11 IRELGQGSFGMVYEGLAKGvvKGEPEtrvAIK------TVNENA---SMRERIeFLNEASvmkefNCHHVVRLLGVVSTG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQIqRSRKFDE---------PRSRFY--AAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKL 548
Cdd:cd05032    82 QPTLVVMELMAKGDLKSYL-RSRRPEAennpglgppTLQKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 549 ADFGMCKE------------GILngvttttfcgtP-DYIAPEILQELEYGPSVDWWALGVLMYEM--MAGQP 605
Cdd:cd05032   161 GDFGMTRDiyetdyyrkggkGLL-----------PvRWMAPESLKDGVFTTKSDVWSFGVVLWEMatLAEQP 221
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
243-293 9.90e-14

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410360  Cd Length: 52  Bit Score: 65.74  E-value: 9.90e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVaPNCG 293
Cdd:cd20810     3 HSFELTTFKEPTTCSVCKKLLKGLFFQGYKCSVCGAAVHKECIAKV-KRCG 52
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
170-220 1.01e-13

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 65.95  E-value: 1.01e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016  170 HKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWG-SFKQGLRCSECKVKCHKKCADKVPKAC 50
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
410-608 1.10e-13

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: 71.97  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELK----GKDEVYAVKVLKKDVILQDDDVDctmTEKRILALARKHPYLTQLYCCFQTKDR-LFF 484
Cdd:cd14205     8 FLQQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQHSTEEHLRDFE---REIEILKSLQHDNIVKYKGVCYSAGRRnLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVT 563
Cdd:cd14205    85 IMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTK--VLPQDK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 564 TTTFCGTPD-----YIAPEILQELEYGPSVDWWALGVLMYEMM-----AGQPPFE 608
Cdd:cd14205   163 EYYKVKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELFtyiekSKSPPAE 217
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
410-605 1.14e-13

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: 71.94  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 410 FIKVLGKGSFGKVMLAELKG--KDEVYAVKVLKKDVILQDDdvdCTMTEKRILALARKHPYLTQ-LYCCFQTKDRLFfVM 486
Cdd:cd05087     1 YLKEIGHGWFGKVFLGEVNSglSSTQVVVKELKASASVQDQ---MQFLEEAQPYRALQHTNLLQcLAQCAEVTPYLL-VM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKFD----EPRS-RFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM--CKEGIL 559
Cdd:cd05087    77 EFCPLGDLKGYLRSCRAAEsmapDPLTlQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLshCKYKED 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 560 NGVTTTTFCGTPDYIAPEILQEL-------EYGPSVDWWALGVLMYEM--MAGQP 605
Cdd:cd05087   157 YFVTADQLWVPLRWIAPELVDEVhgnllvvDQTKQSNVWSLGVTIWELfeLGNQP 211
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
412-621 1.16e-13

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: 71.80  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVY---AVKVLKKDVILQDDdVDCTMTEkrilALARK---HPYLTQLY-CCFQTKDRLFF 484
Cdd:cd05035     5 KILGEGEFGSVMEAQLKQDDGSQlkvAVKTMKVDIHTYSE-IEEFLSE----AACMKdfdHPNVMRLIgVCFTASDLNKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 -----VMEYVNGGDLMFQIQRSRKFDEPRS-------RFyAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG 552
Cdd:cd05035    80 pspmvILPFMKHGDLHSYLLYSRLGGLPEKlplqtllKF-MVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFG 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 553 MCKEgILNG--VTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILH 621
Cdd:cd05035   159 LSRK-IYSGdyYRQGRISKMPvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRN 230
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
8-119 1.27e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 67.09  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016   8 LKIKICEAVSLKPTAWSlrhavgprpqtFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCN--GRKIELAVFH 85
Cdd:cd00030     1 LRVTVIEARNLPAKDLN-----------GKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDpeSDTLTVEVWD 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958782016  86 DAPIGYDDFVANCTIQFEELLQNGSRHfEDWIDL 119
Cdd:cd00030    70 KDRFSKDDFLGEVEIPLSELLDSGKEG-ELWLPL 102
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
412-619 1.45e-13

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: 71.10  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVyAVKVLKKDvilqdddvdcTMTEKRILALAR-----KHPYLTQLYCCFqTKDRLFFVM 486
Cdd:cd14203     1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKPG----------TMSPEAFLEEAQimkklRHDKLVQLYAVV-SEEPIYIVT 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLM--FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTT 564
Cdd:cd14203    69 EFMSKGSLLdfLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTA 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 565 TTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd14203   149 RQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 205
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
412-619 1.58e-13

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: 71.22  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELK---GKDEVYAVKVLKKDVILQDDDVDCTMTEKRILaLARKHPYLTQLYCCFQTKdRLFFVMEY 488
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTtpsGKVIQVAVKCLKSDVLSQPNAMDDFLKEVNAM-HSLDHPNLIRLYGVVLSS-PLMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLmfqIQRSRKfdePRSRF-------YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE-GILN 560
Cdd:cd05040    79 APLGSL---LDRLRK---DQGHFlistlcdYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRAlPQNE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 561 GVTTTTF--------CgtpdyiAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05040   153 DHYVMQEhrkvpfawC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKI 214
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
414-610 1.67e-13

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: 71.78  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKgkDEVYAVKVLKKDVILQDDDVDCT-MTEKRILALARkHPYLTQL--YCCfqtkDRLFFVMEYV- 489
Cdd:cd14159     1 IGEGGFGCVYQAVMR--NTEYAVKRLKEDSELDWSVVKNSfLTEVEKLSRFR-HPNIVDLagYSA----QQGNYCLIYVy 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 --NGG--DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQH--GVIYRDLKLDNILLDAEGHCKLADFGM---CKEGILN 560
Cdd:cd14159    74 lpNGSleDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGLarfSRRPKQP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 561 GVT-----TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEAD 610
Cdd:cd14159   154 GMSstlarTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVD 208
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
406-693 1.71e-13

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 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: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 72.01  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDC----TMTEKRILAlARKHPYLTQLYCCFQ-TKD 480
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhkhACREYRIHK-ELDHPRIVKLYDYFSlDTD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQ--HGVIYRDLKLDNILL---DAEGHCKLADFGMCK 555
Cdd:cd14041    85 SFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIKITDFGLSK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 ------EGILNGVT-TTTFCGTPDYIAPEILQELEYGP----SVDWWALGVLMYEMMAGQPPFEADNEDdlfESILHDDv 624
Cdd:cd14041   165 imdddsYNSVDGMElTSQGAGTYWYLPPECFVVGKEPPkisnKVDVWSVGVIFYQCLYGRKPFGHNQSQ---QDILQEN- 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 625 lypvwlskeavSILKAFMTKNPHKRlgcVAAQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIFASV 693
Cdd:cd14041   241 -----------TILKATEVQFPPKP---VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSV 295
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
407-654 2.33e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 70.82  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDcTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd14138     6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQN-ALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQI----QRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL---------------DAEGHCK 547
Cdd:cd14138    85 EYCNGGSLADAIsenyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegdeDEWASNK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 548 LadfgMCKEGILNGVTTTTFC----GTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQP-PFEADNEDDLFESILH 621
Cdd:cd14138   165 V----IFKIGDLGHVTRVSSPqveeGDSRFLANEVLQEnYTHLPKADIFALALTVVCAAGAEPlPTNGDQWHEIRQGKLP 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958782016 622 DdvlYPVWLSKEAVSILKAFMTKNPHKRLGCVA 654
Cdd:cd14138   241 R---IPQVLSQEFLDLLKVMIHPDPERRPSAVA 270
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
165-221 2.62e-13

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 64.67  E-value: 2.62e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 165 HQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCA 221
Cdd:cd20831     1 HIYNDHTFVATHFKGGPSCAVCNKLIPGRFGKQGYQCRDCGLICHKRCHVKVETHCP 57
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
413-617 2.66e-13

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: 70.94  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKV---MLAELKGKDEVYAVKVLKKDV-ILQdddVDCTMTEKRILALArKHPYLTQLYC-CFQTKDRLFFVME 487
Cdd:cd05043    13 LLQEGTFGRIfhgILRDEKGKEEEVLVKTVKDHAsEIQ---VTMLLQESSLLYGL-SHQNLLPILHvCIEDGEKPMVLYP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSR--------FYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADfgmckegil 559
Cdd:cd05043    89 YMNWGNLKLFLQQCRLSEANNPQalstqqlvHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITD--------- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 560 NGVTTTTFCGtpDY-------------IAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEadnEDDLFE 617
Cdd:cd05043   160 NALSRDLFPM--DYhclgdnenrpikwMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYV---EIDPFE 226
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
414-602 2.99e-13

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: 70.21  E-value: 2.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDvilqddDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRF------DEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSrkfDEP---RSRFY-AAEVTSALMFLHQHGVIYRDLKLDNILL---DAEGHCKLADFGMCKE-GILNGV--- 562
Cdd:cd14065    75 LEELLKSM---DEQlpwSQRVSlAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREmPDEKTKkpd 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 563 --TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA 602
Cdd:cd14065   152 rkKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIG 193
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
414-607 3.89e-13

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 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: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 70.98  E-value: 3.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVdctmtEKRILALARK--HPYLTQLYCC---FQTKDRLFfVMEY 488
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDV-----QMREFEVLKKlnHKNIVKLFAIeeeLTTRHKVL-VMEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQR-SRKFDEPRSRFYAA--EVTSALMFLHQHGVIYRDLKLDNIL--LDAEGHC--KLADFGMCKEgILNG 561
Cdd:cd13988    75 CPCGSLYTVLEEpSNAYGLPESEFLIVlrDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGAARE-LEDD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 562 VTTTTFCGTPDYIAPEILQ--------ELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd13988   154 EQFVSLYGTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
411-601 4.38e-13

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: 70.31  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELK----GKDEVYAVKVLKKDVILQDDDvdCTMTEKRILALARKHPYLTQLYCCFQTKDR-LFFV 485
Cdd:cd05080     9 IRDLGEGHFGKVSLYCYDptndGTGEMVAVKALKADCGPQHRS--GWKQEIDILKTLYHENIVKYKGCCSEQGGKsLQLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSrKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK---EGILNGV 562
Cdd:cd05080    87 MEYVPLGSLRDYLPKH-SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKavpEGHEYYR 165
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMM 601
Cdd:cd05080   166 VREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELL 204
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
403-607 4.58e-13

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: 69.52  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 403 LGLDEFNFIKVLGKGSFGKVMLAELKGKDevYAVKVLKKDVILQDD-DVDCTMTEKRilalarkHPYLTQLYCCFqTKDR 481
Cdd:cd05083     3 LNLQKLTLGEIIGEGEFGAVLQGEYMGQK--VAVKNIKCDVTAQAFlEETAVMTKLQ-------HKNLVRLLGVI-LHNG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGDLM-FQIQRSRKFDEPRSRF-YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGiL 559
Cdd:cd05083    73 LYIVMELMSKGNLVnFLRSRGRALVPVIQLLqFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVG-S 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782016 560 NGVTTTTFcgTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05083   152 MGVDNSRL--PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
406-614 6.28e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. 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 HIPK1 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: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 70.89  E-value: 6.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKD-VILQDDDVDCTMTEKRILALARKHPYLTQlYCCFQTKDRLFF 484
Cdd:cd14228    15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHpSYARQGQIEVSILSRLSSENADEYNFVRS-YECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 VMEYVNGGdlMFQIQRSRKFDEPRSRFYAA---EVTSALMFLHQHGVIYRDLKLDNILL----DAEGHCKLADFGMCKEg 557
Cdd:cd14228    94 VFEMLEQN--LYDFLKQNKFSPLPLKYIRPilqQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH- 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 558 iLNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14228   171 -VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYD 226
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
414-601 6.84e-13

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: 69.46  E-value: 6.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLkkdvILQDDDVDCT-MTEKRILALArKHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKEL----IRFDEEAQRNfLKEVKVMRSL-DHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQ-RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC------KEGILNGVTTT 565
Cdd:cd14154    76 TLKDVLKdMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveeRLPSGNMSPSE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 566 --------------TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMM 601
Cdd:cd14154   156 tlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
482-619 6.94e-13

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: 70.29  E-value: 6.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVnGGDLmFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegiLNG 561
Cdd:cd07856    85 IYFVTELL-GTDL-HRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR---IQD 159
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 562 VTTTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI 619
Cdd:cd07856   160 PQMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSII 218
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
414-601 8.19e-13

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: 69.21  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVyavkVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEV----MVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMfQIQRSRKFDEPRSR--FYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK---------EGILNGV 562
Cdd:cd14221    77 LR-GIIKSMDSHYPWSQrvSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARlmvdektqpEGLRSLK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 563 TTT-----TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMM 601
Cdd:cd14221   156 KPDrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
412-611 8.40e-13

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: 68.98  E-value: 8.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKV-------MLAELKGKDEVyAVKVLKKDVILQDddvdctmtEKRILALAR-----KHPY-LTQLYCCFQT 478
Cdd:cd05044     1 KFLGSGAFGEVfegtakdILGDGSGETKV-AVKTLRKGATDQE--------KAEFLKEAHlmsnfKHPNiLKLLGVCLDN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 479 kDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAE-------VTSALMFLHQHGVIYRDLKLDNILLDAEGHC----K 547
Cdd:cd05044    72 -DPQYIILELMEGGDLLSYLRAARPTAFTPPLLTLKDllsicvdVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRervvK 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 548 LADFGMCK------------EGILNgvttttfcgtPDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADN 611
Cdd:cd05044   151 IGDFGLARdiykndyyrkegEGLLP----------VRWMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQPYPARN 217
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
480-669 8.57e-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: 70.19  E-value: 8.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGgDLMFQIQRSRkFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC-KLADFGMCK--- 555
Cdd:cd07854    89 NSVYIVQEYMET-DLANVLEQGP-LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARivd 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 -----EGILNGVTTTTFcgtpdYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILH-------- 621
Cdd:cd07854   167 physhKGYLSEGLVTKW-----YRSPRLlLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILEsvpvvree 241
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 622 --DDVL--YPVWLSK------------------EAVSILKAFMTKNPHKRLgcvaaqNGEDAIkQHPFFK 669
Cdd:cd07854   242 drNELLnvIPSFVRNdggeprrplrdllpgvnpEALDFLEQILTFNPMDRL------TAEEAL-MHPYMS 304
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
238-293 8.89e-13

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 63.23  E-value: 8.89e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 238 SVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCG 293
Cdd:cd20828     1 GFTQPHNFEPHSFVTPTNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
414-619 1.13e-12

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the 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. The WNK2-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: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 68.57  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMlaelKGKDEVYAVKVlkkdvilqdddVDCTMTEKRILALARK-------------HPYLTQLYCCFQTKD 480
Cdd:cd14032     9 LGRGSFKTVY----KGLDTETWVEV-----------AWCELQDRKLTKVERQrfkeeaemlkglqHPNIVRFYDFWESCA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 R----LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNILLDA-EGHCKLADFGM 553
Cdd:cd14032    74 KgkrcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 554 CKegILNGVTTTTFCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLFESI 619
Cdd:cd14032   154 AT--LKRASFAKSVIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKV 217
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
408-614 1.13e-12

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: 69.67  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKD-VILQDDDVDCTMTEKRILALARKHPYLtQLYCCFQTKDRLFFVM 486
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHpSYARQGQIEVGILARLSNENADEFNFV-RAYECFQHRNHTCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGdlMFQIQRSRKFDEPRSRFYAA---EVTSALMFLHQHGVIYRDLKLDNILL----DAEGHCKLADFGMCKEgiL 559
Cdd:cd14229    81 EMLEQN--LYDFLKQNKFSPLPLKVIRPilqQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH--V 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 560 NGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14229   157 SKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYD 211
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
407-614 1.34e-12

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: 68.50  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 407 EFNFIKVLGKGSFGKVMLAELKGKdevYAVKVLKkdviLQDDDVDCTMTEKRILALARKHPYLT-QLYCCFQTKDRLFFV 485
Cdd:cd14150     1 EVSMLKRIGTGSFGTVFRGKWHGD---VAVKILK----VTEPTPEQLQAFKNEMQVLRKTRHVNiLLFMGFMTRPNFAII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC--KEGILNGV 562
Cdd:cd14150    74 TQWCEGSSLYRHLHVTEtRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQ 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 563 TTTTFCGTPDYIAPEILQELEYGP---SVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14150   154 QVEQPSGSILWMAPEVIRMQDTNPysfQSDVYAYGVVLYELMSGTLPYSNINNRD 208
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
412-617 1.43e-12

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: 68.50  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELKGKDEVY--AVKVLKKDVilqdddvdCTMTEKRIL---ALARK---HPYLTQLY-CCFQTKDRL 482
Cdd:cd05075     6 KTLGEGEFGSVMEGQLNQDDSVLkvAVKTMKIAI--------CTRSEMEDFlseAVCMKefdHPNVMRLIgVCLQNTESE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FF-----VMEYVNGGDLMFQIQRSRKFDEP---RSRF---YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADF 551
Cdd:cd05075    78 GYpspvvILPFMKHGDLHSFLLYSRLGDCPvylPTQMlvkFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADF 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 552 GMCKEgILNG--VTTTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFE 617
Cdd:cd05075   158 GLSKK-IYNGdyYRQGRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYD 226
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
243-295 1.48e-12

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. 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. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. 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. 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. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410383  Cd Length: 58  Bit Score: 62.81  E-value: 1.48e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC-GVD 295
Cdd:cd20833     3 HKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCSFVVHKRCHEFVTFSCpGAD 56
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
484-620 2.13e-12

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: 68.91  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgilNGVT 563
Cdd:cd07877    98 YLVTHLMGADLN-NIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARH---TDDE 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782016 564 TTTFCGTPDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd07877   174 MTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLIL 231
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
412-613 2.23e-12

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: 67.97  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELK--GKDEVY-AVKVLKKDVI-LQDDDVdctMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVME 487
Cdd:cd05066    10 KVIGAGEFGEVCSGRLKlpGKREIPvAIKTLKAGYTeKQRRDF---LSEASIMG-QFDHPNIIHLEGVVTRSKPVMIVTE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDL-MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK--EGILNGVTT 564
Cdd:cd05066    86 YMENGSLdAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDPEAAYT 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 565 TTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF-EADNED 613
Cdd:cd05066   166 TRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYwEMSNQD 217
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
414-607 2.89e-12

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: 67.79  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVyAVKVLKKDVIlqddDVDCTMTEKRILALARkHPYLTQLYCCFqTKDRLFFVMEYVNGGD 493
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTRV-AIKTLKPGTM----SPEAFLQEAQVMKKLR-HEKLVQLYAVV-SEEPIYIVTEYMSKGS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LM--FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05071    90 LLdfLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFP 169
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958782016 572 -DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPF 607
Cdd:cd05071   170 iKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPY 207
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
519-667 3.94e-12

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: 68.10  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 519 ALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTT---TTFCGTPDYIAPEI-LQELEYGPSVDWWALG 594
Cdd:cd07849   118 GLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTgflTEYVATRWYRAPEImLNSKGYTKAIDIWSVG 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 595 VLMYEMMAGQPPFEAD----------------NEDDL----------------FESILHDDVLYPVWLSKeAVSILKAFM 642
Cdd:cd07849   198 CILAEMLSNRPLFPGKdylhqlnlilgilgtpSQEDLnciislkarnyikslpFKPKVPWNKLFPNADPK-ALDLLDKML 276
                         170       180
                  ....*....|....*....|....*
gi 1958782016 643 TKNPHKRLgcvaaqNGEDAIKqHPF 667
Cdd:cd07849   277 TFNPHKRI------TVEEALA-HPY 294
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
412-649 4.21e-12

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: 67.30  E-value: 4.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLA---ELKGKD--EVYAVKVLKKDVilQDDDVDCTMTEKRILALArKHPYLTQLYCCFQTKDRLFFVM 486
Cdd:cd05045     6 KTLGEGEFGKVVKAtafRLKGRAgyTTVAVKMLKENA--SSSELRDLLSEFNLLKQV-NHPHVIKLYGACSQDGPLLLIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 487 EYVNGGDLMFQIQRSRKF----------------DEPRSR--------FYAAEVTSALMFLHQHGVIYRDLKLDNILLdA 542
Cdd:cd05045    83 EYAKYGSLRSFLRESRKVgpsylgsdgnrnssylDNPDERaltmgdliSFAWQISRGMQYLAEMKLVHRDLAARNVLV-A 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 543 EGH-CKLADFGMCKEGILNGVTTTTFCG-TP-DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFeS 618
Cdd:cd05045   162 EGRkMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLF-N 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958782016 619 ILHDD--VLYPVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd05045   241 LLKTGyrMERPENCSEEMYNLMLTCWKQEPDKR 273
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
406-649 4.28e-12

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: 67.52  E-value: 4.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEV-----YAVKVLKKDVilQDDDVDCTMTEKRILALARKHPYLTQLY-CCFQTK 479
Cdd:cd05054     7 DRLKLGKPLGRGAFGKVIQASAFGIDKSatcrtVAVKMLKEGA--TASEHKALMTELKILIHIGHHLNVVNLLgACTKPG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGGDLMFQIQRSRK----------------------FDEPRSR----FYAAEVTSALMFLHQHGVIYRDL 533
Cdd:cd05054    85 GPLMVIVEFCKFGNLSNYLRSKREefvpyrdkgardveeeedddelYKEPLTLedliCYSFQVARGMEFLASRKCIHRDL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 534 KLDNILLDAEGHCKLADFGMCKEGILNgvttttfcgtPDYI------------APEILQELEYGPSVDWWALGVLMYEMM 601
Cdd:cd05054   165 AARNILLSENNVVKICDFGLARDIYKD----------PDYVrkgdarlplkwmAPESIFDKVYTTQSDVWSFGVLLWEIF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 602 A-GQPPFEADNEDDLFESILHDDVLY--PVWLSKEAVSILKAFMTKNPHKR 649
Cdd:cd05054   235 SlGASPYPGVQMDEEFCRRLKEGTRMraPEYTTPEIYQIMLDCWHGEPKER 285
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
414-604 4.39e-12

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: 66.89  E-value: 4.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVyavkVLKKDVILQDDDVDCT-MTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNGG 492
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTfLTEVKVMR-SLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 493 DLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKE---------------- 556
Cdd:cd14222    76 TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveekkkpppdkpttk 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 557 ----GILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMaGQ 604
Cdd:cd14222   156 krtlRKNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII-GQ 206
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
411-615 4.50e-12

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 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: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 67.66  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLK-KDVILQDddvdcTMTEKRILALARK------HPYLTQLYCCFQTKDRLF 483
Cdd:cd14212     4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKnKPAYFRQ-----AMLEIAILTLLNTkydpedKHHIVRLLDHFMHHGHLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 484 FVMEY--VNggdlMFQIQRSRKFdepRS------RFYAAEVTSALMFLHQHGVIYRDLKLDNILLDA--EGHCKLADFG- 552
Cdd:cd14212    79 IVFELlgVN----LYELLKQNQF---RGlslqliRKFLQQLLDALSVLKDARIIHCDLKPENILLVNldSPEIKLIDFGs 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 553 MCKEGilngVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDL 615
Cdd:cd14212   152 ACFEN----YTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQ 210
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
406-644 4.84e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 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: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 67.39  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 406 DEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDC----TMTEKRILAlARKHPYLTQLYCCFQ-TKD 480
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhACREYRIHK-ELDHPRIVKLYDYFSlDTD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 481 RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQ--HGVIYRDLKLDNILL---DAEGHCKLADFGMCK 555
Cdd:cd14040    85 TFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 ------EGILNGVTTTTFCGTPDYIAPEILQELEYGP----SVDWWALGVLMYEMMAGQPPF--EADNEDDLFESIL--H 621
Cdd:cd14040   165 imdddsYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPkisnKVDVWSVGVIFFQCLYGRKPFghNQSQQDILQENTIlkA 244
                         250       260
                  ....*....|....*....|....*
gi 1958782016 622 DDVLYPV--WLSKEAvsilKAFMTK 644
Cdd:cd14040   245 TEVQFPVkpVVSNEA----KAFIRR 265
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
412-659 4.96e-12

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: 67.40  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 412 KVLGKGSFGKVMLAELK----GKDEVYAVKvlkkdvILQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRL---- 482
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKqnasGQYETVAVK------IFPYEEYASWKNEKDIFTDASlKHENILQFLTAEERGVGLdrqy 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 483 FFVMEYVNGGDLM-FQIQRSRKFDEPRSrfYAAEVTSALMFLH---------QHGVIYRDLKLDNILLDAEGHCKLADFG 552
Cdd:cd14055    75 WLITAYHENGSLQdYLTRHILSWEDLCK--MAGSLARGLAHLHsdrtpcgrpKIPIAHRDLKSSNILVKNDGTCVLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 553 MCKEgILNGVTTTTFC-----GTPDYIAPEI------LQELEYGPSVDWWALGVLMYEMMAG----------QPPF-EAD 610
Cdd:cd14055   153 LALR-LDPSLSVDELAnsgqvGTARYMAPEAlesrvnLEDLESFKQIDVYSMALVLWEMASRceasgevkpyELPFgSKV 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 611 NEDDLFES----ILHDDVLYPV---WLSKEAVSILKAFMTK----NPHKRL--GCVAAQNGE 659
Cdd:cd14055   232 RERPCVESmkdlVLRDRGRPEIpdsWLTHQGMCVLCDTITEcwdhDPEARLtaSCVAERFNE 293
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
241-293 5.69e-12

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 60.86  E-value: 5.69e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 241 MPHKFGIHNYKVPTFCDHCGSLLWGllrQGLQCKVCKMNVHRRCETNVAPNCG 293
Cdd:cd20826     1 KSHSFKEKSFRKPRTCDVCKQIIWN---EGSSCRVCKYACHRKCEPKVTAACS 50
C2 pfam00168
C2 domain;
6-119 6.28e-12

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 62.34  E-value: 6.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016   6 GLLKIKICEAVSLKPtawslrhavgpRPQTFLLDPYIALNVDDS-RIGQTATKQKTNSPAWHDEFVTDV--CNGRKIELA 82
Cdd:pfam00168   1 GRLTVTVIEAKNLPP-----------KDGNGTSDPYVKVYLLDGkQKKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIE 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958782016  83 VFHDAPIGYDDFVANCTIQFEELLQngSRHFEDWIDL 119
Cdd:pfam00168  70 VYDYDRFGRDDFIGEVRIPLSELDS--GEGLDGWYPL 104
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
465-619 7.98e-12

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: 66.18  E-value: 7.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 465 KHPYLTQLYCCFQTKDR----LFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNI 538
Cdd:cd14033    58 QHPNIVRFYDSWKSTVRghkcIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNI 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 539 LLDA-EGHCKLADFGMCKegILNGVTTTTFCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLF 616
Cdd:cd14033   138 FITGpTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEE-KYDEAVDVYAFGMCILEMATSEYPYsECQNAAQIY 214

                  ...
gi 1958782016 617 ESI 619
Cdd:cd14033   215 RKV 217
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
170-212 9.32e-12

first protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410379  Cd Length: 53  Bit Score: 60.44  E-value: 9.32e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGViGKQGYQCQVCTCVVHKRC 212
Cdd:cd20829     1 HRLVDVYFVTPILCRHCKDYIWGK-GKVGVRCEDCHACFHLVC 42
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
242-292 1.15e-11

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410410  Cd Length: 55  Bit Score: 60.33  E-value: 1.15e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20860     2 PHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFEC 52
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
482-620 1.17e-11

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: 66.85  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGgDLmfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGilnG 561
Cdd:cd07879    95 FYLVMPYMQT-DL--QKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHA---D 168
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 562 VTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd07879   169 AEMTGYVVTRWYRAPEvILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQIL 228
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
414-619 1.19e-11

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: 65.85  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKdevYAVKVLKKDVIlQDDDVDCTMTEKRILALARKHPYLtqLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd14151    16 IGSGSFGTVYKGKWHGD---VAVKMLNVTAP-TPQQLQAFKNEVGVLRKTRHVNIL--LFMGYSTKPQLAIVTQWCEGSS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSR-KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMC--KEGILNGVTTTTFCGT 570
Cdd:cd14151    90 LYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 571 PDYIAPEILQELEYGP---SVDWWALGVLMYEMMAGQPPFE-ADNEDDLFESI 619
Cdd:cd14151   170 ILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSnINNRDQIIFMV 222
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
491-620 1.28e-11

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: 66.61  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGilnGVTTTTFCGT 570
Cdd:cd07878   103 GADLN-NIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQA---DDEMTGYVAT 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 571 PDYIAPEI-LQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd07878   179 RWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIM 229
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
414-607 1.53e-11

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of 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. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK 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: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 65.22  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDC-TMTEKRILAL---ARKHPYLTQLyccfqtkdrlffvMEYV 489
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACaGLTSPRVVPLygaVREGPWVNIF-------------MDLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 490 NGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEG-HCKLADFGMCK----EGI-LNGVT 563
Cdd:cd13991    81 EGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAEcldpDGLgKSLFT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958782016 564 TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd13991   161 GDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
243-297 1.59e-11

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410407  Cd Length: 61  Bit Score: 60.05  E-value: 1.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDAR 297
Cdd:cd20857     6 HNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLK 60
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
414-614 1.67e-11

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: 65.11  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGkdeVYAVKVLKKdvilqdddVDCTMTE----KRILALARKHPYLT-QLYCCFQTKDRLFFVMEY 488
Cdd:cd14062     1 IGSGSFGTVYKGRWHG---DVAVKKLNV--------TDPTPSQlqafKNEVAVLRKTRHVNiLLFMGYMTKPQLAIVTQW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDLMFQIQ-RSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMckegilnGVTTTTF 567
Cdd:cd14062    70 CEGSSLYKHLHvLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGL-------ATVKTRW 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 568 CGTPD---------YIAPEILQELE---YGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14062   143 SGSQQfeqptgsilWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
168-220 1.69e-11

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; 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. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 59.61  E-value: 1.69e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 168 NGHKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd21095     1 NGHLFQAKRFNRRAYCGQCSERIWG-LGRQGYKCINCKLLVHKRCHKLVPLTC 52
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
242-292 1.75e-11

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 59.63  E-value: 1.75e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 242 PHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20803     1 GHSFRKKTFHKPTYCHHCTDLLWGLLNQGYQCEVCNFVSHERCLKTVVTPC 51
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
7-111 1.85e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 60.96  E-value: 1.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016    7 LLKIKICEAVSLKPtawslrhavgpRPQTFLLDPYIALNVD--DSRIGQTATKQKTNSPAWHDEFVTDVCN--GRKIELA 82
Cdd:smart00239   1 TLTVKIISARNLPP-----------KDKGGKSDPYVKVSLDgdPKEKKKTKVVKNTLNPVWNETFEFEVPPpeLAELEIE 69
                           90       100
                   ....*....|....*....|....*....
gi 1958782016   83 VFHDAPIGYDDFVANCTIQFEELLQNGSR 111
Cdd:smart00239  70 VYDKDRFGRDDFIGQVTIPLSDLLLGGRH 98
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
414-670 1.97e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 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: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 65.46  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMlaelKGKDEVYAVKVLKKDviLQDDDVDCT----MTEKRILALARKHPYLTQLYCCFQT----KDRLFFV 485
Cdd:cd14030    33 IGRGSFKTVY----KGLDTETTVEVAWCE--LQDRKLSKSerqrFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 MEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG--VIYRDLKLDNILLDA-EGHCKLADFGMCKegILNGV 562
Cdd:cd14030   107 TELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT--LKRAS 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 563 TTTTFCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPF-EADNEDDLFESILHDdvLYPVWLSKEAVSILKAF 641
Cdd:cd14030   185 FAKSVIGTPEFMAPEMYEE-KYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRRVTSG--VKPASFDKVAIPEVKEI 261
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958782016 642 MTknphkrlGCVAAQNGED-AIK---QHPFFKE 670
Cdd:cd14030   262 IE-------GCIRQNKDERyAIKdllNHAFFQE 287
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
414-600 2.02e-11

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: 64.75  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRIlalarKHPYLTQLYCCFQTKDRLFFVMEYVNGGD 493
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEI-----KHPNLVQLLGVCTREPPFYIITEFMPYGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFD-EPRSRFY-AAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGVTTTTFCGTP 571
Cdd:cd05052    89 LLDYLRECNREElNAVVLLYmATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR--LMTGDTYTAHAGAK 166
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958782016 572 ---DYIAPEILQELEYGPSVDWWALGVLMYEM 600
Cdd:cd05052   167 fpiKWTAPESLAYNKFSIKSDVWAFGVLLWEI 198
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
409-607 2.07e-11

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: 65.78  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIKVLGKGSFGKVM--LAELKGKDEVYAVKVLKKDVilqDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKDRLFFV 485
Cdd:cd08216     1 ELLYEIGKCFKGGGVvhLAKHKPTNTLVAVKKINLES---DSKEDLKFLQQEILTSRQlQHPNILPYVTSFVVDNDLYVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 486 ---MEYVNGGDLMfQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGV 562
Cdd:cd08216    78 tplMAYGSCRDLL-KTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGK 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 563 TTTTFCGTPDYI-------APEILQE--LEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd08216   157 RQRVVHDFPKSSeknlpwlSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPF 210
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
482-620 2.21e-11

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: 65.82  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 LFFVMEYVNGGdlMFQIQRsRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNg 561
Cdd:cd07876   101 VYLVMELMDAN--LCQVIH-MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTN- 176
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782016 562 VTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 620
Cdd:cd07876   177 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVI 235
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
414-650 2.43e-11

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: 65.06  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKG----KDEVY-AVKVLKKdvilQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEY 488
Cdd:cd05093    13 LGEGAFGKVFLAECYNlcpeQDKILvAVKTLKD----ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 489 VNGGDL-------------MFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCK 555
Cdd:cd05093    89 MKHGDLnkflrahgpdavlMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 556 EgilngVTTTTFCGTPD-------YIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESILHDDVLY- 626
Cdd:cd05093   169 D-----VYSTDYYRVGGhtmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQr 243
                         250       260
                  ....*....|....*....|....
gi 1958782016 627 PVWLSKEAVSILKAFMTKNPHKRL 650
Cdd:cd05093   244 PRTCPKEVYDLMLGCWQREPHMRL 267
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
170-220 2.62e-11

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 58.86  E-value: 2.62e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIGkQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20806     2 HNFKVHTFKGPHWCDYCGNFMWGLIA-QGVKCEDCGFNAHKQCSKLVPHDC 51
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
170-212 2.66e-11

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; 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. 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 59.21  E-value: 2.66e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRC 212
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLYGLY-KQGLQCKVCKMNVHKRC 44
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
416-607 2.86e-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: 64.26  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 416 KGSFGKVMLAELKGKDEVYAVKVLKKDViLQDDDVDctmtekrILALARkHPYLTQLYCCFQTKDRLFFVMEYVNGGDLM 495
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPVEQ-FKPSDVE-------IQACFR-HENIAELYGALLWEETVHLFMEAGEGGSVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 496 FQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLdAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIA 575
Cdd:cd13995    85 EKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDVYVPKDLRGTEIYMS 163
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958782016 576 PEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:cd13995   164 PEVILCRGHNTKADIYSLGATIIHMQTGSPPW 195
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
413-619 3.04e-11

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: 64.68  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELK--GKDEVYAVKVLKkDVILQDDDVDCTmTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVN 490
Cdd:cd05047     2 VIGEGNFGQVLKARIKkdGLRMDAAIKRMK-EYASKDDHRDFA-GELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 491 GGDLMFQIQRSRKFdEPRSRF-----------------YAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGM 553
Cdd:cd05047    80 HGNLLDFLRKSRVL-ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782016 554 CKeGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05047   159 SR-GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 224
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
414-619 3.11e-11

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: 64.71  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGKDEVyAVKVLKKDVILQDddvdCTMTEKRILALARkHPYLTQLYCCFqTKDRLFFVMEYVNGGD 493
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMMPE----AFLQEAQIMKKLR-HDKLVPLYAVV-SEEPIYIVTEFMGKGS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRS--RKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 571
Cdd:cd05069    93 LLDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFP 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 572 -DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEADNEDDLFESI 619
Cdd:cd05069   173 iKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQV 222
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
413-655 3.18e-11

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: 64.77  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 413 VLGKGSFGKVMLAELKGkdEVYAVKvlkkdvILQDDDVDCTMTEKRILALAR-KHPYLTQLYCCFQTKD----RLFFVME 487
Cdd:cd13998     2 VIGKGRFGEVWKASLKN--EPVAVK------IFSSRDKQSWFREKEIYRTPMlKHENILQFIAADERDTalrtELWLVTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGGDLMFQIQRSRKFDEPRSRFyAAEVTSALMFLHQHGVI---------YRDLKLDNILLDAEGHCKLADFG--MCKE 556
Cdd:cd13998    74 FHPNGSL*DYLSLHTIDWVSLCRL-ALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIADFGlaVRLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 557 GILN--GVTTTTFCGTPDYIAPEILQE------LEYGPSVDWWALGVLMYEMMAG-----------QPPFEAD-NEDDLF 616
Cdd:cd13998   153 PSTGeeDNANNGQVGTKRYMAPEVLEGainlrdFESFKRVDIYAMGLVLWEMASRctdlfgiveeyKPPFYSEvPNHPSF 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 617 ES----ILHDDV---LYPVWLSKEAVSILKAFMTK----NPHKRL--GCVAA 655
Cdd:cd13998   233 EDmqevVVRDKQrpnIPNRWLSHPGLQSLAETIEEcwdhDAEARLtaQCIEE 284
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
401-650 3.29e-11

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: 64.65  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 401 KRLGLDEFNFIKVLGKGSFGKVMLAELKG-----KDEVYAVKVLKkdvilqdDDVDCTMTEK-RILALAR---KHPYLTQ 471
Cdd:cd05091     1 KEINLSAVRFMEELGEDRFGKVYKGHLFGtapgeQTQAVAIKTLK-------DKAEGPLREEfRHEAMLRsrlQHPNIVC 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 472 LYCCFQTKDRLFFVMEYVNGGDLM-FQIQRSRKFD--------------EPRSRFY-AAEVTSALMFLHQHGVIYRDLKL 535
Cdd:cd05091    74 LLGVVTKEQPMSMIFSYCSHGDLHeFLVMRSPHSDvgstdddktvkstlEPADFLHiVTQIAAGMEYLSSHHVVHKDLAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 536 DNILLDAEGHCKLADFGMCKEgiLNGVTTTTFCGTP----DYIAPEILQELEYGPSVDWWALGVLMYEMMA-GQPPFEAD 610
Cdd:cd05091   154 RNVLVFDKLNVKISDLGLFRE--VYAADYYKLMGNSllpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGY 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 611 NEDDLFESILHDDVLY-----PVWLSKEAVSILKAFMTKNP-----HKRL 650
Cdd:cd05091   232 SNQDVIEMIRNRQVLPcpddcPAWVYTLMLECWNEFPSRRPrfkdiHSRL 281
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
170-220 3.29e-11

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410358  Cd Length: 52  Bit Score: 58.89  E-value: 3.29e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20808     2 HNFQETTYFKPTFCDHCTGLLWGLI-KQGYKCKDCGINCHKHCKDLVVVEC 51
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
408-614 3.37e-11

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; 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 DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 65.54  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 408 FNFIKVLGKGSFGKVMLAeLKGKDEVY-AVKVLK--KDVILQDDDvdctmtEKRILALARKHPY-----LTQLYCCFQTK 479
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKA-YDHKTHQHvALKMVRneKRFHRQAAE------EIRILEHLKKQDKdntmnVIHMLESFTFR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 480 DRLFFVMEYVNGgDLMFQIQRSR--KFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC--KLADFGM-C 554
Cdd:cd14224   140 NHICMTFELLSM-NLYELIKKNKfqGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSgiKVIDFGSsC 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KEGilngVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd14224   219 YEH----QRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGD 274
C1_aPKC_iota cd21094
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
168-221 3.68e-11

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota type; 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. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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. Members of this family contain C1 domain found in aPKC isoform iota. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410447  Cd Length: 55  Bit Score: 58.86  E-value: 3.68e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782016 168 NGHKFMATYLRQPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKCA 221
Cdd:cd21094     1 NGHTFQAKRFNRRAHCAICTDRIWG-LGRQGYKCINCKLLVHKKCHKLVTIECG 53
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
340-607 4.14e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 65.25  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 340 EDDRSKSAPTSPCDQELKELENNIRKALSFDNR------GEEHRASSSTDGQLASPGENGEVRQGQAKRLgldEFNFIKV 413
Cdd:PHA03207   23 FSLTGGTDTSDSKDTTGDKFDDCDELGDSDDVThatdydADEESLSPQTDVCQEPCETTSSSDPASVVRM---QYNILSS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELKGkdEVYAVKVLKKDVILQDDdvdcTMTEKRILAlARKHPYLTQLYCCFQTKDRLFFVMEYVNGgD 493
Cdd:PHA03207  100 LTPGSEGEVFVCTKHG--DEQRKKVIVKAVTGGKT----PGREIDILK-TISHRAIINLIHAYRWKSTVCMVMPKYKC-D 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 494 LMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFG-MCKegiLNGVTTTTFC---- 568
Cdd:PHA03207  172 LFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGaACK---LDAHPDTPQCygws 248
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958782016 569 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 607
Cdd:PHA03207  249 GTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
411-612 4.24e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; 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. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. 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. The DYRK4 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: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 65.11  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVL--KKDVILQdddvdcTMTEKRIL-ALARKHPylTQLYCCFQTKDRLFF--- 484
Cdd:cd14225    48 LEVIGKGSFGQVVKALDHKTNEHVAIKIIrnKKRFHHQ------ALVEVKILdALRRKDR--DNSHNVIHMKEYFYFrnh 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 485 ---VMEYVnGGDLMFQIQRS--RKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHC--KLADFGM-CKE 556
Cdd:cd14225   120 lciTFELL-GMNLYELIKKNnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSsiKVIDFGSsCYE 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 557 GilngVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE 612
Cdd:cd14225   199 H----QRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENE 250
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
409-553 4.32e-11

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: 64.28  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 409 NFIKVLGKGSFGKVMLAELKG--------------KDEV--YAVKVLKKDV---ILQDddvdcTMTEKRILAlARKHPYL 469
Cdd:cd05051     8 EFVEKLGEGQFGEVHLCEANGlsdltsddfigndnKDEPvlVAVKMLRPDAsknARED-----FLKEVKIMS-QLKDPNI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 470 TQLY--CcfqTKDR-LFFVMEYVNGGDLmFQIQRSRKFDEPRSR-------------FYAAEVTSALMFLHQHGVIYRDL 533
Cdd:cd05051    82 VRLLgvC---TRDEpLCMIVEYMENGDL-NQFLQKHEAETQGASatnsktlsygtllYMATQIASGMKYLESLNFVHRDL 157
                         170       180
                  ....*....|....*....|
gi 1958782016 534 KLDNILLDAEGHCKLADFGM 553
Cdd:cd05051   158 ATRNCLVGPNYTIKIADFGM 177
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
411-614 4.87e-11

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: 64.74  E-value: 4.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 411 IKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDviLQDddvdcTMTEKR-----ILALARKHPYLTQLYCCFqTKDR---- 481
Cdd:cd07850     5 LKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRP--FQN-----VTHAKRayrelVLMKLVNHKNIIGLLNVF-TPQKslee 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 482 ---LFFVMEYVNGgDLMFQIQRsrKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGI 558
Cdd:cd07850    77 fqdVYLVMELMDA-NLCQVIQM--DLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 559 lNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 614
Cdd:cd07850   154 -TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHID 208
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
373-602 5.23e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 65.49  E-value: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 373 GEEHRASSSTDGQLASPGENGEVRQGQAKRLGLDEF----NFIKVLGKGSFGKVMLAELKGKDEvYAVKVLKKDVILQDD 448
Cdd:PHA03210  111 GAEDSDASHLDFDEAPPDAAGPVPLAQAKLKHDDEFlahfRVIDDLPAGAFGKIFICALRASTE-EAEARRGVNSTNQGK 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 449 DVDCTMTEKRILALARKHPYLTQ--LYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFD--------------EP---RS 509
Cdd:PHA03210  190 PKCERLIAKRVKAGSRAAIQLENeiLALGRLNHENILKIEEILRSEANTYMITQKYDFDlysfmydeafdwkdRPllkQT 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 510 RFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGmckegilngvTTTTF-----------CGTPDYIAPEI 578
Cdd:PHA03210  270 RAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFG----------TAMPFekereafdygwVGTVATNSPEI 339
                         250       260
                  ....*....|....*....|....
gi 1958782016 579 LQELEYGPSVDWWALGVLMYEMMA 602
Cdd:PHA03210  340 LAGDGYCEITDIWSCGLILLDMLS 363
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
414-625 5.49e-11

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 64.32  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 414 LGKGSFGKVMLAELK-GKDEV-YAVKvlkkdvilQDDDVDCTMTEKRILALAR--KHPYLTQLYCCF--QTKDRLFFVME 487
Cdd:cd07867    10 VGRGTYGHVYKAKRKdGKDEKeYALK--------QIEGTGISMSACREIALLRelKHPNVIALQKVFlsHSDRKVWLLFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 488 YVNGgDL--MFQIQRSRKFDE-----PRSRFYAA--EVTSALMFLHQHGVIYRDLKLDNILLDAEG----HCKLADFGMC 554
Cdd:cd07867    82 YAEH-DLwhIIKFHRASKANKkpmqlPRSMVKSLlyQILDGIHYLHANWVLHRDLKPANILVMGEGpergRVKIADMGFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782016 555 KE--------GILNGVTTTTFcgtpdYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL 625
Cdd:cd07867   161 RLfnsplkplADLDPVVVTFW-----YRAPELLlGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQL 235
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
170-220 5.65e-11

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410410  Cd Length: 55  Bit Score: 58.02  E-value: 5.65e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20860     3 HNFQETTYLKPTFCDNCAGFLWGVI-KQGYRCKDCGMNCHKQCKDLVVFEC 52
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
170-220 9.96e-11

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; 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. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) 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. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 57.29  E-value: 9.96e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLYGLV-RQGLKCKDCGMNVHHRCKENVPHLC 50
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
168-212 5.07e-10

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410360  Cd Length: 52  Bit Score: 55.34  E-value: 5.07e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958782016 168 NGHKF-MATYlRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRC 212
Cdd:cd20810     1 TGHSFeLTTF-KEPTTCSVCKKLLKGLF-FQGYKCSVCGAAVHKEC 44
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
166-226 1.84e-08

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 51.58  E-value: 1.84e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 166 QVNGHKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAGLKKQ 226
Cdd:cd20841     7 QIRPHTLYVHSYKAPTFCDYCGEMLWGLV-RQGLKCEGCGLNYHKRCAFKIPNNCSGVRKR 66
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
166-226 3.16e-08

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 50.79  E-value: 3.16e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 166 QVNGHKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAGLKKQ 226
Cdd:cd20839     4 QIRPHALFVHSYRAPAFCDHCGEMLWGLV-RQGLKCEGCGLNYHKRCAFKIPNNCSGVRKR 63
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
170-222 3.25e-08

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 50.36  E-value: 3.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20796     2 HTFVVHTYTKPTVCQHCKKLLKGLF-RQGLQCKDCKFNCHKKCAEKVPKDCTG 53
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
165-220 6.87e-08

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 49.36  E-value: 6.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 165 HQVNGHKFMAtylrqPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20837     1 HRFKVYNYMS-----PTFCDHCGSLLWGLF-RQGLKCEECGMNVHHKCQKKVANLC 50
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
170-222 1.30e-07

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 48.47  E-value: 1.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGViGKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20824     2 HNFKPHSFSIPTKCDYCGEKIWGL-SKKGLSCKDCGFNCHIKCELKVPPECPG 53
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
243-294 2.57e-07

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; 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. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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. 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. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 47.65  E-value: 2.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGV 294
Cdd:cd20794     3 HLFQAKRFNRRAVCAYCSDRIWGLGRQGYKCINCKLLVHKKCHKLVKVACGQ 54
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
163-212 6.28e-07

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 46.70  E-value: 6.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 163 RVHQVNGHKFMAtylrqPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRC 212
Cdd:cd20797     2 RPHVVEVEQYMT-----PTFCDYCGEMLTGLM-KQGVKCKNCRCNFHKRC 45
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
170-220 6.69e-07

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410407  Cd Length: 61  Bit Score: 46.96  E-value: 6.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIGkQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20857     6 HNFKVHTFRGPHWCEYCANFMWGLIA-QGVRCSDCGLNVHKQCSKHVPNDC 55
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
166-226 1.05e-06

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 46.59  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 166 QVNGHKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAGLKKQ 226
Cdd:cd20840     7 QIRPHALNVHSYRAPAFCDHCGEMLFGLV-RQGLKCDGCGLNYHKRCAFSIPNNCSGARKR 66
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
243-292 1.21e-06

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; 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. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 45.75  E-value: 1.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd21095     3 HLFQAKRFNRRAYCGQCSERIWGLGRQGYKCINCKLLVHKRCHKLVPLTC 52
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
170-212 1.40e-06

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 45.76  E-value: 1.40e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRC 212
Cdd:cd20795     4 HSLFVHSYKSPTFCDFCGEMLFGLV-RQGLKCEGCGLNFHKRC 45
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
170-220 2.54e-06

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 44.95  E-value: 2.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVGLV-RQGLVCEVCGYACHVSCADKAPQVC 50
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
170-221 1.12e-05

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 43.17  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCA 221
Cdd:cd20827     2 HRFEKHNFTTPTYCDYCSSLLWGLV-KTGMRCADCGYSCHEKCLEHVPKNCT 52
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
169-220 1.16e-05

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 43.15  E-value: 1.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782016 169 GHKFMATYLRQPTYCSHCRDFIWGvigkQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20826     2 SHSFKEKSFRKPRTCDVCKQIIWN----EGSSCRVCKYACHRKCEPKVTAAC 49
C1_aPKC_iota cd21094
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
243-293 1.45e-05

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota type; 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. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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. Members of this family contain C1 domain found in aPKC isoform iota. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410447  Cd Length: 55  Bit Score: 43.07  E-value: 1.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCG 293
Cdd:cd21094     3 HTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECG 53
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
170-222 1.88e-05

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 43.85  E-value: 1.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20842    35 HTFVIHSYTRPTVCQYCKKLLKGLF-RQGLQCKDCKFNCHKRCAPKVPNNCLG 86
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
170-220 3.38e-05

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 41.72  E-value: 3.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20798     2 HTLAEHNYKKPTVCKVCDKLLVGLV-RQGLKCRDCGVNVHKKCASLLPSNC 51
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
165-220 3.83e-05

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 41.66  E-value: 3.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782016 165 HQVNGHKFMAtylrqPTYCSHCRDFIWGvIGKQGYQCQVCTCVVHKRCHELIITKC 220
Cdd:cd20828     6 HNFEPHSFVT-----PTNCDYCLQILWG-IVKKGMKCSECGYNCHEKCQPQVPKQC 55
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
170-222 5.88e-05

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 41.88  E-value: 5.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20843    12 HTFVIHSYTRPTVCQFCKKLLKGLF-RQGLQCKDCKFNCHKRCATRVPNDCLG 63
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
170-214 1.12e-04

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 40.39  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHE 214
Cdd:cd20817     1 HSFQEHTFKKPTFCDVCKELLVGLS-KQGLRCKNCKMNVHHKCQE 44
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
170-222 2.69e-04

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 39.61  E-value: 2.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782016 170 HKFMATYLRQPTYCSHCRDFIWGVIgKQGYQCQVCTCVVHKRCHELIITKCAG 222
Cdd:cd20844     6 HTFAVHSYTRPTICQYCKRLLKGLF-RQGMQCKDCRFNCHKRCASKVPRDCLG 57
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
243-292 3.16e-04

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 39.25  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLL-RQGLQCKVCKMNVHRRCETNVAPNC 292
Cdd:cd20831     6 HTFVATHFKGGPSCAVCNKLIPGRFgKQGYQCRDCGLICHKRCHVKVETHC 56
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
243-284 1.18e-03

first protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410379  Cd Length: 53  Bit Score: 37.33  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958782016 243 HKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRC 284
Cdd:cd20829     1 HRLVDVYFVTPILCRHCKDYIWGKGKVGVRCEDCHACFHLVC 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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