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Conserved domains on  [gi|148539879|ref|NP_005151|]
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G protein-coupled receptor kinase 3 isoform 1 [Homo sapiens]

Protein Classification

beta-adrenergic receptor kinase 2( domain architecture ID 10171709)

beta-adrenergic receptor kinase 2 specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
185-530 0e+00

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: 736.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTP 264
Cdd:cd05633    1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05633   81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd05633  161 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 425 LEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQE 504
Cdd:cd05633  241 LEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQE 320
                        330       340
                 ....*....|....*....|....*.
gi 148539879 505 LYKNFPLVISERWQQEVTETVYEAVN 530
Cdd:cd05633  321 LYKNFPLVISERWQQEVAETVYEAVN 346
RGS_GRK2_GRK3 cd08747
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 ...
30-186 3.23e-108

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 (GRK2) and G protein-coupled receptor kinase 3 (GRK3); The RGS domain is an essential part of the GRK2 (G protein-coupled receptor kinases 2) and the GRK3 proteins, which are members of the beta-adrenergic receptor kinases subfamily. GRK2 and GRK3 are ubiquitously expressed and can phosphorylate many different GPCR. The C-terminus of GRK2 and 3 contains a plekstrin homology domain (PH) with binding sites for the membrane phospholipid PIP2 and free G#? subunits. These specific interactions could help to maintain a membrane-bound population of GRK2 prior to the agonist-dependent overt GRK2 translocation. GRK2 and GRK3 are members of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


:

Pssm-ID: 188701  Cd Length: 157  Bit Score: 324.31  E-value: 3.23e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  30 KRIVLPEPSIRSVMQKYLAERNEITFDKIFNQKIGFLLFKDFCLNEINEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIY 109
Cdd:cd08747    1 KKILLPDPSIRSVMHKYLEKRGEVTFDKIFNQKLGYLLFKDFCENVSEEPVPQLKFYEEIKKYEKLDTEEERIKKAREIY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 110 DAYIMKELLSCSHPFSKQAVEHVQSHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVELNIHL 186
Cdd:cd08747   81 DNYIMKELLSCSHPFSKSAVEHVQKHLSKKEVPVDLFEPYIEEICDSLRGDVFQKFLESDKFTRFCQWKNLELNIQL 157
PH_GRK2_subgroup cd01240
G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain; GRKs are a ...
553-670 3.35e-68

G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain; GRKs are a family of serine-threonine kinases which phosphorylates activated G-protein coupled receptors leading to the release of the previously bound heterotrimeric G protein agonist and thus signal termination. There are seven mammalian GRKs (GRK1-7) grouped into three subfamilies: GRK1 (GRK1 and 7), GRK2 (GRK2 and 3), and GRK4 (GRK4-6). GRKs have three functional components: an N-terminal Regulators of G-protein signaling (RGS) which interacts with the seven-trans-membrane helical receptor protein and/or other membrane targets, a central catalytic protein kinase C (PKc) domain, and a C-terminal section containing a autophosphorylation region and a variable region that mediates membrane association. In both GRK2 (also known as beta-adrenergic receptor kinase-1) and GRK3 (beta-adrenergic receptor kinase-2), the C-terminal variable region contains a PH domain which gives binding specificity to Gbetagamma proteins. The GRK2 PH domain has an extended C-terminal helix, which mediates interactions with G beta gamma subunits. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269946  Cd Length: 118  Bit Score: 218.76  E-value: 3.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 553 YALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQNLLTMEQILSVEETQIKDKKCILFRIKGGKQFVL 632
Cdd:cd01240    1 YAKGKDCIVHGYILKLGGPFLSAWQRRYFYLFPNRLELYGEGEDQQNKLELEEMDQVEETCIKGEKCIQLKLKGGKQFLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 148539879 633 QCESDPEFVQWKKELNETFKEAQRLLRRAPKFLNKPRS 670
Cdd:cd01240   81 NSDSEPELVQWKKELRDAFREAQRLLQRMPKKAGKIYG 118
 
Name Accession Description Interval E-value
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
185-530 0e+00

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: 736.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTP 264
Cdd:cd05633    1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05633   81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd05633  161 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 425 LEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQE 504
Cdd:cd05633  241 LEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQE 320
                        330       340
                 ....*....|....*....|....*.
gi 148539879 505 LYKNFPLVISERWQQEVTETVYEAVN 530
Cdd:cd05633  321 LYKNFPLVISERWQQEVAETVYEAVN 346
RGS_GRK2_GRK3 cd08747
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 ...
30-186 3.23e-108

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 (GRK2) and G protein-coupled receptor kinase 3 (GRK3); The RGS domain is an essential part of the GRK2 (G protein-coupled receptor kinases 2) and the GRK3 proteins, which are members of the beta-adrenergic receptor kinases subfamily. GRK2 and GRK3 are ubiquitously expressed and can phosphorylate many different GPCR. The C-terminus of GRK2 and 3 contains a plekstrin homology domain (PH) with binding sites for the membrane phospholipid PIP2 and free G#? subunits. These specific interactions could help to maintain a membrane-bound population of GRK2 prior to the agonist-dependent overt GRK2 translocation. GRK2 and GRK3 are members of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188701  Cd Length: 157  Bit Score: 324.31  E-value: 3.23e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  30 KRIVLPEPSIRSVMQKYLAERNEITFDKIFNQKIGFLLFKDFCLNEINEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIY 109
Cdd:cd08747    1 KKILLPDPSIRSVMHKYLEKRGEVTFDKIFNQKLGYLLFKDFCENVSEEPVPQLKFYEEIKKYEKLDTEEERIKKAREIY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 110 DAYIMKELLSCSHPFSKQAVEHVQSHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVELNIHL 186
Cdd:cd08747   81 DNYIMKELLSCSHPFSKSAVEHVQKHLSKKEVPVDLFEPYIEEICDSLRGDVFQKFLESDKFTRFCQWKNLELNIQL 157
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
191-453 3.17e-82

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 260.54  E-value: 3.17e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFI 270
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKL---KHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS 350
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   351 -VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:smart00220 156 fVGTPEYMAPEVLL-GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLElFKKIGKPKPPFPPPEWDISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|....*
gi 148539879   429 LQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:smart00220 235 LVKDPEKRLTAE-----EALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
191-453 3.17e-70

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 227.90  E-value: 3.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVStgdCPFIVCMTYAFHTPDKLCFI 270
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKN-ILREIKILKKLN---HPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEhmhnrfvvyrdlkpanilldehgharisdlglacdfSKKKPHAS 350
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE------------------------------------SGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  351 VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQ 430
Cdd:pfam00069 121 VGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|...
gi 148539879  431 RDVSKRLGCHgggsqEVKEHSFF 453
Cdd:pfam00069 200 KDPSKRLTAT-----QALQHPWF 217
PH_GRK2_subgroup cd01240
G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain; GRKs are a ...
553-670 3.35e-68

G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain; GRKs are a family of serine-threonine kinases which phosphorylates activated G-protein coupled receptors leading to the release of the previously bound heterotrimeric G protein agonist and thus signal termination. There are seven mammalian GRKs (GRK1-7) grouped into three subfamilies: GRK1 (GRK1 and 7), GRK2 (GRK2 and 3), and GRK4 (GRK4-6). GRKs have three functional components: an N-terminal Regulators of G-protein signaling (RGS) which interacts with the seven-trans-membrane helical receptor protein and/or other membrane targets, a central catalytic protein kinase C (PKc) domain, and a C-terminal section containing a autophosphorylation region and a variable region that mediates membrane association. In both GRK2 (also known as beta-adrenergic receptor kinase-1) and GRK3 (beta-adrenergic receptor kinase-2), the C-terminal variable region contains a PH domain which gives binding specificity to Gbetagamma proteins. The GRK2 PH domain has an extended C-terminal helix, which mediates interactions with G beta gamma subunits. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269946  Cd Length: 118  Bit Score: 218.76  E-value: 3.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 553 YALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQNLLTMEQILSVEETQIKDKKCILFRIKGGKQFVL 632
Cdd:cd01240    1 YAKGKDCIVHGYILKLGGPFLSAWQRRYFYLFPNRLELYGEGEDQQNKLELEEMDQVEETCIKGEKCIQLKLKGGKQFLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 148539879 633 QCESDPEFVQWKKELNETFKEAQRLLRRAPKFLNKPRS 670
Cdd:cd01240   81 NSDSEPELVQWKKELRDAFREAQRLLQRMPKKAGKIYG 118
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
188-509 9.31e-64

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 214.68  E-value: 9.31e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDK 266
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlKMKQVQHVAQEKSILMEL----SHPFIVNMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlacdFSKKK 346
Cdd:PTZ00263  93 VYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG----FAKKV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS---VGTHGYMAPEVLQ-KGtaYDSSADWFSLGCMLFKLLRGHSPFRQH---KTKDKheidrmTLTVNVELPDTFSP 419
Cdd:PTZ00263 169 PDRTftlCGTPEYLAPEVIQsKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDtpfRIYEK------ILAGRLKFPNWFDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 420 ELKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPlIPPRGEvNAADAFDIGSFDEEDTKGIK-L 498
Cdd:PTZ00263 241 RARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAP-IPVRVK-SPGDTSNFEKYPDSPVDRLPpL 318
                        330
                 ....*....|.
gi 148539879 499 LDCDQELYKNF 509
Cdd:PTZ00263 319 TAAQQAEFAGF 329
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
191-436 9.18e-44

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.42  E-value: 9.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNE-RIMLSLVStgdcPFIVcMTYAFHTPDKLCF 269
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREaRALARLNH----PNIV-RVYDVGEEDGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 I-LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK---K 345
Cdd:COG0515   84 LvMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGatlT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTF----SPEL 421
Cdd:COG0515  164 QTGTVVGTPGYMAPEQAR-GEPVDPRSDVYSLGVTLYELLTGRPPFD---GDSPAELLRAHLREPPPPPSELrpdlPPAL 239
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:COG0515  240 DAIVLRALAKDPEER 254
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
54-174 7.62e-29

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 111.21  E-value: 7.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879    54 TFDKIFNQKIGFLLFKDFCLNEinEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCsHPFSKQAVEHVQ 133
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESE--FSEENLEFWLAVEEFKKAEDDEERIAKAREIYDKFLSPNAPKE-VNLDSDLREKIE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 148539879   134 SHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRF 174
Cdd:smart00315  78 ENLESEEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
55-174 1.34e-26

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 459870  Cd Length: 117  Bit Score: 104.62  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   55 FDKIFNQKIGFLLFKDFCLNEINEavPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCSHpFSKQAVEHVQS 134
Cdd:pfam00615   2 FDSLLEDQPGRRLFRQFLESEFSE--ENLEFWLACEEFKKADPDEERLKKAKEIYNEFLAPGSPKEIN-LDSDLREEIRE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 148539879  135 HLsKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRF 174
Cdd:pfam00615  79 NL-EKEPTRDLFDEAQAEVYELMEKDSYPRFLKSPLYLRL 117
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
249-391 1.79e-14

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 76.76  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 249 GDCPFIVcMTYafhtpdklcfildlMNGGDLHYHLSQHGVFSEKE-MRfYATEIILGLEHMHNRFVVYRDLKPANILLDE 327
Cdd:NF033483  79 GGIPYIV-MEY--------------VDGRTLKDYIREHGPLSPEEaVE-IMIQILSALEHAHRNGIVHRDIKPQNILITK 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 328 HGHARISDLGLACDFSkkkphAS--------VGTHGYMAPEvlQ-KGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:NF033483 143 DGRVKVTDFGIARALS-----STtmtqtnsvLGTVHYLSPE--QaRGGTVDARSDIYSLGIVLYEMLTGRPPF 208
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
560-649 5.61e-10

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 56.79  E-value: 5.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   560 IMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQ--------NLLTMEQILSVEETQIKDKKCILFRIKGGKQFV 631
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGCTVREAPDPDSSKKPHCFEIKTSDRKTLL 81
                           90
                   ....*....|....*...
gi 148539879   632 LQCESDPEFVQWKKELNE 649
Cdd:smart00233  82 LQAESEEEREKWVEALRK 99
PH pfam00169
PH domain; PH stands for pleckstrin homology.
560-649 2.10e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.26  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  560 IMHGYMLKLGNPFLTQWQRRYFYLFPNRLEW-----RGEGESRQNLLTMEQILSVEETQIKDKK---CILFRI---KGGK 628
Cdd:pfam00169   2 VKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYykddkSGKSKEPKGSISLSGCEVVEVVASDSPKrkfCFELRTgerTGKR 81
                          90       100
                  ....*....|....*....|.
gi 148539879  629 QFVLQCESDPEFVQWKKELNE 649
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAIQS 102
 
Name Accession Description Interval E-value
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
185-530 0e+00

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: 736.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTP 264
Cdd:cd05633    1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05633   81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd05633  161 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 425 LEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQE 504
Cdd:cd05633  241 LEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQE 320
                        330       340
                 ....*....|....*....|....*.
gi 148539879 505 LYKNFPLVISERWQQEVTETVYEAVN 530
Cdd:cd05633  321 LYKNFPLVISERWQQEVAETVYEAVN 346
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
196-473 0e+00

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: 639.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTG-DCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGgDCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTH 354
Cdd:cd05606   81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd05606  161 GYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVS 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148539879 435 KRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPP 473
Cdd:cd05606  241 KRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIPP 279
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
190-510 0e+00

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: 635.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd14223   81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLL 429
Cdd:cd14223  161 SVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 430 QRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQELYKNF 509
Cdd:cd14223  241 QRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLESDQELYRNF 320

                 .
gi 148539879 510 P 510
Cdd:cd14223  321 P 321
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
197-473 2.90e-165

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: 475.09  E-value: 2.90e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVS---SPFIVSLAYAFETKDKLCLVLTLMNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS-KKKPHASVGT 353
Cdd:cd05577   78 GDLKYHIYNVGtrGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKgGKKIKGRVGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK-DKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05577  158 HGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKvDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKD 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 148539879 433 VSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPP 473
Cdd:cd05577  238 PERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVPD 278
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
197-453 1.03e-117

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: 352.59  E-value: 1.03e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERV---NHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS--VGTH 354
Cdd:cd05123   78 GELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYtfCGTP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHktkDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd05123  158 EYLAPEVLL-GKGYGKAVDWWSLGVLLYEMLTGKPPFYAE---NRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPT 233
                        250
                 ....*....|....*....
gi 148539879 435 KRLGChgGGSQEVKEHSFF 453
Cdd:cd05123  234 KRLGS--GGAEEIKAHPFF 250
RGS_GRK2_GRK3 cd08747
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 ...
30-186 3.23e-108

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 2 (GRK2) and G protein-coupled receptor kinase 3 (GRK3); The RGS domain is an essential part of the GRK2 (G protein-coupled receptor kinases 2) and the GRK3 proteins, which are members of the beta-adrenergic receptor kinases subfamily. GRK2 and GRK3 are ubiquitously expressed and can phosphorylate many different GPCR. The C-terminus of GRK2 and 3 contains a plekstrin homology domain (PH) with binding sites for the membrane phospholipid PIP2 and free G#? subunits. These specific interactions could help to maintain a membrane-bound population of GRK2 prior to the agonist-dependent overt GRK2 translocation. GRK2 and GRK3 are members of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188701  Cd Length: 157  Bit Score: 324.31  E-value: 3.23e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  30 KRIVLPEPSIRSVMQKYLAERNEITFDKIFNQKIGFLLFKDFCLNEINEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIY 109
Cdd:cd08747    1 KKILLPDPSIRSVMHKYLEKRGEVTFDKIFNQKLGYLLFKDFCENVSEEPVPQLKFYEEIKKYEKLDTEEERIKKAREIY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 110 DAYIMKELLSCSHPFSKQAVEHVQSHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVELNIHL 186
Cdd:cd08747   81 DNYIMKELLSCSHPFSKSAVEHVQKHLSKKEVPVDLFEPYIEEICDSLRGDVFQKFLESDKFTRFCQWKNLELNIQL 157
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
191-472 3.26e-106

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: 324.31  E-value: 3.26e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKV---NSRFVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP- 347
Cdd:cd05605   79 LTIMNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETi 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd05605  159 RGRVGTVGYMAPEVV-KNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKrEEVDRRVKEDQEEYSEKFSEEAKSICS 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 427 GLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05605  238 QLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
191-472 1.74e-96

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: 299.25  E-value: 1.74e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNS---RFVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP- 347
Cdd:cd05630   79 LTLMNGGDLKFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTi 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd05630  159 KGRVGTVGYMAPEVV-KNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKrEEVERLVKEVPEEYSEKFSPQARSLCS 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 427 GLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05630  238 MLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
191-472 1.10e-90

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: 283.81  E-value: 1.10e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcpFIVCMTYAFHTPDKLCFI 270
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSR---FVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK-KKP 347
Cdd:cd05631   79 LTIMNGGDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEgETV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd05631  159 RGRVGTVGYMAPEVINN-EKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKrEEVDRRVKEDQEEYSEKFSEDAKSICR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 427 GLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05631  238 MLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
189-502 1.47e-83

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: 266.45  E-value: 1.47e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNS---QFVVNLAYAYETKDALC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd05632   79 LVLTIMNGGDLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 P-HASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd05632  159 SiRGRVGTVGYMAPEVL-NNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKrEEVDRRVLETEEVYSAKFSEEAKSI 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 425 LEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEedTKGIKLLDCD 502
Cdd:cd05632  238 CKMLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFST--VKGVNLDQTD 313
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
191-472 1.55e-83

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: 265.59  E-value: 1.55e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHS---RFIVSLAYAFQTKTDLCLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHL----SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--K 344
Cdd:cd05608   80 MTIMNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKdgQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK-DKHEIDRMTLTVNVELPDTFSPELKS 423
Cdd:cd05608  160 TKTKGYAGTPGFMAPELLL-GEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKvENKELKQRILNDSVTYSEKFSPASKS 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 424 LLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05608  239 ICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
191-453 3.17e-82

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 260.54  E-value: 3.17e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFI 270
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKL---KHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS 350
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   351 -VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:smart00220 156 fVGTPEYMAPEVLL-GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLElFKKIGKPKPPFPPPEWDISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|....*
gi 148539879   429 LQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:smart00220 235 LVKDPEKRLTAE-----EALQHPFF 254
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
195-509 9.55e-82

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: 261.77  E-value: 9.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALAN--RHPFLTGLHACFQTEDRLYFVMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCD---FSKKKPHASV 351
Cdd:cd05570   79 NGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGM-CKegiWGGNTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQR 431
Cdd:cd05570  158 GTPDYIAPEILR-EQDYGFSVDWWALGVLLYEMLAGQSPFE---GDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 432 DVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTKG---------IKLLDCD 502
Cdd:cd05570  234 DPARRLGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKP-----KVKSPRDTSNFDPEFTSEsprltpvdsDLLTNID 308

                 ....*..
gi 148539879 503 QELYKNF 509
Cdd:cd05570  309 QEEFRGF 315
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
196-456 1.17e-79

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: 254.63  E-value: 1.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGET-LALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd05583    1 VLGTGAYGKVFLVRKVgghDAGKLYAMKVLKKATIVQKAKTAeHTMTERQVLEAVR--QSPFLVTLHYAFQTDAKLHLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF---SKKKPH 348
Cdd:cd05583   79 DYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFlpgENDRAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd05583  159 SFCGTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQsEISKRILKSHPPIPKTFSAEAKDFIL 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 427 GLLQRDVSKRLGCHGGGSQEVKEHSFFKGV 456
Cdd:cd05583  239 KLLEKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
189-489 6.54e-79

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: 253.27  E-value: 6.54e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMKQGETLaLNERIMLSLVSTgdcPFIVCMTYAFHTPDKL 267
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKaKIIKLKQVEHV-LNEKRILSEVRH---PFIVNLLGSFQDDRNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSKKKP 347
Cdd:cd05580   77 YMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFA-KRVKDRT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEG 427
Cdd:cd05580  156 YTLCGTPEYLAPEIIL-SKGHGKAVDWWALGILIYEMLAGYPPFF---DENPMKIYEKILEGKIRFPSFFDPDAKDLIKR 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 428 LLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPrgevnAADAFDIGSFD 489
Cdd:cd05580  232 LLVVDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPK-----VRGPGDTSNFD 288
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
190-494 5.24e-78

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: 252.53  E-value: 5.24e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRI--KMKQGETlALNERIMLSLVStgDCPFIVCMTYAFHTP 264
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVsghDANKLYAMKVLRKAALvqKAKTVEH-TRTERNVLEHVR--QSPFLVTLHYAFQTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF-- 342
Cdd:cd05614   78 AKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFlt 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 -SKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD-KHEIDRMTLTVNVELPDTFSPE 420
Cdd:cd05614  158 eEKERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNtQSEVSRRILKCDPPFPSFIGPV 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 421 LKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPP-RGEVnaadafDIGSFDEEDTK 494
Cdd:cd05614  238 ARDLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSiRSEL------DVGNFAEEFTN 306
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
191-453 4.63e-77

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: 247.17  E-value: 4.63e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER-IMLSLvstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELeILQEL----EHPFLVNLWYSFQDEEDMYM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd05578   78 VVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:cd05578  158 STsGTKPYMAPEVFMR-AGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGWSEEAIDLINKL 236
                        250       260
                 ....*....|....*....|....*
gi 148539879 429 LQRDVSKRLGCHgggsQEVKEHSFF 453
Cdd:cd05578  237 LERDPQKRLGDL----SDLKNHPYF 257
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
195-491 1.53e-76

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: 248.39  E-value: 1.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkMKQGETlalnERIMLS---LVSTGDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAI-LKRNEV----KHIMAErnvLLKNVKHPFLVGLHYSFQTKDKLYFVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV 351
Cdd:cd05575   76 DYVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 --GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLL 429
Cdd:cd05575  156 fcGTPEYLAPEVLRK-QPYDRTVDWWCLGAVLYEMLYGLPPFY---SRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLL 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 430 QRDVSKRLGcHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEE 491
Cdd:cd05575  232 QKDRTKRLG-SGNDFLEIKNHSFFRPINWDDLEAKKIPPPFNP-----NVSGPLDLRNIDPE 287
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
195-494 4.94e-75

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: 244.24  E-value: 4.94e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRK---ADTGKMYAMKCLDKKRIKMKQGETLALN-ERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05584    2 KVLGKGGYGKVFQVRKttgSDKGKIFAMKVLKKASIVRNQKDTAHTKaERNILEAVKH---PFIVDLHYAFQTGGKLYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCDFS---KKKP 347
Cdd:cd05584   79 LEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGL-CKESihdGTVT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF---RQHKTKDKheIDRMTLTvnveLPDTFSPELKSL 424
Cdd:cd05584  158 HTFCGTIEYMAPEILTR-SGHGKAVDWWSLGALMYDMLTGAPPFtaeNRKKTIDK--ILKGKLN----LPPYLTNEARDL 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 425 LEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPrgevnAADAFDIGSFDEEDTK 494
Cdd:cd05584  231 LKKLLKRNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPL-----LQSEEDVSQFDSKFTK 295
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
191-472 2.37e-74

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: 241.35  E-value: 2.37e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNS---PFIVSLAYAFETKTHLCLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd05607   81 MSLMNGGDLKYHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 AS-VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK-DKHEIDRMTLTVNVELP-DTFSPELKSLL 425
Cdd:cd05607  161 TQrAGTNGYMAPEIL-KEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKvSKEELKRRTLEDEVKFEhQNFTEEAKDIC 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 426 EGLLQRDVSKRLGCHgGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05607  240 RLFLAKKPENRLGSR-TNDDDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
195-494 8.51e-74

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: 240.77  E-value: 8.51e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRK---ADTGKMYAMKCLDKKRIKMKQGETLALnERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd05582    1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDRVRTKM-ERDILADVNH---PFIVKLHYAFQTEGKLYLIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKPHA 349
Cdd:cd05582   77 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKEsiDHEKKAYS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLL 429
Cdd:cd05582  157 FCGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGSLPF---QGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALF 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 430 QRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNaaDAFdigSFDEEDTK 494
Cdd:cd05582  233 KRNPANRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPD--DTF---YFDPEFTS 292
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
195-494 5.07e-72

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: 236.48  E-value: 5.07e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQ---NTRHPFLTSLKYSFQTNDRLCFVMEYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaC--DFS-KKKPHASV 351
Cdd:cd05571   78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGL-CkeEISyGATTKTFC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQR 431
Cdd:cd05571  157 GTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFY---NRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 432 DVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 494
Cdd:cd05571  233 DPKKRLGGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKP-----QVTSETDTRYFDEEFTA 290
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
195-509 1.45e-71

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: 234.97  E-value: 1.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALAS--QHPFLTHLFCTFQTESHLFFVMEYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKPHASVG 352
Cdd:cd05592   79 NGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKEniYGENKASTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05592  159 TPDYIAPEIL-KGQKYNQSVDWWSFGVLLYEMLIGQSPFH---GEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 433 VSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK--------GIKLLDC-DQ 503
Cdd:cd05592  235 PEKRLGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKP-----KVKSANDVSNFDPDFTMekpvltpvDKKLLASmDQ 309

                 ....*.
gi 148539879 504 ELYKNF 509
Cdd:cd05592  310 EQFKGF 315
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
196-498 9.82e-71

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: 232.85  E-value: 9.82e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQV---DCPFIVPLKFSFQSPEKLYLVLAFIN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCDFSKKKPHAS---VG 352
Cdd:cd05585   78 GGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGL-CKLNMKDDDKTntfCG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkdkHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05585  157 TPEYLAPELLL-GHGYTKAVDWWTLGVLLYEMLTGLPPFYDENT---NEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRD 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 433 VSKRLGChgGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPrgevnAADAFDIGSFDEEDTKGIKL 498
Cdd:cd05585  233 PTKRLGY--NGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPA-----VENAIDTSNFDEEFTREKPI 291
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
197-493 2.08e-70

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: 232.46  E-value: 2.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-CDFSKKKP-HASVGTH 354
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSkADLTDNKTtNTFCGTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELP-DTFSPELKSLLEGLLQRDV 433
Cdd:cd05586  161 EYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFY---AEDTQQMYRNIAFGKVRFPkDVLSDEGRSFVKGLLNRNP 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 434 SKRLGCHGGGsQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05586  238 KHRLGAHDDA-VELKEHPFFADIDWDLLSKKKITPPFKP-----IVDSDTDVSNFDPEFT 291
Pkinase pfam00069
Protein kinase domain;
191-453 3.17e-70

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 227.90  E-value: 3.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVStgdCPFIVCMTYAFHTPDKLCFI 270
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKN-ILREIKILKKLN---HPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEhmhnrfvvyrdlkpanilldehgharisdlglacdfSKKKPHAS 350
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE------------------------------------SGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  351 VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQ 430
Cdd:pfam00069 121 VGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|...
gi 148539879  431 RDVSKRLGCHgggsqEVKEHSFF 453
Cdd:pfam00069 200 KDPSKRLTAT-----QALQHPWF 217
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
197-458 7.79e-70

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: 228.64  E-value: 7.79e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQ---NPFVVKLYYSFQGKKNLYLVMEYLPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC----DFSKKKPHAS-- 350
Cdd:cd05579   78 GDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvRRQIKLSIQKks 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 -----------VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDkhEIDRMTLTVNVELPDTF-- 417
Cdd:cd05579  158 ngapekedrriVGTPDYLAPEIL-LGQGHGKTVDWWSLGVILYEFLVGIPPF-HAETPE--EIFQNILNGKIEWPEDPev 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 148539879 418 SPELKSLLEGLLQRDVSKRLGChgGGSQEVKEHSFFKGVDW 458
Cdd:cd05579  234 SDEAKDLISKLLTPDPEKRLGA--KGIEEIKNHPFFKGIDW 272
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
195-474 1.00e-69

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: 230.20  E-value: 1.00e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDK----KRIKMKQgetlALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05574    7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDKeemiKRNKVKR----VLTEREILATL---DHPFLPTLYASFQTSTHLCFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHL-SQ-HGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP- 347
Cdd:cd05574   80 MDYCPGGELFRLLqKQpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPp 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 ---HAS---------------------------VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTK 397
Cdd:cd05574  160 vrkSLRkgsrrssvksieketfvaepsarsnsfVGTEEYIAPEVI-KGDGHGSAVDWWTLGILLYEMLYGTTPF---KGS 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 398 DKHEIDRMTLTVNVELPD--TFSPELKSLLEGLLQRDVSKRLGCHGGGSqEVKEHSFFKGVDWQhvYLQKYPPPLIPPR 474
Cdd:cd05574  236 NRDETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGSKRGAS-EIKRHPFFRGVNWA--LIRNMTPPIIPRP 311
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
191-472 4.76e-69

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: 227.58  E-value: 4.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRI--KMKQGETlALNERIMLSLVSTGdcPFIVCMTYAFHTPD 265
Cdd:cd05613    2 FELLKVLGTGAYGKVFLVRKVsghDAGKLYAMKVLKKATIvqKAKTAEH-TRTERQVLEHIRQS--PFLVTLHYAFQTDT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF--- 342
Cdd:cd05613   79 KLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFlld 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASVGTHGYMAPEVLQKG-TAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTVNVELPDTFSPE 420
Cdd:cd05613  159 ENERAYSFCGTIEYMAPEIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQaEISRRILKSEPPYPQEMSAL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 421 LKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05613  239 AKDIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
189-492 1.09e-68

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: 228.32  E-value: 1.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKR-IKMKQgETLALNER-IMlslvSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDmLKREQ-IAHVRAERdIL----ADADSPWIVRLHYAFQDEDH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd05573   76 LYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 P-------------------------------HASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF---R 392
Cdd:cd05573  156 DresylndsvntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLR-GTGYGPECDWWSLGVILYEMLYGFPPFysdS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 393 QHKTKDKheIdrMTLTVNVELPD--TFSPELKSLLEGLLqRDVSKRLgchgGGSQEVKEHSFFKGVDWQHvyLQKYPPPL 470
Cdd:cd05573  235 LVETYSK--I--MNWKESLVFPDdpDVSPEAIDLIRRLL-CDPEDRL----GSAEEIKAHPFFKGIDWEN--LRESPPPF 303
                        330       340
                 ....*....|....*....|..
gi 148539879 471 IPprgEVNAADafDIGSFDEED 492
Cdd:cd05573  304 VP---ELSSPT--DTSNFDDFE 320
PH_GRK2_subgroup cd01240
G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain; GRKs are a ...
553-670 3.35e-68

G Protein-Coupled Receptor Kinase 2 subgroup pleckstrin homology (PH) domain; GRKs are a family of serine-threonine kinases which phosphorylates activated G-protein coupled receptors leading to the release of the previously bound heterotrimeric G protein agonist and thus signal termination. There are seven mammalian GRKs (GRK1-7) grouped into three subfamilies: GRK1 (GRK1 and 7), GRK2 (GRK2 and 3), and GRK4 (GRK4-6). GRKs have three functional components: an N-terminal Regulators of G-protein signaling (RGS) which interacts with the seven-trans-membrane helical receptor protein and/or other membrane targets, a central catalytic protein kinase C (PKc) domain, and a C-terminal section containing a autophosphorylation region and a variable region that mediates membrane association. In both GRK2 (also known as beta-adrenergic receptor kinase-1) and GRK3 (beta-adrenergic receptor kinase-2), the C-terminal variable region contains a PH domain which gives binding specificity to Gbetagamma proteins. The GRK2 PH domain has an extended C-terminal helix, which mediates interactions with G beta gamma subunits. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269946  Cd Length: 118  Bit Score: 218.76  E-value: 3.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 553 YALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQNLLTMEQILSVEETQIKDKKCILFRIKGGKQFVL 632
Cdd:cd01240    1 YAKGKDCIVHGYILKLGGPFLSAWQRRYFYLFPNRLELYGEGEDQQNKLELEEMDQVEETCIKGEKCIQLKLKGGKQFLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 148539879 633 QCESDPEFVQWKKELNETFKEAQRLLRRAPKFLNKPRS 670
Cdd:cd01240   81 NSDSEPELVQWKKELRDAFREAQRLLQRMPKKAGKIYG 118
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
195-493 1.31e-67

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: 224.89  E-value: 1.31e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRH---PFLTALKYAFQTHDRLCFVMEYA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA----CDFSKKKPHAs 350
Cdd:cd05595   78 NGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCkegiTDGATMKTFC- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 vGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQ 430
Cdd:cd05595  157 -GTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY---NQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLK 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 431 RDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05595  232 KDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKP-----QVTSEVDTRYFDDEFT 289
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
189-493 1.50e-66

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: 221.72  E-value: 1.50e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkMKQGETLALN-ERIMLSLVstgDCPFIVCMTYAFHTPDKL 267
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEM-LEKEQVAHVRaERDILAEA---DNPWVVKLYYSFQDEENL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCDFSKKKP 347
Cdd:cd05599   77 YLIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL-CTGLKKSH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HA--SVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF---RQHKTKDKHEIDRMTLTVNVELPdtFSPELK 422
Cdd:cd05599  156 LAysTVGTPDYIAPEVFLQ-KGYGKECDWWSLGVIMYEMLIGYPPFcsdDPQETCRKIMNWRETLVFPPEVP--ISPEAK 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 423 SLLEGLLQrDVSKRLGCHggGSQEVKEHSFFKGVDWQHVYLQkyPPPLIPprgEVNAADafDIGSFDEEDT 493
Cdd:cd05599  233 DLIERLLC-DAEHRLGAN--GVEEIKSHPFFKGVDWDHIRER--PAPILP---EVKSIL--DTSNFDEFEE 293
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
187-493 4.54e-64

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: 216.10  E-value: 4.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDK 266
Cdd:cd05593   13 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRH---PFLTSLKYSFQTKDR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA----CDF 342
Cdd:cd05593   90 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCkegiTDA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHAsvGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDTFSPELK 422
Cdd:cd05593  170 ATMKTFC--GTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEDIKFPRTLSADAK 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 423 SLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05593  244 SLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKP-----QVTSETDTRYFDEEFT 309
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
189-453 7.87e-64

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: 213.23  E-value: 7.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI----KMKQgetlALNERIMLSLVSTgdcPFIVCMTYAFHTP 264
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIikekKVKY----VTIEKEVLSRLAH---PGIVKLYYTFQDE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05581   74 SKLYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHAS-------------------VGTHGYMAPEVLQKGTAyDSSADWFSLGCMLFKLLRGHSPFR---QHKTKDKhei 402
Cdd:cd05581  154 DSSPEStkgdadsqiaynqaraasfVGTAEYVSPELLNEKPA-GKSSDLWALGCIIYQMLTGKPPFRgsnEYLTFQK--- 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 403 drmTLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGCH-GGGSQEVKEHSFF 453
Cdd:cd05581  230 ---IVKLEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNeNGGYDELKAHPFF 278
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
188-509 9.31e-64

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 214.68  E-value: 9.31e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDK 266
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlKMKQVQHVAQEKSILMEL----SHPFIVNMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlacdFSKKK 346
Cdd:PTZ00263  93 VYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG----FAKKV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS---VGTHGYMAPEVLQ-KGtaYDSSADWFSLGCMLFKLLRGHSPFRQH---KTKDKheidrmTLTVNVELPDTFSP 419
Cdd:PTZ00263 169 PDRTftlCGTPEYLAPEVIQsKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDtpfRIYEK------ILAGRLKFPNWFDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 420 ELKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPlIPPRGEvNAADAFDIGSFDEEDTKGIK-L 498
Cdd:PTZ00263 241 RARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAP-IPVRVK-SPGDTSNFEKYPDSPVDRLPpL 318
                        330
                 ....*....|.
gi 148539879 499 LDCDQELYKNF 509
Cdd:PTZ00263 319 TAAQQAEFAGF 329
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
190-490 2.21e-63

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: 212.26  E-value: 2.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVvKLKQVEHTLNEKRILQAI----NFPFLVKLEYSFKDNSNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlacdFSKK-KP 347
Cdd:cd14209   78 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFG----FAKRvKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASV--GTHGYMAPEVLQ-KGtaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDTFSPELKSL 424
Cdd:cd14209  154 RTWTlcGTPEYLAPEIILsKG--YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE---KIVSGKVRFPSHFSSDLKDL 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 425 LEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDE 490
Cdd:cd14209  229 LRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIP-----KLKGPGDTSNFDD 289
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
186-493 5.09e-63

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: 213.74  E-value: 5.09e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPD 265
Cdd:cd05594   22 VTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ---NSRHPFLTALKYSFQTHD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMH-NRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05594   99 RLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASV--GTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDTFSPELK 422
Cdd:cd05594  179 DGATMKTfcGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEEIRFPRTLSPEAK 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 423 SLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05594  255 SLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKP-----QVTSETDTRYFDEEFT 320
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
191-509 2.74e-61

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: 207.92  E-value: 2.74e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQG-ETLALNERImLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEvESLMCEKRI-FETVNSARHPFLVNLFACFQTPEHVCF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCD---FSKKK 346
Cdd:cd05589   80 VMEYAAGGDLMMHIHED-VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL-CKegmGFGDR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd05589  158 TSTFCGTPEFLAPEVLTD-TSYTRAVDWWGLGVLIYEMLVGESPF---PGDDEEEVFDSIVNDEVRYPRFLSTEAISIMR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 427 GLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTKGIKLL------- 499
Cdd:cd05589  234 RLLRKNPERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVP-----TIKSPEDVSNFDEEFTSEKPVLtppkepr 308
                        330
                 ....*....|...
gi 148539879 500 ---DCDQELYKNF 509
Cdd:cd05589  309 pltEEEQALFKDF 321
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
195-494 3.20e-61

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: 207.51  E-value: 3.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLslVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVL--LKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV--G 352
Cdd:cd05603   79 NGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTfcG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05603  159 TPEYLAPEVLRK-EPYDRTVDWWCLGAVLYEMLYGLPPFY---SRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKD 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 433 VSKRLGCHgGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 494
Cdd:cd05603  235 QRRRLGAK-ADFLEIKNHVFFSPINWDDLYHKRITPPYNP-----NVAGPADLRHFDPEFTQ 290
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
195-494 1.11e-60

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: 206.35  E-value: 1.11e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER-IMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERnVLLKNVKH---PFLVGLHYSFQTTDKLYFVLDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCDFSKKKPHASV-- 351
Cdd:cd05604   79 VNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGL-CKEGISNSDTTTtf 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 -GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQ 430
Cdd:cd05604  158 cGTPEYLAPEVIRK-QPYDNTVDWWCLGSVLYEMLYGLPPFY---CRDTAEMYENILHKPLVLRPGISLTAWSILEELLE 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539879 431 RDVSKRLGCHgGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 494
Cdd:cd05604  234 KDRQLRLGAK-EDFLEIKNHPFFESINWTDLVQKKIPPPFNP-----NVNGPDDISNFDAEFTE 291
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
183-494 1.13e-60

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: 206.79  E-value: 1.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 183 NIHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER-IMLSLVSTgdcPFIVCMTYAF 261
Cdd:cd05602    1 NPHAKPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERnVLLKNVKH---PFLVGLHFSF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 HTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD 341
Cdd:cd05602   78 QTTDKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FSKKKPHASV--GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDTFSP 419
Cdd:cd05602  158 NIEPNGTTSTfcGTPEYLAPEVLHK-QPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYD---NILNKPLQLKPNITN 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 420 ELKSLLEGLLQRDVSKRLGCHgGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 494
Cdd:cd05602  234 SARHLLEGLLQKDRTKRLGAK-DDFTEIKNHIFFSPINWDDLINKKITPPFNP-----NVSGPNDLRHFDPEFTD 302
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
196-508 1.14e-59

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: 203.39  E-value: 1.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvsTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd05587    3 VLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLAL--SGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKPHASVGT 353
Cdd:cd05587   81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEgiFGGKTTRTFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDV 433
Cdd:cd05587  161 PDYIAPEIIAY-QPYGKSVDWWAYGVLLYEMLAGQPPF---DGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHP 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 434 SKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDiGSFDEEDTkgiKLLDCDQELYKN 508
Cdd:cd05587  237 AKRLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFD-KEFTKEPP---VLTPTDKLVIMN 307
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
197-459 1.21e-59

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: 201.30  E-value: 1.21e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER-IMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKeILEEC----NSPFIVKLYRTFKDKKYLYMLMEYCL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlacdFSKK-----KPHAS 350
Cdd:cd05572   77 GGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFG----FAKKlgsgrKTWTF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEV-LQKGtaYDSSADWFSLGCMLFKLLRGHSPFRQHKTkDKHEIDRMTLTVN--VELPDTFSPELKSLLEG 427
Cdd:cd05572  153 CGTPEYVAPEIiLNKG--YDFSVDYWSLGILLYELLTGRPPFGGDDE-DPMKIYNIILKGIdkIEFPKYIDKNAKNLIKQ 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 428 LLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQ 459
Cdd:cd05572  230 LLRRNPEERLGYLKGGIRDIKKHKWFEGFDWE 261
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
195-515 1.51e-58

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: 200.52  E-value: 1.51e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNH--PFLTQLYCCFQTPDRLFFVMEFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKPHASVG 352
Cdd:cd05590   79 NGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEgiFNGKTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05590  159 TPDYIAPEILQE-MLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFE---AILNDEVVYPTWLSQDAVDILKAFMTKN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 433 VSKRLGCHG-GGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgEVNAADafDIGSFDEEDTKGIKLLD---------CD 502
Cdd:cd05590  235 PTMRLGSLTlGGEEAILRHPFFKELDWEKLNRRQIEPPFRP---RIKSRE--DVSNFDPDFIKEDPVLTpieesllpmIN 309
                        330
                 ....*....|...
gi 148539879 503 QELYKNFPLVISE 515
Cdd:cd05590  310 QDEFRNFSYTAPE 322
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
190-509 1.78e-58

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: 200.23  E-value: 1.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvsTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLAL--SGKPPFLTQLHSCFQTMDRLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKP 347
Cdd:cd05616   79 VMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEniWDGVTT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEG 427
Cdd:cd05616  159 KTFCGTPDYIAPEIIAY-QPYGKSVDWWAFGVLLYEMLAGQAPF---EGEDEDELFQSIMEHNVAYPKSMSKEAVAICKG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 428 LLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADafdigsFDEEDTKG-IKLLDCDQELY 506
Cdd:cd05616  235 LMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGRNAEN------FDRFFTRHpPVLTPPDQEVI 308

                 ...
gi 148539879 507 KNF 509
Cdd:cd05616  309 RNI 311
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
191-452 4.13e-58

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: 196.93  E-value: 4.13e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSED-EEMLRREiEILKRL----DHPNIVKLYEVFEDDKNLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLACDFSKKK 346
Cdd:cd05117   77 VMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 P-HASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd05117  157 KlKTVCGTPYYVAPEVL-KGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEkILKGKYSFDSPEWKNVSEEAKDL 235
                        250       260
                 ....*....|....*....|....*...
gi 148539879 425 LEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd05117  236 IKRLLVVDPKKRLTA-----AEALNHPW 258
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
190-472 1.75e-57

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: 196.50  E-value: 1.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKR-IKMKQGETLAlNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvIRLKQEQHVH-NEKRVLKEVSH---PFIIRLFWTEHDQRFLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlacdFSKK--- 345
Cdd:cd05612   78 MLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFG----FAKKlrd 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd05612  154 RTWTLCGTPEYLAPEVIQS-KGHNKAVDWWALGILIYEMLVGYPPFFD---DNPFGIYEKILAGKLEFPRHLDLYAKDLI 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 426 EGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05612  230 KKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVP 276
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
197-458 2.12e-57

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: 195.39  E-value: 2.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKR-IKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDmIAKNQVTNVKAERAIMMI---QGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-CDFSKKKPHASVGTH 354
Cdd:cd05611   81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSrNGLEKRHNKKFVGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK---DKHEIDRMTLTVNVElpDTFSPELKSLLEGLLQR 431
Cdd:cd05611  161 DYLAPETIL-GVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDavfDNILSRRINWPEEVK--EFCSPEAVDLINRLLCM 237
                        250       260
                 ....*....|....*....|....*..
gi 148539879 432 DVSKRLGCHGGgsQEVKEHSFFKGVDW 458
Cdd:cd05611  238 DPAKRLGANGY--QEIKSHPFFKSINW 262
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
190-454 1.06e-56

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: 193.07  E-value: 1.06e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREiEIQSHL----RHPNILRLYGYFEDKKRIY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd14007   77 LILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNRRK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:cd14007  157 TFCGTLDYLPPEMV-EGKEYDYKVDIWSLGVLCYELLVGKPPF---ESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKL 232
                        250       260
                 ....*....|....*....|....*.
gi 148539879 429 LQRDVSKRLGChgggsQEVKEHSFFK 454
Cdd:cd14007  233 LQKDPSKRLSL-----EQVLNHPWIK 253
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
191-472 1.99e-56

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: 195.23  E-value: 1.99e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05598    3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILA---EADNEWVVKLYYSFQDKENLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF-----SKK 345
Cdd:cd05598   80 MDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdSKY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 -KPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF-------RQHKTKDKHEIDRMTLTVNvelpdtF 417
Cdd:cd05598  160 yLAHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILYEMLVGQPPFlaqtpaeTQLKVINWRTTLKIPHEAN------L 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 418 SPELKSLLEGLLqRDVSKRLGCHggGSQEVKEHSFFKGVDWQhvYLQKYPPPLIP 472
Cdd:cd05598  233 SPEAKDLILRLC-CDAEDRLGRN--GADEIKAHPFFAGIDWE--KLRKQKAPYIP 282
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
186-512 1.74e-55

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: 192.45  E-value: 1.74e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvsTGDCPFIVCMTYAFHTPD 265
Cdd:cd05619    2 LTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSL--AWEHPFLTHLFCTFQTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FS 343
Cdd:cd05619   80 NLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKEnmLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHktkDKHEIDRMTLTVNVELPDTFSPELKS 423
Cdd:cd05619  160 DAKTSTFCGTPDYIAPEILL-GQKYNTSVDWWSFGVLLYEMLIGQSPFHGQ---DEEELFQSIRMDNPFYPRWLEKEAKD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 424 LLEGLLQRDVSKRLGCHGggsqEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTKGIKLLDC-- 501
Cdd:cd05619  236 ILVKLFVREPERRLGVRG----DIRQHPFFREINWEALEEREIEPPFKP-----KVKSPFDCSNFDKEFLNEKPRLSFad 306
                        330
                 ....*....|....*...
gi 148539879 502 -------DQELYKNFPLV 512
Cdd:cd05619  307 ralinsmDQNMFRNFSFV 324
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
190-493 3.15e-55

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: 191.79  E-value: 3.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkMKQGETLALNE-RIMLSlvsTGDCPFIVCMTYAFHTPDKLC 268
Cdd:cd05597    2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEM-LKRAETACFREeRDVLV---NGDRRWITKLHYAFQDENYLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEM-RFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlAC----DFS 343
Cdd:cd05597   78 LVMDYYCGGDLLTLLSKFEDRLPEEMaRFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SClklrEDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLQ-----KGTaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIdrMTLTVNVELPD-- 415
Cdd:cd05597  157 TVQSSVAVGTPDYISPEILQamedgKGR-YGPECDWWSLGVCMYEMLYGETPFYAESLVETYgKI--MNHKEHFSFPDde 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 416 -TFSPELKSLLEGLLQrDVSKRLGchGGGSQEVKEHSFFKGVDWQHVYLQKypPPLIPprgEVNAADafDIGSFDEEDT 493
Cdd:cd05597  234 dDVSEEAKDLIRRLIC-SRERRLG--QNGIDDFKKHPFFEGIDWDNIRDST--PPYIP---EVTSPT--DTSNFDVDDD 302
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
193-450 4.72e-55

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: 188.50  E-value: 4.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 193 VHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd14003    4 LGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLL----NHPNIIKLYEVIETENKIYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK-KKPHASV 351
Cdd:cd14003   80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGgSLLKTFC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQkGTAYD-SSADWFSLGCMLFKLLRGHSPFRQHktkDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQ 430
Cdd:cd14003  160 GTPAYAAPEVLL-GRKYDgPKADVWSLGVILYAMLTGYLPFDDD---NDSKLFRKILKGKYPIPSHLSPDARDLIRRMLV 235
                        250       260
                 ....*....|....*....|
gi 148539879 431 RDVSKRLGChgggsQEVKEH 450
Cdd:cd14003  236 VDPSKRITI-----EEILNH 250
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
189-509 1.81e-53

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: 186.75  E-value: 1.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER-IMlslvSTGDCPFIVCMTYAFHTPDKL 267
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERdIM----AKANSPWITKLQYAFQDSENL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd05601   77 YLVMEYHPGGDLLSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 ---PHASVGTHGYMAPEVLQ-----KGTAYDSSADWFSLGCMLFKLLRGHSPF---RQHKTKDKheIdrMTLTVNVELPD 415
Cdd:cd05601  157 tvtSKMPVGTPDYIAPEVLTsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFtedTVIKTYSN--I--MNFKKFLKFPE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 416 TF--SPELKSLLEGLLQrDVSKRLGCHGggsqeVKEHSFFKGVDWQHvyLQKYPPPLIPprgEVNAADafDIGSFDEEDT 493
Cdd:cd05601  233 DPkvSESAVDLIKGLLT-DAKERLGYEG-----LCCHPFFSGIDWNN--LRQTVPPFVP---TLTSDD--DTSNFDEFEP 299
                        330
                 ....*....|....*.
gi 148539879 494 KGIKLLDCDQELYKNF 509
Cdd:cd05601  300 KKTRPSYENFNKSKGF 315
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
195-491 1.02e-52

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: 184.38  E-value: 1.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAW--ENPFLTHLYCTFQTKEHLFFVMEFL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKPHASVG 352
Cdd:cd05620   79 NGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKEnvFGDNRASTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTvnvELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05620  159 TPDYIAPEILQ-GLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTP---HYPRWITKESKDILEKLFERD 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 433 VSKRLGCHGggsqEVKEHSFFKGVDWQHVYLQKYPPPLIPprgEVNAADafDIGSFDEE 491
Cdd:cd05620  235 PTRRLGVVG----NIRGHPFFKTINWTALEKRELDPPFKP---KVKSPS--DYSNFDRE 284
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
188-472 1.59e-51

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: 182.12  E-value: 1.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMTYAFHTPDKL 267
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKP--PFLTQLHSCFQTVDRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKK 345
Cdd:cd05615   87 YFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEhmVEGV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd05615  167 TTRTFCGTPDYIAPEIIAY-QPYGRSVDWWAYGVLLYEMLAGQPPF---DGEDEDELFQSIMEHNVSYPKSLSKEAVSIC 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 426 EGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIP 472
Cdd:cd05615  243 KGLMTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKP 289
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
195-493 1.96e-51

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: 181.46  E-value: 1.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNH--PFLVGLHSCFQTESRLFFVIEFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV--G 352
Cdd:cd05588   79 NGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTfcG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEID------RMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd05588  159 TPNYIAPEIL-RGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDNPDQNtedylfQVILEKPIRIPRSLSVKAASVLK 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 427 GLLQRDVSKRLGCH-GGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05588  238 GFLNKNPAERLGCHpQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKP-----RIESERDLENFDPQFT 300
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
195-494 1.54e-50

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: 178.84  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKH--PFLTALHSCFQTKDRLFFVMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD--FSKKKPHASVG 352
Cdd:cd05591   79 NGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGKTTTTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd05591  159 TPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFE---SILHDDVLYPVWLSKEAVSILKAFMTKN 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539879 433 VSKRLGCHG--GGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 494
Cdd:cd05591  235 PAKRLGCVAsqGGEDAIRQHPFFREIDWEALEQRKVKPPFKP-----KIKTKRDANNFDQDFTK 293
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
180-507 2.73e-49

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: 176.37  E-value: 2.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 180 VELNIHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcPFIVCMTY 259
Cdd:cd05617    6 IKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSN--PFLVGLHS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 260 AFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd05617   84 CFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKPHASV--GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPF----RQHKTKDKHEIDRMTLTVNVEL 413
Cdd:cd05617  164 KEGLGPGDTTSTfcGTPNYIAPEIL-RGEEYGFSVDWWALGVLMFEMMAGRSPFdiitDNPDMNTEDYLFQVILEKPIRI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 414 PDTFSPELKSLLEGLLQRDVSKRLGCH-GGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEED 492
Cdd:cd05617  243 PRFLSVKASHVLKGFLNKDPKERLGCQpQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKP-----QITDDYGLENFDTQF 317
                        330
                 ....*....|....*.
gi 148539879 493 T-KGIKLLDCDQELYK 507
Cdd:cd05617  318 TsEPVQLTPDDEDVIK 333
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
186-493 7.22e-49

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: 175.61  E-value: 7.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdCPFIVCMTYAFHTPD 265
Cdd:cd05618   17 LGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASN--HPFLVGLHSCFQTES 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd05618   95 RLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASV--GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEID------RMTLTVNVELPDTF 417
Cdd:cd05618  175 GDTTSTfcGTPNYIAPEIL-RGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNtedylfQVILEKQIRIPRSL 253
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 418 SPELKSLLEGLLQRDVSKRLGCH-GGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05618  254 SVKAASVLKSFLNKDPKERLGCHpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKP-----NISGEFGLDNFDSQFT 325
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
189-493 8.07e-49

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: 175.81  E-value: 8.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLAlNERIMLSLVSTGDCPFIVCMTYAFHTPDKLC 268
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKS--EMFKKDQLA-HVKAERDVLAESDSPWVVSLYYSFQDAQYLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK---- 344
Cdd:cd05629   78 LIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFHKqhds 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 ---KKP------------------------------------------HASVGTHGYMAPEV-LQKGtaYDSSADWFSLG 378
Cdd:cd05629  158 ayyQKLlqgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaYSTVGTPDYIAPEIfLQQG--YGQECDWWSLG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 379 CMLFKLLRGHSPFrqhKTKDKHEIDR--MTLTVNVELPD--TFSPELKSLLEGLLQrDVSKRLGchGGGSQEVKEHSFFK 454
Cdd:cd05629  236 AIMFECLIGWPPF---CSENSHETYRkiINWRETLYFPDdiHLSVEAEDLIRRLIT-NAENRLG--RGGAHEIKSHPFFR 309
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 148539879 455 GVDWQHvyLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05629  310 GVDWDT--IRQIRAPFIP-----QLKSITDTSYFPTDEL 341
RGS_GRK-like cd08724
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase (GRK); ...
58-173 1.10e-48

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase (GRK); The RGS domain is found in G protein-coupled receptor kinases (GRKs). These proteins play a key role in phosphorylation-dependent desensitization/resensitization of GPCRs (G protein-coupled receptors), intracellular trafficking, endocytosis, as well as in the modulation of important intracellular signaling cascades by GPCR. GRKs also modulate cellular response in phosphorylation-independent manner using their ability to interact with multiple signaling proteins involved in many essential cellular pathways. The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. Based on sequence homology the GRK family consists of three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188679  Cd Length: 114  Bit Score: 166.21  E-value: 1.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  58 IFNQK-IGFLLFKDFCLNeINEAVPQVKFYEEIKEYEKLDnEEDRLCRSRQIYDAYIMKELLSCSHPFSKQAVEHVQSHL 136
Cdd:cd08724    1 ICEQQpIGRLLFRQFCET-RPELVPQIEFLDEIKEYEVAE-DEERAKKAREIYDKYIMKESLAHSHEFSKDAVEHVQENL 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 148539879 137 SkKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTR 173
Cdd:cd08724   79 E-KEVPKDLFQPYIEEIHDYLRGAPFQKFLESDYFTR 114
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
186-490 2.49e-48

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: 174.45  E-value: 2.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGET-LALNERimlSLVSTGDCPFIVCMTYAFHTP 264
Cdd:cd05600    8 LKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIM-KKKVLFKLNEVnHVLTER---DILTTTNSPWLVKLLYAFQDP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF-- 342
Cdd:cd05600   84 ENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTls 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 -------------------------------------SKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd05600  164 pkkiesmkirleevkntafleltakerrniyramrkeDQNYANSVVGSPDYMAPEVL-RGEGYDLTVDYWSLGCILFECL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 386 RGHSPFRQHKTKD--------KHEIDRmTLTVNVELPDTFSPELKSLLEGLLQrDVSKRLgchgGGSQEVKEHSFFKGVD 457
Cdd:cd05600  243 VGFPPFSGSTPNEtwanlyhwKKTLQR-PVYTDPDLEFNLSDEAWDLITKLIT-DPQDRL----QSPEQIKNHPFFKNID 316
                        330       340       350
                 ....*....|....*....|....*....|...
gi 148539879 458 WQHVyLQKYPPPLIPprgEVNaaDAFDIGSFDE 490
Cdd:cd05600  317 WDRL-REGSKPPFIP---ELE--SEIDTSYFDD 343
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
195-453 8.00e-48

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: 169.24  E-value: 8.00e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSL----KHPNIVRYLGTERTENTLNIFLEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLacdfSKKK-------- 346
Cdd:cd06606   82 PGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGC----AKRLaeiatgeg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdkheiDRMTLTVNV-------ELPDTFSP 419
Cdd:cd06606  158 TKSLRGTPYWMAPEVI-RGEGYGRAADIWSLGCTVIEMATGKPPWSELG-------NPVAALFKIgssgeppPIPEHLSE 229
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 420 ELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd06606  230 EAKDFLRKCLQRDPKKRPTA-----DELLQHPFL 258
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
133-492 2.22e-47

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: 172.50  E-value: 2.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 133 QSHLSKKQVTSTLFQPYIEEICESLRGDIF-QKFMESDK-FTRFCQwknvELNIHltMNEFSVHRIIGRGGFGEVYGCRK 210
Cdd:cd05624   20 ESALSVETLLDVLVCLYTECSHSPLRRDKYvSEFLEWAKpFTQLVK----EMQLH--RDDFEIIKVIGRGAFGEVAVVKM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 211 ADTGKMYAMKCLDKKRIkMKQGETLALNERimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQ-HGVF 289
Cdd:cd05624   94 KNTERIYAMKILNKWEM-LKRAETACFREE--RNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKfEDKL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 290 SEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK---KPHASVGTHGYMAPEVLQ--- 363
Cdd:cd05624  171 PEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDgtvQSSVAVGTPDYISPEILQame 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 364 KGTA-YDSSADWFSLGCMLFKLLRGHSPFRQH---KTKDK---HEiDRMTLTVNVelpDTFSPELKSLLEGLL-QRDvsK 435
Cdd:cd05624  251 DGMGkYGPECDWWSLGVCMYEMLYGETPFYAEslvETYGKimnHE-ERFQFPSHV---TDVSEEAKDLIQRLIcSRE--R 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 436 RLGCHggGSQEVKEHSFFKGVDWQHVylQKYPPPLIPprgevNAADAFDIGSFDEED 492
Cdd:cd05624  325 RLGQN--GIEDFKKHAFFEGLNWENI--RNLEAPYIP-----DVSSPSDTSNFDVDD 372
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
189-494 2.45e-47

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: 171.02  E-value: 2.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkMKQGETLAL-NER-IMlslvSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd05596   26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEM-IKRSDSAFFwEERdIM----AHANSEWIVQLHYAFQDDKY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd05596  101 LYMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS---VGTHGYMAPEVL--QKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQHK---TKDKHEIDRMTLTVNVELPdtF 417
Cdd:cd05596  180 LVRSdtaVGTPDYISPEVLksQGGDGvYGRECDWWSVGVFLYEMLVGDTPFYADSlvgTYGKIMNHKNSLQFPDDVE--I 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 418 SPELKSLLEGLLQrDVSKRLGCHggGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgEVNAADafDIGSFD--EEDTK 494
Cdd:cd05596  258 SKDAKSLICAFLT-DREVRLGRN--GIEEIKAHPFFKNDQWTWDNIRETVPPVVP---ELSSDI--DTSNFDdiEEDET 328
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
190-458 2.48e-46

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: 165.66  E-value: 2.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFA---ENPFVVSMYCSFETKRHLCM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL----------- 338
Cdd:cd05609   78 VMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLskiglmslttn 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 ---------ACDFSKKKphaSVGTHGYMAPEV-LQKGtaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLT 408
Cdd:cd05609  158 lyeghiekdTREFLDKQ---VCGTPEYIAPEViLRQG--YGKPVDWWAMGIILYEFLVGCVPFFGDTPE---ELFGQVIS 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 409 VNVELP---DTFSPELKSLLEGLLQRDVSKRLGChgGGSQEVKEHSFFKGVDW 458
Cdd:cd05609  230 DEIEWPegdDALPDDAQDLITRLLQQNPLERLGT--GGAEEVKQHPFFQDLDW 280
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
197-451 1.42e-45

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: 161.67  E-value: 1.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKE--KLKKLLEELLREiEILKKL----NHPNIVKLYDVFETENFLYLVMEYCE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLH-YHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV--- 351
Cdd:cd00180   75 GGSLKdLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTtgg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLlrghspfrqhktkdkheidrmtltvnvelpdtfsPELKSLLEGLLQR 431
Cdd:cd00180  155 TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRRMLQY 200
                        250       260
                 ....*....|....*....|
gi 148539879 432 DVSKRLGChgggsQEVKEHS 451
Cdd:cd00180  201 DPKKRPSA-----KELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
191-436 1.22e-44

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: 160.44  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNE-RIMLSLvstgDCPFIVcMTYAFHTPDKLCF 269
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREaRALARL----SHPNIV-RVYDVGEDDGRPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 I-LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF---SKK 345
Cdd:cd14014   77 IvMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALgdsGLT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd14014  157 QTGSVLGTPAYMAPEQAR-GGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAI 235
                        250
                 ....*....|..
gi 148539879 425 LEGLLQRDVSKR 436
Cdd:cd14014  236 ILRALAKDPEER 247
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
190-453 7.53e-44

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: 158.10  E-value: 7.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:cd14099    2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKQREKLKSEIKIHRSL----KHPNIVKFHDCFEDEENVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC----DFSK 344
Cdd:cd14099   78 ILLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAArleyDGER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKphASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDT--FSPELK 422
Cdd:cd14099  158 KK--TLCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPF---ETSDVKETYKRIKKNEYSFPSHlsISDEAK 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148539879 423 SLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14099  233 DLIRSMLQPDPTKRPSL-----DEILSHPFF 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
191-436 9.18e-44

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.42  E-value: 9.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNE-RIMLSLVStgdcPFIVcMTYAFHTPDKLCF 269
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREaRALARLNH----PNIV-RVYDVGEEDGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 I-LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK---K 345
Cdd:COG0515   84 LvMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGatlT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTF----SPEL 421
Cdd:COG0515  164 QTGTVVGTPGYMAPEQAR-GEPVDPRSDVYSLGVTLYELLTGRPPFD---GDSPAELLRAHLREPPPPPSELrpdlPPAL 239
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:COG0515  240 DAIVLRALAKDPEER 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
195-436 2.98e-43

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: 156.47  E-value: 2.98e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEtLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd08215    6 RVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKERE-EALNEvKLLSKL----KHPNIVKYYESFEENGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGV----FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd08215   81 ADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 S--VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVE-LPDTFSPELKSLLE 426
Cdd:cd08215  161 KtvVGTPYYLSPELCE-NKPYNYKSDIWALGCVLYELCTLKHPF---EANNLPALVYKIVKGQYPpIPSQYSSELRDLVN 236
                        250
                 ....*....|
gi 148539879 427 GLLQRDVSKR 436
Cdd:cd08215  237 SMLQKDPEKR 246
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
188-490 2.56e-41

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: 154.45  E-value: 2.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERimlSLVSTGDCPFIVCMTYAFHTPDKL 267
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAER---DILVEADGAWVVKMFYSFQDKRNL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-------- 339
Cdd:cd05627   78 YLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglkkahr 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 ------------CDF------SKKK-----------PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSP 390
Cdd:cd05627  158 tefyrnlthnppSDFsfqnmnSKRKaetwkknrrqlAYSTVGTPDYIAPEVFMQ-TGYNKLCDWWSLGVIMYEMLIGYPP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 391 FRQHKTKDKHEID---RMTLTVNVELPdtFSPELKSLLEGLLQrDVSKRLGchGGGSQEVKEHSFFKGVDWQHVylqKYP 467
Cdd:cd05627  237 FCSETPQETYRKVmnwKETLVFPPEVP--ISEKAKDLILRFCT-DAENRIG--SNGVEEIKSHPFFEGVDWEHI---RER 308
                        330       340
                 ....*....|....*....|...
gi 148539879 468 PPLIPPrgEVNAADafDIGSFDE 490
Cdd:cd05627  309 PAAIPI--EIKSID--DTSNFDD 327
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
190-453 3.55e-41

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: 150.82  E-value: 3.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKIN---LESKEKKESILNEIAILKKCKH---PNIVKYYGSYLKKDELWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd05122   75 VMEFCSGGSLKDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 AS-VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQ-HKTKdkheidRMTLTVNV---ELPD--TFSPEL 421
Cdd:cd05122  155 NTfVGTPYWMAPEVIQ-GKPYGFKADIWSLGITAIEMAEGKPPYSElPPMK------ALFLIATNgppGLRNpkKWSKEF 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 422 KSLLEGLLQRDVSKRlgchgGGSQEVKEHSFF 453
Cdd:cd05122  228 KDFLKKCLQKDPEKR-----PTAEQLLKHPFI 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
197-453 1.82e-40

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: 149.24  E-value: 1.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKR-IKMKQGETLALNERIMLSLVSTG-------DCPFIVCMTYAFHTP--DK 266
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRlRKRREGKNDRGKIKNALDDVRREiaimkklDHPNIVRLYEVIDDPesDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd14008   81 LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPH--ASVGTHGYMAPEVLQKG-TAYDSSA-DWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVEL--PDTFS 418
Cdd:cd14008  161 GNDTlqKTAGTPAFLAPELCDGDsKTYSGKAaDIWALGVTLYCLVFGRLPF---NGDNILELYEAIQNQNDEFpiPPELS 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148539879 419 PELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd14008  238 PELKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
184-495 1.82e-40

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: 152.46  E-value: 1.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 184 IHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstGDCPFIVCMTYAFHT 263
Cdd:cd05621   47 LQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAF---ANSPWVVQLFCAFQD 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS 343
Cdd:cd05621  124 DKYLYMVMEYMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMD 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KK---KPHASVGTHGYMAPEVL--QKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQHK-----TKDKHEIDRMTLTVNVE 412
Cdd:cd05621  203 ETgmvHCDTAVGTPDYISPEVLksQGGDGyYGRECDWWSVGVFLFEMLVGDTPFYADSlvgtySKIMDHKNSLNFPDDVE 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 413 LpdtfSPELKSLLEGLLQrDVSKRLGchGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDE-E 491
Cdd:cd05621  283 I----SKHAKNLICAFLT-DREVRLG--RNGVEEIKQHPFFRNDQWNWDNIRETAAPVVP-----ELSSDIDTSNFDDiE 350

                 ....
gi 148539879 492 DTKG 495
Cdd:cd05621  351 DDKG 354
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
183-495 2.55e-40

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: 152.85  E-value: 2.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 183 NIHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFH 262
Cdd:cd05622   67 DLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANS---PWVVQLFYAFQ 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCFILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd05622  144 DDRYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKK---KPHASVGTHGYMAPEVL--QKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQHK---TKDKHEIDRMTLTvnveL 413
Cdd:cd05622  223 NKEgmvRCDTAVGTPDYISPEVLksQGGDGyYGRECDWWSVGVFLYEMLVGDTPFYADSlvgTYSKIMNHKNSLT----F 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 414 PD--TFSPELKSLLEGLLQrDVSKRLGchGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPprgevNAADAFDIGSFDE- 490
Cdd:cd05622  299 PDdnDISKEAKNLICAFLT-DREVRLG--RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVP-----DLSSDIDTSNFDDl 370

                 ....*
gi 148539879 491 EDTKG 495
Cdd:cd05622  371 EEDKG 375
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
187-493 3.86e-40

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: 150.80  E-value: 3.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDK 266
Cdd:cd05610    2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKS---PFIVHLYYSLQSANN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA------- 339
Cdd:cd05610   79 VYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnre 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 --------------------------------CDFSKKKPHAS----------------VGTHGYMAPEVLQkGTAYDSS 371
Cdd:cd05610  159 lnmmdilttpsmakpkndysrtpgqvlslissLGFNTPTPYRTpksvrrgaarvegeriLGTPDYLAPELLL-GKPHGPA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 372 ADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTVNVELPD---TFSPELKSLLEGLLQRDVSKRlgchgGGSQEVK 448
Cdd:cd05610  238 VDWWALGVCLFEFLTGIPPFNDETPQ---QVFQNILNRDIPWPEgeeELSVNAQNAIEILLTMDPTKR-----AGLKELK 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 148539879 449 EHSFFKGVDWQHvyLQKYPPPLIPprgevNAADAFDIGSFDEEDT 493
Cdd:cd05610  310 QHPLFHGVDWEN--LQNQTMPFIP-----QPDDETDTSYFEARNN 347
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
195-495 4.29e-40

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: 151.32  E-value: 4.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05626    7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILA---EADNEWVVKLYYSFQDKDNLYFVMDYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF------------ 342
Cdd:cd05626   84 PGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthnskyyqkg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 --------------------------------SKKK-----PHASVGTHGYMAPEV-LQKGtaYDSSADWFSLGCMLFKL 384
Cdd:cd05626  164 shirqdsmepsdlwddvsncrcgdrlktleqrATKQhqrclAHSLVGTPNYIAPEVlLRKG--YTQLCDWWSVGVILFEM 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 385 LRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLeGLLQRDVSKRLGchGGGSQEVKEHSFFKGVDWQhVYL 463
Cdd:cd05626  242 LVGQPPFlAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLI-TKLCCSAEERLG--RNGADDIKAHPFFSEVDFS-SDI 317
                        330       340       350
                 ....*....|....*....|....*....|..
gi 148539879 464 QKYPPPLIPprgevNAADAFDIGSFDEEDTKG 495
Cdd:cd05626  318 RTQPAPYVP-----KISHPMDTSNFDPVEEES 344
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
195-437 6.93e-40

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: 147.17  E-value: 6.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERI-MLSLVstgDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14663    6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVA-REGMVEQIKREIaIMKLL---RHPNIVELHEVMATKTKIFFVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP----HA 349
Cdd:cd14663   82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQdgllHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVL-QKGtaYD-SSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDTFSPELKSLLEG 427
Cdd:cd14663  162 TCGTPNYVAPEVLaRRG--YDgAKADIWSCGVILFVLLAGYLPFDD---ENLMALYRKIMKGEFEYPRWFSPGAKSLIKR 236
                        250
                 ....*....|
gi 148539879 428 LLQRDVSKRL 437
Cdd:cd14663  237 ILDPNPSTRI 246
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
189-452 8.75e-40

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: 146.63  E-value: 8.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKL----NHPNIIEMLDSFETKKEFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKkkpH 348
Cdd:cd14002   77 VVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSC---N 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASV-----GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKS 423
Cdd:cd14002  153 TLVltsikGTPLYMAPELVQE-QPYDHTADLWSLGCILYELFVGQPPF---YTNSIYQLVQMIVKDPVKWPSNMSPEFKS 228
                        250       260
                 ....*....|....*....|....*....
gi 148539879 424 LLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14002  229 FLQGLLNKDPSKRLSW-----PDLLEHPF 252
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
184-492 1.32e-39

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: 150.94  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 184 IHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkMKQGETLALNERimLSLVSTGDCPFIVCMTYAFHT 263
Cdd:cd05623   67 MRLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEM-LKRAETACFREE--RDVLVNGDSQWITTLHYAFQD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFILDLMNGGDLHYHLSQ-HGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd05623  144 DNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKL 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKK---KPHASVGTHGYMAPEVLQ-----KGTaYDSSADWFSLGCMLFKLLRGHSPFRQH---KTKDKHEIDRMTLTVNV 411
Cdd:cd05623  224 MEDgtvQSSVAVGTPDYISPEILQamedgKGK-YGPECDWWSLGVCMYEMLYGETPFYAEslvETYGKIMNHKERFQFPT 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 412 ELPDTfSPELKSLLEGLL-QRDvsKRLGchGGGSQEVKEHSFFKGVDWQHVylQKYPPPLIPprgEVNAADafDIGSFDE 490
Cdd:cd05623  303 QVTDV-SENAKDLIRRLIcSRE--HRLG--QNGIEDFKNHPFFVGIDWDNI--RNCEAPYIP---EVSSPT--DTSNFDV 370

                 ..
gi 148539879 491 ED 492
Cdd:cd05623  371 DD 372
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
190-437 1.85e-39

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: 145.93  E-value: 1.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGK--EHMIENEVAILRRV---KHPNIVQLIEEYDTDTELYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS----DLGLACDFskK 345
Cdd:cd14095   76 VMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSlklaDFGLATEV--K 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtKDKHEIDRMTLTVNVELP----DTFSPE 420
Cdd:cd14095  154 EPLFTVcGTPTYVAPEILAE-TGYGLKVDIWAAGVITYILLCGFPPFRSPD-RDQEELFDLILAGEFEFLspywDNISDS 231
                        250
                 ....*....|....*..
gi 148539879 421 LKSLLEGLLQRDVSKRL 437
Cdd:cd14095  232 AKDLISRMLVVDPEKRY 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
197-457 1.16e-38

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: 143.89  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGET---LALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd06623    9 LGQGSSGVVYKVRHKPTGKIYALK-----KIHVDGDEEfrkQLLRE---LKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHN-RFVVYRDLKPANILLDEHGHARISDLGLACDFSK-KKPHAS- 350
Cdd:cd06623   81 MDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENtLDQCNTf 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIdrMTLTVNVELP----DTFSPELKSLLE 426
Cdd:cd06623  161 VGTVTYMSPERIQ-GESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFEL--MQAICDGPPPslpaEEFSPEFRDFIS 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148539879 427 GLLQRDVSKRLGCHgggsqEVKEHSFFKGVD 457
Cdd:cd06623  238 ACLQKDPKKRPSAA-----ELLQHPFIKKAD 263
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
190-490 3.58e-38

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: 145.95  E-value: 3.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERimlSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAER---DILVEADSLWVVKMFYSFQDKLNLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA---------- 339
Cdd:cd05628   79 IMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCtglkkahrte 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 ----------CDF------SKKKPH-----------ASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd05628  159 fyrnlnhslpSDFtfqnmnSKRKAEtwkrnrrqlafSTVGTPDYIAPEVFMQ-TGYNKLCDWWSLGVIMYEMLIGYPPFC 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 393 QHKTKDKHEidrmtLTVNVELPDTFSPELKSLLEGllqRDVSKRLGCHG------GGSQEVKEHSFFKGVDWQHVylqKY 466
Cdd:cd05628  238 SETPQETYK-----KVMNWKETLIFPPEVPISEKA---KDLILRFCCEWehrigaPGVEEIKTNPFFEGVDWEHI---RE 306
                        330       340
                 ....*....|....*....|....
gi 148539879 467 PPPLIPPrgEVNAADafDIGSFDE 490
Cdd:cd05628  307 RPAAIPI--EIKSID--DTSNFDE 326
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
195-472 3.80e-38

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: 145.96  E-value: 3.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERimlSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd05625    7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAER---DILAEADNEWVVRLYYSFQDKDNLYFVMDYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL---------------- 338
Cdd:cd05625   84 PGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqsg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 ------ACDFSKK-------------KP--------------HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLL 385
Cdd:cd05625  164 dhlrqdSMDFSNEwgdpencrcgdrlKPlerraarqhqrclaHSLVGTPNYIAPEVLLR-TGYTQLCDWWSVGVILFEML 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 386 RGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLqRDVSKRLGchGGGSQEVKEHSFFKGVDWQHvYLQ 464
Cdd:cd05625  243 VGQPPFlAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLG--KNGADEIKAHPFFKTIDFSS-DLR 318

                 ....*...
gi 148539879 465 KYPPPLIP 472
Cdd:cd05625  319 QQSAPYIP 326
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
190-436 5.37e-38

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: 141.59  E-value: 5.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGETLALNERImlSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQI--SLEKIPKSDLKSVMGEI--DLLKKLNHPNIVKYIGSVKTKDSLYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC--DFSKKKP 347
Cdd:cd06627   77 ILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATklNEVEKDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLQKGTAYDSSADWfSLGCMLFKLLRGHSPFrqhktkdkHEIDRM-TLTVNVE-----LPDTFSPEL 421
Cdd:cd06627  157 NSVVGTPYWMAPEVIEMSGVTTASDIW-SVGCTVIELLTGNPPY--------YDLQPMaALFRIVQddhppLPENISPEL 227
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:cd06627  228 RDFLLQCFQKDPTLR 242
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
191-439 9.86e-38

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: 140.99  E-value: 9.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNE-RIMLSLVStgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKERED-SVNEiRLLASVNH----PNIIRYKEAFLDGNRLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHG----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd08530   77 VMEYAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD-KHEIDRMTLTvnvELPDTFSPELKSL 424
Cdd:cd08530  157 LAKTQIGTPLYAAPEVW-KGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQElRYKVCRGKFP---PIPPVYSQDLQQI 232
                        250
                 ....*....|....*
gi 148539879 425 LEGLLQRDVSKRLGC 439
Cdd:cd08530  233 IRSLLQVNPKKRPSC 247
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
197-452 7.55e-37

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: 138.97  E-value: 7.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMkqgetlaLNE-RIMLSLvstgDCPFIVcmtyAFH----TPDKLCFI 270
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKsKRPEV-------LNEvRLTHEL----KHPNVL----KFYewyeTSNHLWLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC---------- 340
Cdd:cd14010   73 VEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelf 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 341 --------DFSKKKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDkhEIDRMTLT---- 408
Cdd:cd14010  153 gqfsdegnVNKVSKKQAKRGTPYYMAPELFQGGV-HSFASDLWALGCVLYEMFTGKPPF-VAESFT--ELVEKILNedpp 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148539879 409 -VNVELPDTFSPELKSLLEGLLQRDVSKRLGCHgggsqEVKEHSF 452
Cdd:cd14010  229 pPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWD-----ELVKHPF 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
197-436 1.51e-36

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: 137.28  E-value: 1.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVY-G-CRkadtGKMYAMKCLDKKRikmKQGETLA--LNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd13999    1 IGSGSFGEVYkGkWR----GTDVAIKKLKVED---DNDELLKefRREVSILSKLRH---PNIVQFIGACLSPPPLCIVTE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHL-SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH--A 349
Cdd:cd13999   71 YMPGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKmtG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRqhktkdkhEIDRMTLTVNV-------ELPDTFSPELK 422
Cdd:cd13999  151 VVGTPRWMAPEVLRGEP-YTEKADVYSFGIVLWELLTGEVPFK--------ELSPIQIAAAVvqkglrpPIPPDCPPELS 221
                        250
                 ....*....|....
gi 148539879 423 SLLEGLLQRDVSKR 436
Cdd:cd13999  222 KLIKRCWNEDPEKR 235
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
197-438 7.92e-36

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: 135.43  E-value: 7.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLaLNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENL-ESEIAILKSI---KHPNIVRLYDVQKTEDFIYLVLEYCAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGlacdFSKKKPHASV-- 351
Cdd:cd14009   77 GDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFG----FARSLQPASMae 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 ---GTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEG 427
Cdd:cd14009  153 tlcGSPLYMAPEILQ-FQKYDAKADLWSVGAILFEMLVGKPPFRgSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRR 231
                        250
                 ....*....|.
gi 148539879 428 LLQRDVSKRLG 438
Cdd:cd14009  232 LLRRDPAERIS 242
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
195-452 6.08e-35

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: 133.30  E-value: 6.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL-----DKKRIK-MKQgetlaLNERImlSLVSTGDCPFIVCMTYAFHTPDKLC 268
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVslvddDKKSREsVKQ-----LEQEI--ALLSKLRHPNIVQYYGTEREEDNLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd06632   79 IFLEYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASV-GTHGYMAPEVL-QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQH----------KTKDKHEIdrmtltvnvelPDT 416
Cdd:cd06632  159 KSFkGSPYWMAPEVImQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYegvaaifkigNSGELPPI-----------PDH 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148539879 417 FSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd06632  228 LSPDAKDFIRLCLQRDPEDRPTA-----SQLLEHPF 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
195-453 9.44e-35

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: 132.76  E-value: 9.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14081    7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLI---EHPNVLKLYDVYENKKYLYLVLEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC-DFSKKKPHASVGT 353
Cdd:cd14081   84 SGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASlQPEGSLLETSCGS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLqKGTAYD-SSADWFSLGCMLFKLLRGHSPFrqhktkDKHEIDRMTLTVNV---ELPDTFSPELKSLLEGLL 429
Cdd:cd14081  164 PHYACPEVI-KGEKYDgRKADIWSCGVILYALLVGALPF------DDDNLRQLLEKVKRgvfHIPHFISPDAQDLLRRML 236
                        250       260
                 ....*....|....*....|....
gi 148539879 430 QRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:cd14081  237 EVNPEKRITIE-----EIKKHPWF 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
190-436 1.10e-34

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: 132.78  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQgetlalneriMLSLVSTGDC------------PFIVCM 257
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALK-----KVQIFE----------MMDAKARQDClkeidllqqlnhPNIIKY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 258 TYAFHTPDKLCFILDLMNGGDLHY---HLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARI 333
Cdd:cd08224   66 LASFIENNELNIVLELADAGDLSRlikHFKKQKRlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 334 SDLGLACDFSKK--KPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdkheIDRMTLTVNV 411
Cdd:cd08224  146 GDLGLGRFFSSKttAAHSLVGTPYYMSPERI-REQGYDFKSDIWSLGCLLYEMAALQSPFYGEK------MNLYSLCKKI 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 412 E------LP-DTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd08224  219 EkceyppLPaDLYSQELRDLVAACIQPDPEKR 250
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
197-436 1.98e-34

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: 131.92  E-value: 1.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVY--GCRKADTGKMYAMKCLDKKRIKMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14080    8 IGEGSYSKVKlaEYTKSGLKEKVACKIIDKKKAPKDFLEKFLPRE---LEILRKLRHPNIIQVYSIFERGSKVFIFMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS---- 350
Cdd:cd14080   85 EHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVLsktf 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEVLQkGTAYDS-SADWFSLGCMLFKLLRGHSPFRQHKTKDKHEiDRMTLTVNV-ELPDTFSPELKSLLEGL 428
Cdd:cd14080  165 CGSAAYAAPEILQ-GIPYDPkKYDIWSLGVILYIMLCGSMPFDDSNIKKMLK-DQQNRKVRFpSSVKKLSPECKDLIDQL 242

                 ....*...
gi 148539879 429 LQRDVSKR 436
Cdd:cd14080  243 LEPDPTKR 250
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
195-453 6.43e-34

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: 130.55  E-value: 6.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI--KMKQgETLALNERImlSLVSTGDCPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPIntEASK-EVKALECEI--QLLKNLQHERIVQYYGCLQDEKSLSIFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA------CdfSKKK 346
Cdd:cd06625   83 YMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASkrlqtiC--SSTG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRM-------TLTVNVELPDTFSP 419
Cdd:cd06625  161 MKSVTGTPYWMSPEVI-NGEGYGRKADIWSVGCTVVEMLTTKPPW--------AEFEPMaaifkiaTQPTNPQLPPHVSE 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 420 ELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFF 453
Cdd:cd06625  232 DARDFLSLIFVRNKKQR-----PSAEELLSHSFV 260
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
194-437 7.94e-34

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: 130.55  E-value: 7.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 194 HRIIGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGETLALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14106   13 STPLGRGKFAVVRKCIHKETGKEYAAKFL-RKRRRGQDCRNEILHEIAVLELCK--DCPRVVNLHEVYETRSELILILEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLACDFSKK-KPHA 349
Cdd:cd14106   90 AAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVIGEGeEIRE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQkgtaYDS---SADWFSLGCMLFKLLRGHSPFrqhKTKDKHE----IDRMTLTVNVELPDTFSPELK 422
Cdd:cd14106  170 ILGTPDYVAPEILS----YEPislATDMWSIGVLTYVLLTGHSPF---GGDDKQEtflnISQCNLDFPEELFKDVSPLAI 242
                        250
                 ....*....|....*
gi 148539879 423 SLLEGLLQRDVSKRL 437
Cdd:cd14106  243 DFIKRLLVKDPEKRL 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
190-436 3.56e-33

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: 128.36  E-value: 3.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNE--RIMLSLvstgDCPFIVCMTYAFHTPDKL 267
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQReiNILKSL----EHPGIVRLIDWYEDDQHI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG--HARISDLGLAcdfskK 345
Cdd:cd14098   77 YLVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLA-----K 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHAS------VGTHGYMAPEVL-QKGTA----YDSSADWFSLGCMLFKLLRGHSPFRQhKTKDKHE--IDRMTLTVNVE 412
Cdd:cd14098  152 VIHTGtflvtfCGTMAYLAPEILmSKEQNlqggYSNLVDMWSVGCLVYVMLTGALPFDG-SSQLPVEkrIRKGRYTQPPL 230
                        250       260
                 ....*....|....*....|....
gi 148539879 413 LPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14098  231 VDFNISEEAIDFILRLLDVDPEKR 254
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
191-453 3.64e-33

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: 128.12  E-value: 3.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQGE---TLALNE-RIMLSLVSTGDCPFIVCMTYAFHTP-- 264
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIK-------KIKNDFrhpKAALREiKLLKHLNDVEGHPNIVKLLDVFEHRgg 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMnGGDLhYHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLACD 341
Cdd:cd05118   74 NHLCLVFELM-GMNL-YELIKDypRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGhspfrQHKTKDKHEIDRMTLTVNVelpdTFSPEL 421
Cdd:cd05118  152 FTSPPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTG-----RPLFPGDSEVDQLAKIVRL----LGTPEA 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 422 KSLLEGLLQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:cd05118  223 LDLLSKMLKYDPAKRITAS-----QALAHPYF 249
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
196-451 7.46e-33

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: 127.86  E-value: 7.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK---------------QGETLALNERIM--LSLVSTGDCPFIVCMT 258
Cdd:cd14118    1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQagffrrppprrkpgaLGKPLDPLDRVYreIAILKKLDHPNVVKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 259 YAFHTP--DKLCFILDLMNGGDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDL 336
Cdd:cd14118   81 EVLDDPneDNLYMVFELVDKGAV-MEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 337 GLACDF--SKKKPHASVGTHGYMAPEVLQKGTAYDS--SADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRmtlTVNVE 412
Cdd:cd14118  160 GVSNEFegDDALLSSTAGTPAFMAPEALSESRKKFSgkALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIK---TDPVV 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 148539879 413 LPD--TFSPELKSLLEGLLQRDVSKRLGCHgggsqEVKEHS 451
Cdd:cd14118  237 FPDdpVVSEQLKDLILRMLDKNPSERITLP-----EIKEHP 272
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
197-454 1.13e-32

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: 126.56  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKM-KQGETLALNE-RIMLSLVStgdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06614    8 IGEGASGEVYKATDRATGKEVAIK-----KMRLrKQNKELIINEiLIMKECKH----PNIVDYYDSYLVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS--V 351
Cdd:cd06614   79 DGGSLTDIITQNPVrMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNsvV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPF---------RQHKTKDKHEIDRmtltvnvelPDTFSPELK 422
Cdd:cd06614  159 GTPYWMAPEVI-KRKDYGPKVDIWSLGIMCIEMAEGEPPYleepplralFLITTKGIPPLKN---------PEKWSPEFK 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 423 SLLEGLLQRDVSKRLGChgggsQEVKEHSFFK 454
Cdd:cd06614  229 DFLNKCLVKDPEKRPSA-----EELLQHPFLK 255
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
190-436 3.68e-32

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: 125.22  E-value: 3.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREE-AIDEARVLSKL---NSPYVIKYYDSFVDKGKLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHL-SQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP 347
Cdd:cd08529   77 VMEYAENGDLHSLIkSQRGrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HAS--VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHktKDKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd08529  157 FAQtiVGTPYYLSPELCE-DKPYNEKSDVWALGCVLYELCTGKHPFEAQ--NQGALILKIVRGKYPPISASYSQDLSQLI 233
                        250
                 ....*....|.
gi 148539879 426 EGLLQRDVSKR 436
Cdd:cd08529  234 DSCLTKDYRQR 244
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
197-437 8.57e-32

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: 123.92  E-value: 8.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmkQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD----KKKEAVLREiSILNQL----QHPRIIQLHEAYESPTELVLILELCS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG--HARISDLGLACDFSKKKP-HASVG 352
Cdd:cd14006   73 GGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKLNPGEElKEIFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVEL----PDTFSPELKSLLEGL 428
Cdd:cd14006  153 TPEFVAPEIVN-GEPVSLATDMWSIGVLTYVLLSGLSPFL---GEDDQETLANISACRVDFseeyFSSVSQEAKDFIRKL 228

                 ....*....
gi 148539879 429 LQRDVSKRL 437
Cdd:cd14006  229 LVKEPRKRP 237
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
189-454 2.11e-31

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: 123.22  E-value: 2.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQGETLALNERIM--LSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVK-------VIRLEIDEALQKQILreLDVLHKCNSPYIVGFYGAFYSEGD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHN-RFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd06605   74 ISICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI-DRMTLTVNVELP----DTFSPE 420
Cdd:cd06605  154 LAKTFVGTRSYMAPERIS-GGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIfELLSYIVDEPPPllpsGKFSPD 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 421 LKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd06605  233 FQDFVSQCLQKDPTER-----PSYKELMEHPFIK 261
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
195-453 3.33e-31

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: 122.73  E-value: 3.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNE---IELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC--DFSKKKPHASVG 352
Cdd:cd14189   84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAArlEPPEQRKKTICG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd14189  164 TPNYLAPEVLLR-QGHGPESDVWSLGCVMYTLLCGNPPF---ETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRN 239
                        250       260
                 ....*....|....*....|.
gi 148539879 433 VSKRLGChgggsQEVKEHSFF 453
Cdd:cd14189  240 PGDRLTL-----DQILEHEFF 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
189-454 5.99e-31

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: 122.35  E-value: 5.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLD----KKRIKMKQGEtlalnerimLSLVSTGDCPFIVCMTYAFHTP 264
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleeaEDEIEDIQQE---------IQFLSQCDSPYITKYYGSFLKG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA--CDF 342
Cdd:cd06609   72 SKLWIIMEYCGGGSV-LDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSgqLTS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASVGTHGYMAPEVLQKGtAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNVELP----DTFS 418
Cdd:cd06609  151 TMSKRNTFVGTPFWMAPEVIKQS-GYDEKADIWSLGITAIELAKGEPPL-----SDLHPMRVLFLIPKNNPPslegNKFS 224
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148539879 419 PELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFFK 454
Cdd:cd06609  225 KPFKDFVELCLNKDPKERPSA-----KELLKHKFIK 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
190-437 6.97e-31

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: 122.12  E-value: 6.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLA-----LNE-RIMLSLvstgDCPFIVCMTYAFHT 263
Cdd:cd14084    7 KYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREINkprniETEiEILKKL----SHPCIIKIEDFFDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLac 340
Cdd:cd14084   83 EDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGL-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 341 dfSKKKPHASV-----GTHGYMAPEVLQKG--TAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD--KHEIDRMTLTVNV 411
Cdd:cd14084  161 --SKILGETSLmktlcGTPTYLAPEVLRSFgtEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMslKEQILSGKYTFIP 238
                        250       260
                 ....*....|....*....|....*.
gi 148539879 412 ELPDTFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14084  239 KAWKNVSEEAKDLVKKMLVVDPSRRP 264
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
196-453 1.82e-30

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: 120.92  E-value: 1.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIM-----LSLVSTGdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14093   10 ILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEELREATRreieiLRQVSGH--PNIIELHDVFESPTFIFLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK-KKPHA 349
Cdd:cd14093   88 FELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEgEKLRE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKGT-----AYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdKHEIDRMTLTVNVELP----DTFSPE 420
Cdd:cd14093  168 LCGTPGYLAPEVLKCSMydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRK---QMVMLRNIMEGKYEFGspewDDISDT 244
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148539879 421 LKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd14093  245 AKDLISKLLVVDPKKRL-----TAEEALEHPFF 272
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
189-437 4.12e-30

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: 120.60  E-value: 4.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLL----KHPNIVRLHDSISEEGFHY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLACDFSKK 345
Cdd:cd14086   77 LVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KP--HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELP----DTFSP 419
Cdd:cd14086  157 QQawFGFAGTPGYLSPEVLRK-DPYGKPVDIWACGVILYILLVGYPPFWD---EDQHRLYAQIKAGAYDYPspewDTVTP 232
                        250
                 ....*....|....*...
gi 148539879 420 ELKSLLEGLLQRDVSKRL 437
Cdd:cd14086  233 EAKDLINQMLTVNPAKRI 250
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
189-437 6.36e-30

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: 118.97  E-value: 6.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLAlNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIK-KEVCIQKMLSH---KNVVRFYGHRREGEFQY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP- 347
Cdd:cd14069   77 LFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKe 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 ---HASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP-DTFSPELKS 423
Cdd:cd14069  157 rllNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTYLTPwKKIDTAALS 236
                        250
                 ....*....|....
gi 148539879 424 LLEGLLQRDVSKRL 437
Cdd:cd14069  237 LLRKILTENPNKRI 250
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
191-452 6.50e-30

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: 118.90  E-value: 6.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNE-RIMLSLVStgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGK--EDMIESEiLIIKSLSH----PNIVKLFEVYETEKEIYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL----DEHGHARISDLGLACDFSkk 345
Cdd:cd14185   76 ILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASV-GTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtKDKHEIDRMTLTVNVE-LP---DTFSPE 420
Cdd:cd14185  154 GPIFTVcGTPTYVAPEILS-EKGYGLEVDMWAAGVILYILLCGFPPFRSPE-RDQEELFQIIQLGHYEfLPpywDNISEA 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 421 LKSLLEGLLQRDVSKRLGCHgggsqEVKEHSF 452
Cdd:cd14185  232 AKDLISRLLVVDPEKRYTAK-----QVLQHPW 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
196-453 7.29e-30

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: 119.31  E-value: 7.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLD--KKRIKMKQGETL---ALNERIMLSLVSTGdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14181   17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEvtAERLSPEQLEEVrssTLKEIHILRQVSGH--PSIITLIDSYESSTFIFLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS-KKKPHA 349
Cdd:cd14181   95 FDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEpGEKLRE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVL-----QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdKHEIDRMTLTVNVELP----DTFSPE 420
Cdd:cd14181  175 LCGTPGYLAPEILkcsmdETHPGYGKEVDLWACGVILFTLLAGSPPFWHRR---QMLMLRMIMEGRYQFSspewDDRSST 251
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148539879 421 LKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd14181  252 VKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
190-492 1.56e-29

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 120.08  E-value: 1.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCR-KADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:PTZ00426  31 DFNFIRTLGTGSFGRVILATyKNEDFPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINH---PFCVNLYGSFKDESYLY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSKKKPH 348
Cdd:PTZ00426 108 LVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA-KVVDTRTY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:PTZ00426 187 TLCGTPEYIAPEILLN-VGHGKAADWWTLGIFIYEILVGCPPFY---ANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKL 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 429 LQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVnaadaFDIGSFD--EED 492
Cdd:PTZ00426 263 LSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNV-----FDSSNFErvQED 323
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
195-436 1.57e-29

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: 117.90  E-value: 1.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMlSLVSTgdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14074    9 ETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCM-KLVQH---PNVVRLYEVIDTQTKLYLILELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE-HGHARISDLGLACDFSK-KKPHASV 351
Cdd:cd14074   85 DGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSNKFQPgEKLETSC 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQkGTAYDSSA-DWFSLGCMLFKLLRGHSPFRQhkTKDKhEIDRMTLTVNVELPDTFSPELKSLLEGLLQ 430
Cdd:cd14074  165 GSLAYSAPEILL-GDEYDAPAvDIWSLGVILYMLVCGQPPFQE--ANDS-ETLTMIMDCKYTVPAHVSPECKDLIRRMLI 240

                 ....*.
gi 148539879 431 RDVSKR 436
Cdd:cd14074  241 RDPKKR 246
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
197-453 2.11e-29

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: 117.84  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKC--LDKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06610    9 IGSGATAVVYAAYCLPKKEKVAIKRidLEKCQTSMDE----LRKE---IQAMSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLhYHLSQH----GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC------DFSK 344
Cdd:cd06610   82 SGGSL-LDIMKSsyprGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSAslatggDRTR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqHKTKdkhEIDRMTLTVNVELPD--------T 416
Cdd:cd06610  161 KVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPY--SKYP---PMKVLMLTLQNDPPSletgadykK 235
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148539879 417 FSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFF 453
Cdd:cd06610  236 YSKSFRKMISLCLQKDPSKR-----PTAEELLKHKFF 267
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
197-453 2.48e-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: 118.20  E-value: 2.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMK--CLdkkRIKMKQGETLALNEriMLSLVSTGDCPFIVCMTYAFhtPDKLCFIL--D 272
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALKkvAL---RKLEGGIPNQALRE--IKALQACQGHPYVVKLRDVF--PHGTGFVLvfE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMnGGDLH--YHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA- 349
Cdd:cd07832   81 YM-LSSLSevLRDEERP-LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLy 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 --SVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGhSPFRQHKTkdkhEIDRMTLTVNV-------------ELP 414
Cdd:cd07832  159 shQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNG-SPLFPGEN----DIEQLAIVLRTlgtpnektwpeltSLP 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 415 D----TF---------------SPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd07832  234 DynkiTFpeskgirleeifpdcSPEAIDLLKGLLVYNPKKRLSA-----EEALRHPYF 286
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-439 2.51e-29

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: 117.44  E-value: 2.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGK--ETSIENEIAVLHKIKH---PNIVALDDIYESGGHLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL---LDEHGHARISDLGLacdfSKKKP 347
Cdd:cd14167   80 MQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL----SKIEG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASV-----GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPEL 421
Cdd:cd14167  156 SGSVmstacGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFyDENDAKLFEQILKAEYEFDSPYWDDISDSA 234
                        250
                 ....*....|....*...
gi 148539879 422 KSLLEGLLQRDVSKRLGC 439
Cdd:cd14167  235 KDFIQHLMEKDPEKRFTC 252
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
54-174 7.62e-29

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 214613  Cd Length: 118  Bit Score: 111.21  E-value: 7.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879    54 TFDKIFNQKIGFLLFKDFCLNEinEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCsHPFSKQAVEHVQ 133
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESE--FSEENLEFWLAVEEFKKAEDDEERIAKAREIYDKFLSPNAPKE-VNLDSDLREKIE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 148539879   134 SHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRF 174
Cdd:smart00315  78 ENLESEEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-439 2.19e-28

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: 115.47  E-value: 2.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGETLAlNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFI 270
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCI--KKSPLSRDSSLE-NEIAVLKRIKHEN---IVTLEDIYESTTHYYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLacdfSKKKP 347
Cdd:cd14166   79 MQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL----SKMEQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HA----SVGTHGYMAPEVL-QKgtAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPEL 421
Cdd:cd14166  155 NGimstACGTPGYVAPEVLaQK--PYSKAVDCWSIGVITYILLCGYPPFyEETESRLFEKIKEGYYEFESPFWDDISESA 232
                        250
                 ....*....|....*...
gi 148539879 422 KSLLEGLLQRDVSKRLGC 439
Cdd:cd14166  233 KDFIRHLLEKNPSKRYTC 250
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
191-453 2.71e-28

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: 114.26  E-value: 2.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVY-GCRKADtGKMYAMKCLDKKRIK---MKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd14005    2 YEVGDLLGKGGFGTVYsGVRIRD-GLPVAVKFVPKSRVTewaMINGPVPVPLEIALLLKASKPGVPGVIRLLDWYERPDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 lcFILDL---MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLAcDF 342
Cdd:cd14005   81 --FLLIMerpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCG-AL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASV-GTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRqhktkdkHEIDRMTLTVNVelPDTFSPEL 421
Cdd:cd14005  158 LKDSVYTDFdGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFE-------NDEQILRGNVLF--RPRLSKEC 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 422 KSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14005  229 CDLISRCLQFDPSKRPSL-----EQILSHPWF 255
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
195-436 4.00e-28

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: 113.98  E-value: 4.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGE----TLALNERIMLSLVSTGdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd13993    6 SPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNdfqkLPQLREIDLHRRVSRH--PNIITLHDVFETEVAIYIV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHY--HLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH-GHARISDLGLACDfSKKKP 347
Cdd:cd13993   84 LEYCPNGDLFEaiTENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLATT-EKISM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVL----QKGTAYDS-SADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNveLPDTFSP--- 419
Cdd:cd13993  163 DFGVGSEFYMAPECFdevgRSLKGYPCaAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYYLNSPN--LFDVILPmsd 240
                        250
                 ....*....|....*..
gi 148539879 420 ELKSLLEGLLQRDVSKR 436
Cdd:cd13993  241 DFYNLLRQIFTVNPNNR 257
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
187-450 5.64e-28

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: 113.51  E-value: 5.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERIMLSlvSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd14116    3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLE-KAGVEHQLRREVEIQ--SHLRHPNILRLYGYFHDATR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd14116   80 VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd14116  160 RTTLCGTLDYLPPEMIE-GRMHDEKVDLWSLGVLCYEFLVGKPPF---EANTYQETYKRISRVEFTFPDFVTEGARDLIS 235
                        250       260
                 ....*....|....*....|....
gi 148539879 427 GLLQRDVSKRLGChgggsQEVKEH 450
Cdd:cd14116  236 RLLKHNPSQRPML-----REVLEH 254
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
196-455 6.59e-28

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: 114.70  E-value: 6.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALnerimlslvstgdC---PFIVCMTYAFHTPDKLCFILD 272
Cdd:cd14092   13 ALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREVQLLRL-------------CqghPNIVKLHEVFQDELHTYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGlacdFSKKKP-- 347
Cdd:cd14092   80 LLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFG----FARLKPen 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 ---HASVGTHGYMAPEVLQKGTA---YDSSADWFSLGCMLFKLLRGHSPFrQHKTKDKHEIDRMT------LTVNVELPD 415
Cdd:cd14092  156 qplKTPCFTLPYAAPEVLKQALStqgYDESCDLWSLGVILYTMLSGQVPF-QSPSRNESAAEIMKriksgdFSFDGEEWK 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148539879 416 TFSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFFKG 455
Cdd:cd14092  235 NVSSEAKSLIQGLLTVDPSKRLTM-----SELRNHPWLQG 269
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-439 1.54e-27

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: 112.08  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGK--EDSLENEIAVLRKIKH---PNIVQLLDIYESKSHLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL---LDEHGHARISDLGLACDFSKKKP 347
Cdd:cd14083   80 MELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKMEDSGVM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVL-QKGtaYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVEL--P--DTFSPELK 422
Cdd:cd14083  160 STACGTPGYVAPEVLaQKP--YGKAVDCWSIGVISYILLCGYPPFYD---ENDSKLFAQILKAEYEFdsPywDDISDSAK 234
                        250
                 ....*....|....*..
gi 148539879 423 SLLEGLLQRDVSKRLGC 439
Cdd:cd14083  235 DFIRHLMEKDPNKRYTC 251
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
189-436 1.67e-27

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: 112.39  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLalNERIM--LSLVSTGDCPFIVcmtyAFHT--- 263
Cdd:cd13996    6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIK-----KIRLTEKSSA--SEKVLreVKALAKLNHPNIV----RYYTawv 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFI-LDLMNGGDLhYHLSQHGVFSEKEMRFYATE----IILGLEHMHNRFVVYRDLKPANILLDEH-GHARISDLG 337
Cdd:cd13996   75 EEPPLYIqMELCEGGTL-RDWIDRRNSSSKNDRKLALElfkqILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKKPHA----------------SVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLrghSPF-----RQHKT 396
Cdd:cd13996  154 LATSIGNQKRELnnlnnnnngntsnnsvGIGTPLYASPEQL-DGENYNEKADIYSLGIILFEML---HPFktameRSTIL 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 148539879 397 KDKHeidrmtltvNVELPDTFS---PELKSLLEGLLQRDVSKR 436
Cdd:cd13996  230 TDLR---------NGILPESFKakhPKEADLIQSLLSKNPEER 263
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
197-437 2.36e-27

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: 112.34  E-value: 2.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDK-KRikMKQGETlalneRIMLSLvstGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14091    8 IGKGSYSVCKRCIHKATGKEYAVKIIDKsKR--DPSEEI-----EILLRY---GQHPNIITLRDVYDDGNSVYLVTELLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL-DEHGHA---RISDLGLAcdfskKKPHASV 351
Cdd:cd14091   78 GGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDPeslRICDFGFA-----KQLRAEN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 G-------THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI-DRMT---LTVNVELPDTFSPE 420
Cdd:cd14091  153 GllmtpcyTANFVAPEVLKK-QGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVIlARIGsgkIDLSGGNWDHVSDS 231
                        250
                 ....*....|....*..
gi 148539879 421 LKSLLEGLLQRDVSKRL 437
Cdd:cd14091  232 AKDLVRKMLHVDPSQRP 248
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
191-392 2.46e-27

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: 112.19  E-value: 2.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGE-----TlALNE-RIMLSLvstgDCPFIVCMTYAFHTP 264
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK-----KIRLDNEEegipsT-ALREiSLLKEL----KHPNIVKLLDVIHTE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGgDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS 343
Cdd:cd07829   71 NKLYLVFEYCDQ-DLKKYLDKRpGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 344 -KKKPHasvgTHG-----YMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd07829  150 iPLRTY----THEvvtlwYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFP 200
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
195-436 4.08e-27

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: 110.98  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd08220    6 RVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMT-KEERQAALNEVKVLSMLHH---PNIIEYYESFLEDKALMIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH-ARISDLGLACDF-SKKKPHAS 350
Cdd:cd08220   82 PGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILsSKSKAYTV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTvnvELPDTFSPELKSLLEGLL 429
Cdd:cd08220  162 VGTPCYISPELCE-GKPYNQKSDIWALGCVLYELASLKRAFEaANLPALVLKIMRGTFA---PISDRYSEELRHLILSML 237

                 ....*..
gi 148539879 430 QRDVSKR 436
Cdd:cd08220  238 HLDPNKR 244
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
197-453 4.30e-27

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: 110.82  E-value: 4.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmkqgeTLALNERI-----MLSLVSTgdcPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd14079   10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIK-----SLDMEEKIrreiqILKLFRH---PHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC-----DFSKkk 346
Cdd:cd14079   82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNimrdgEFLK-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 phASVGTHGYMAPEVLQkGTAY-DSSADWFSLGCMLFKLLRGHSPFrqhktkDKHEIDrmTLTVNVE-----LPDTFSPE 420
Cdd:cd14079  160 --TSCGSPNYAAPEVIS-GKLYaGPEVDVWSCGVILYALLCGSLPF------DDEHIP--NLFKKIKsgiytIPSHLSPG 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148539879 421 LKSLLEGLLQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:cd14079  229 ARDLIKRMLVVDPLKRITIP-----EIRQHPWF 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
196-439 4.56e-27

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: 110.97  E-value: 4.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14082   10 VLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQ-ESQLRNEVAILQQLSH---PGVVNLECMFETPERVFVVMEKLH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQ-HGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG---HARISDLGLACDFSKKKPHAS- 350
Cdd:cd14082   86 GDMLEMILSSeKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKSFRRSv 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdkhEIDRMTLTVNVELPDT----FSPELKSLLE 426
Cdd:cd14082  166 VGTPAYLAPEVLRN-KGYNRSLDMWSVGVIIYVSLSGTFPFNEDE-----DINDQIQNAAFMYPPNpwkeISPDAIDLIN 239
                        250
                 ....*....|...
gi 148539879 427 GLLQRDVSKRLGC 439
Cdd:cd14082  240 NLLQVKMRKRYSV 252
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
195-436 5.08e-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: 110.70  E-value: 5.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMK-----CLDKKRIKMKQGETLALNERImlSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd06628    6 ALIGSGSFGSVYLGMNASSGELMAVKqvelpSVSAENKDRKKSMLDALQREI--ALLRELQHENIVQYLGSSSDANHLNI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLacdfSKKKPHA 349
Cdd:cd06628   84 FLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGI----SKKLEAN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SV------------GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRqhKTKDKHEIDRMTLTVNVELPDTF 417
Cdd:cd06628  160 SLstknngarpslqGSVFWMAPEVV-KQTSYTRKADIWSLGCLVVEMLTGTHPFP--DCTQMQAIFKIGENASPTIPSNI 236
                        250
                 ....*....|....*....
gi 148539879 418 SPELKSLLEGLLQRDVSKR 436
Cdd:cd06628  237 SSEARDFLEKTFEIDHNKR 255
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
195-436 5.14e-27

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: 110.30  E-value: 5.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14072    6 KTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKIL----NHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK-KKPHASVGT 353
Cdd:cd14072   82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPgNKLDTFCGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQkGTAYDS-SADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd14072  162 PPYAAPELFQ-GKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRE---RVLRGKYRIPFYMSTDCENLLKKFLVLN 237

                 ....
gi 148539879 433 VSKR 436
Cdd:cd14072  238 PSKR 241
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
190-438 6.36e-27

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: 111.19  E-value: 6.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI---------------KMKQGE---TLALNERIM--LSLVSTG 249
Cdd:cd14200    1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgsKAAQGEqakPLAPLERVYqeIAILKKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 250 DCPFIVCMTYAFHTP--DKLCFILDLMNGGDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE 327
Cdd:cd14200   81 DHVNIVKLIEVLDDPaeDNLYMVFDLLRKGPVMEVPSDKP-FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 328 HGHARISDLGLACDFSKKKPHAS--VGTHGYMAPEVLQ-KGTAYDSSA-DWFSLGCMLFKLLRGHSPFrqhktkdkheID 403
Cdd:cd14200  160 DGHVKIADFGVSNQFEGNDALLSstAGTPAFMAPETLSdSGQSFSGKAlDVWAMGVTLYCFVYGKCPF----------ID 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148539879 404 RMTLTVN-------VELPD--TFSPELKSLLEGLLQRDVSKRLG 438
Cdd:cd14200  230 EFILALHnkiknkpVEFPEepEISEELKDLILKMLDKNPETRIT 273
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
197-455 9.75e-27

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: 110.37  E-value: 9.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14169   11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGK--EAMVENEIAVLRRINH---ENIVSLEDIYESPTHLYLAMELVTG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD---EHGHARISDLGLACDFSKKKPHASVGT 353
Cdd:cd14169   86 GELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIEAQGMLSTACGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRD 432
Cdd:cd14169  166 PGYVAPELLEQKP-YGKAVDVWAIGVISYILLCGYPPFyDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRHLLERD 244
                        250       260
                 ....*....|....*....|...
gi 148539879 433 VSKRLGChgggsQEVKEHSFFKG 455
Cdd:cd14169  245 PEKRFTC-----EQALQHPWISG 262
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
190-437 1.21e-26

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: 109.72  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKM-YAMKCLDKKRIKMKQG----ETLALNERIMLSLVSTGDCPFIVCMTYafhtp 264
Cdd:cd14202    3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTllgkEIKILKELKHENIVALYDFQEIANSVY----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 dklcFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR---------ISD 335
Cdd:cd14202   78 ----LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRKsnpnnirikIAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 336 LGLACDFSKKKPHASV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP 414
Cdd:cd14202  154 FGFARYLQNNMMAATLcGSPMYMAPEVIMS-QHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIP 232
                        250       260
                 ....*....|....*....|...
gi 148539879 415 DTFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14202  233 RETSSHLRQLLLGLLQRNQKDRM 255
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
55-174 1.34e-26

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.


Pssm-ID: 459870  Cd Length: 117  Bit Score: 104.62  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   55 FDKIFNQKIGFLLFKDFCLNEINEavPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCSHpFSKQAVEHVQS 134
Cdd:pfam00615   2 FDSLLEDQPGRRLFRQFLESEFSE--ENLEFWLACEEFKKADPDEERLKKAKEIYNEFLAPGSPKEIN-LDSDLREEIRE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 148539879  135 HLsKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRF 174
Cdd:pfam00615  79 NL-EKEPTRDLFDEAQAEVYELMEKDSYPRFLKSPLYLRL 117
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
195-436 1.59e-26

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 109.16  E-value: 1.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   195 RIIGRGGFGEVYGCR----KADTGKMYAMKCLdkKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:smart00219   5 KKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTL--KEDASEQQIEEFLREaRIMRKL----DHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   270 ILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNrPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   349 ASVGTHG---YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFRQHKTKDKHE----IDRMtltvnvELPDTFSPE 420
Cdd:smart00219 159 RKRGGKLpirWMAPESLKEGK-FTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEylknGYRL------PQPPNCPPE 231
                          250
                   ....*....|....*.
gi 148539879   421 LKSLLEGLLQRDVSKR 436
Cdd:smart00219 232 LYDLMLQCWAEDPEDR 247
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
185-454 1.62e-26

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: 109.57  E-value: 1.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERIMLSlvSTGDCPFIVCMTYAFHTP 264
Cdd:cd14117    2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIE-KEGVEHQLRREIEIQ--SHLRHPNILRLYNYFHDR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd14117   79 KRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd14117  159 LRRRTMCGTLDYLPPEMIE-GRTHDEKVDLWCIGVLCYELLVGMPPF---ESASHTETYRRIVKVDLKFPPFLSDGSRDL 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 425 LEGLLQRDVSKRLGCHGggsqeVKEHSFFK 454
Cdd:cd14117  235 ISKLLRYHPSERLPLKG-----VMEHPWVK 259
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
191-391 1.82e-26

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: 109.01  E-value: 1.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREiEIMSSL----NHPHIIRIYEVFENKDKIVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK-PH 348
Cdd:cd14073   79 VMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKlLQ 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148539879 349 ASVGTHGYMAPEVLqKGTAYDS-SADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14073  159 TFCGSPLYASPEIV-NGTPYQGpEVDCWSLGVLLYTLVYGTMPF 201
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
190-437 1.94e-26

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: 108.79  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkmkQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAM---QKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFskKKPH 348
Cdd:cd14186   79 VLEMCHNGEMSRYLKNRKkPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQL--KMPH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 AS----VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKheIDRMTLTvNVELPDTFSPELKSL 424
Cdd:cd14186  157 EKhftmCGTPNYISPEIATR-SAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNT--LNKVVLA-DYEMPAFLSREAQDL 232
                        250
                 ....*....|...
gi 148539879 425 LEGLLQRDVSKRL 437
Cdd:cd14186  233 IHQLLRKNPADRL 245
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-439 1.96e-26

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: 110.14  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFI 270
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHEN---IVALEDIYESPNHLYLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLA-CDFSKKK 346
Cdd:cd14168   87 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSkMEGKGDV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd14168  167 MSTACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQILKADYEFDSPYWDDISDSAKDFI 245
                        250
                 ....*....|....
gi 148539879 426 EGLLQRDVSKRLGC 439
Cdd:cd14168  246 RNLMEKDPNKRYTC 259
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
195-436 2.20e-26

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: 108.79  E-value: 2.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   195 RIIGRGGFGEVYGCR----KADTGKMYAMKCLdkKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCF 269
Cdd:smart00221   5 KKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTL--KEDASEQQIEEFLREaRIMRKL----DHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   270 ILDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP 347
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRpkELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   348 HASVGTHG---YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFRQHKTKDKHEI----DRMtltvnvELPDTFSP 419
Cdd:smart00221 159 YKVKGGKLpirWMAPESLKEGK-FTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYlkkgYRL------PKPPNCPP 231
                          250
                   ....*....|....*..
gi 148539879   420 ELKSLLEGLLQRDVSKR 436
Cdd:smart00221 232 ELYKLMLQCWAEDPEDR 248
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-436 2.23e-26

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: 108.78  E-value: 2.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLaLNE-RIMLSLVStgdcPFIVcmTYAFHTPDK-- 266
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQL-VSEvNILRELKH----PNIV--RYYDRIVDRan 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 --LCFILDLMNGGDL----HYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF-----VVYRDLKPANILLDEHGHARISD 335
Cdd:cd08217   74 ttLYIVMEYCEGGDLaqliKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 336 LGLACDFSKKKPHAS--VGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkheidrmtLTVNV-- 411
Cdd:cd08217  154 FGLARVLSHDSSFAKtyVGTPYYMSPELLNEQS-YDEKSDIWSLGCLIYELCALHPPFQAANQLE--------LAKKIke 224
                        250       260
                 ....*....|....*....|....*....
gi 148539879 412 ----ELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd08217  225 gkfpRIPSRYSSELNEVIKSMLNVDPDKR 253
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
197-437 2.88e-26

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: 108.22  E-value: 2.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVY-GCRKADTGKMYAMKCLDKKRIKMKQG----ETLALNERIMLSLVSTGDCPfivcmtyafHTPDKLCFIL 271
Cdd:cd14120    1 IGHGAFAVVFkGRHRKKPDLPVAIKCITKKNLSKSQNllgkEIKILKELSHENVVALLDCQ---------ETSSSVYLVM 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG---------HARISDLGLAcDF 342
Cdd:cd14120   72 EYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFA-RF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASV--GTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPE 420
Cdd:cd14120  151 LQDGMMAATlcGSPMYMAPEVIM-SLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIPSGTSPA 229
                        250
                 ....*....|....*..
gi 148539879 421 LKSLLEGLLQRDVSKRL 437
Cdd:cd14120  230 LKDLLLGLLKRNPKDRI 246
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
190-437 6.95e-26

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: 107.79  E-value: 6.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVY-GCRKADTGKMYAMKCLDKKRIKMKQgETLALNERIMLSLVSTGdcpfIVCMTYAFHTPDKLC 268
Cdd:cd14201    7 EYSRKDLVGHGAFAVVFkGRHRKKTDWEVAIKSINKKNLSKSQ-ILLGKEIKILKELQHEN----IVALYDVQEMPNSVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA---------RISDLGLA 339
Cdd:cd14201   82 LVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKkssvsgiriKIADFGFA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKPHASV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFS 418
Cdd:cd14201  162 RYLQSNMMAATLcGSPMYMAPEVIMS-QHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRETS 240
                        250
                 ....*....|....*....
gi 148539879 419 PELKSLLEGLLQRDVSKRL 437
Cdd:cd14201  241 PYLADLLLGLLQRNQKDRM 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
197-440 7.67e-26

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: 106.93  E-value: 7.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFI--KCRKAKDREDVRNEIEIMNQL----RHPRLLQLYDAFETPREMVLVMEYVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDL-------HYHLSqhgvfsEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA-RISDLGLACDFSKKKP 347
Cdd:cd14103   75 GELfervvddDFELT------ERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQiKIIDFGLARKYDPDKK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 -HASVGTHGYMAPEVLQkgtaYDS---SADWFSLGCMLFKLLRGHSPFRQhktkdkhEIDRMTLtVNV---------ELP 414
Cdd:cd14103  149 lKVLFGTPEFVAPEVVN----YEPisyATDMWSVGVICYVLLSGLSPFMG-------DNDAETL-ANVtrakwdfddEAF 216
                        250       260
                 ....*....|....*....|....*.
gi 148539879 415 DTFSPELKSLLEGLLQRDVSKRLGCH 440
Cdd:cd14103  217 DDISDEAKDFISKLLVKDPRKRMSAA 242
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
187-436 9.34e-26

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: 107.33  E-value: 9.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPD 265
Cdd:cd14187    5 TRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSL----AHQHVVGFHGFFEDND 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC--DFS 343
Cdd:cd14187   81 FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATkvEYD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVL-QKGTAYDssADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTVnvelPDTFSPEL 421
Cdd:cd14187  161 GERKKTLCGTPNYIAPEVLsKKGHSFE--VDIWSIGCIMYTLLVGKPPFETSCLKETYlRIKKNEYSI----PKHINPVA 234
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:cd14187  235 ASLIQKMLQTDPTAR 249
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
191-436 1.15e-25

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 106.58  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEA-SKKEVILLAKMKH---PNIVTFFASFQENGRLFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLS-QHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH-ARISDLGLA--CDFSKK 345
Cdd:cd08225   78 MEYCDGGDLMKRINrQRGVlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMvAKLGDFGIArqLNDSME 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkdKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd08225  158 LAYTCVGTPYYLSPEICQN-RPYNNKTDIWSLGCVLYELCTLKHPFEGNNL--HQLVLKICQGYFAPISPNFSRDLRSLI 234
                        250
                 ....*....|.
gi 148539879 426 EGLLQrdVSKR 436
Cdd:cd08225  235 SQLFK--VSPR 243
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
188-395 1.32e-25

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: 106.65  E-value: 1.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYgcrkadtgkmYAMKCLDKKRIKMKQGETLAlneriMLSLVSTGDC------------PFIV 255
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVY----------RATCLLDRKPVALKKVQIFE-----MMDAKARQDCvkeidllkqlnhPNVI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 256 CMTYAFHTPDKLCFILDLMNGGDLH----YHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA 331
Cdd:cd08228   66 KYLDSFIEDNELNIVLELADAGDLSqmikYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVV 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 332 RISDLGLACDFSKKK--PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHK 395
Cdd:cd08228  146 KLGDLGLGRFFSSKTtaAHSLVGTPYYMSPERIHE-NGYNFKSDIWSLGCLLYEMAALQSPFYGDK 210
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
196-425 1.82e-25

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: 106.36  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRikMKQGETLALNERIM--LSLVSTGDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd06630    7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFCR--NSSSEQEEVVEAIReeIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG-HARISDLGLACDFSKKKPHAS-- 350
Cdd:cd06630   85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTGAGef 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 ----VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRM-TLTVNVELPDTFSPELKSL 424
Cdd:cd06630  165 qgqlLGTIAFMAPEVL-RGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLAlIFKIaSATTPPPIPEHLSPGLRDV 243

                 .
gi 148539879 425 L 425
Cdd:cd06630  244 T 244
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
195-436 2.63e-25

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: 105.70  E-value: 2.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCR---KADTGKMYAMKCLdkKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTL--KEDASESERKDFLKEaRVMKKL----GHPNVVRLLGVCTEEEPLYLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQH---------GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcD 341
Cdd:cd00192   75 MEYMEGGDLLDFLRKSrpvfpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLS-R 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FSKKKPHASVGTHG-----YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFRQHKTKD--KHEIDRMTLtvnvEL 413
Cdd:cd00192  154 DIYDDDYYRKKTGGklpirWMAPESLKDGI-FTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEvlEYLRKGYRL----PK 228
                        250       260
                 ....*....|....*....|...
gi 148539879 414 PDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd00192  229 PENCPDELYELMLSCWQLDPEDR 251
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
189-453 3.13e-25

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: 105.43  E-value: 3.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkqGETLALNERImlSLVSTGDCPFIVCMTYAFHTPDKL- 267
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVE------EDLQEIIKEI--SILKQCDSPYIVKYYGSYFKNTDLw 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 -----C---FILDLMNggdlhyhlSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd06612   75 ivmeyCgagSVSDIMK--------ITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSK--KKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQ-HKTKDKHEIDRM---TLTVnvel 413
Cdd:cd06612  147 GQLTDtmAKRNTVIGTPFWMAPEVIQE-IGYNNKADIWSLGITAIEMAEGKPPYSDiHPMRAIFMIPNKpppTLSD---- 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148539879 414 PDTFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFF 453
Cdd:cd06612  222 PEKWSPEFNDFVKKCLVKDPEER-----PSAIQLLQHPFI 256
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
189-436 3.53e-25

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: 105.50  E-value: 3.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGK--EHLIENEVSILRRVKH---PNIIMLIEEMDTPAELY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA----RISDLGLACdfSK 344
Cdd:cd14184   76 LVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGtkslKLGDFGLAT--VV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMtLTVNVELP----DTFSP 419
Cdd:cd14184  154 EGPLYTVcGTPTYVAPEIIAE-TGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQI-LLGKLEFPspywDNITD 231
                        250
                 ....*....|....*..
gi 148539879 420 ELKSLLEGLLQRDVSKR 436
Cdd:cd14184  232 SAKELISHMLQVNVEAR 248
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
196-437 3.63e-25

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: 105.63  E-value: 3.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERI-MLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06917    8 LVGRGSYGAVYRGYHVKTGRVVALKVLN---LDTDDDDVSDIQKEVaLLSQLKLGQPKNIIKYYGSYLKGPSLWIIMDYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHyHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF--SKKKPHASVG 352
Cdd:cd06917   85 EGGSIR-TLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLnqNSSKRSTFVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHktkDKHEIdrMTLTVNVELP----DTFSPELKSLLEGL 428
Cdd:cd06917  164 TPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDV---DALRA--VMLIPKSKPPrlegNGYSPLLKEFVAAC 238

                 ....*....
gi 148539879 429 LQRDVSKRL 437
Cdd:cd06917  239 LDEEPKDRL 247
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
191-437 3.92e-25

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: 105.07  E-value: 3.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmKQGET-----LALNERIMLSLVStgdcPFIVCMTYAFHTPD 265
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKK----KAPEDylqkfLPREIEVIKGLKH----PNLICFYEAIETTS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd14162   74 RVYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASV------GTHGYMAPEVLqKGTAYDSS-ADWFSLGCMLFKLLRGHSPF--RQHKTKDKHEIDRMTLTVNVELpdt 416
Cdd:cd14162  154 KDGKPKlsetycGSYAYASPEIL-RGIPYDPFlSDIWSMGVVLYTMVYGRLPFddSNLKVLLKQVQRRVVFPKNPTV--- 229
                        250       260
                 ....*....|....*....|.
gi 148539879 417 fSPELKSLLEGLLqRDVSKRL 437
Cdd:cd14162  230 -SEECKDLILRML-SPVKKRI 248
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
190-436 4.15e-25

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: 105.06  E-value: 4.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMK-----EIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP 347
Cdd:cd08219   76 VMEYCDGGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkdKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd08219  156 YACtyVGTPYYVPPEIWEN-MPYNNKSDIWSLGCILYELCTLKHPFQANSW--KNLILKVCQGSYKPLPSHYSYELRSLI 232
                        250
                 ....*....|.
gi 148539879 426 EGLLQRDVSKR 436
Cdd:cd08219  233 KQMFKRNPRSR 243
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
191-386 5.01e-25

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: 105.31  E-value: 5.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQ-----GETLALNEriMLSLVSTGDCPFIVCMTYAFHTPD 265
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIK-------KMKKkfyswEECMNLRE--VKSLRKLNEHPNIVKLKEVFREND 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGgDLhYHL---SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd07830   72 ELYFVFEYMEG-NL-YQLmkdRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 148539879 343 SKKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLR 386
Cdd:cd07830  150 RSRPPYTDyVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYT 194
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
197-399 5.36e-25

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: 105.08  E-value: 5.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGC--RKADTGKMYAMKCLDKKRI--KMKQGETLALNERIMLS------LVSTGDCpfivCMTYAfhtpDK 266
Cdd:cd13994    1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRRDDesKRKDYVKRLTSEYIISSklhhpnIVKVLDL----CQDLH----GK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--- 343
Cdd:cd13994   73 WCLVMEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGmpa 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 -KKKPHAS--VGTHGYMAPEVLQKGTaYD-SSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd13994  153 eKESPMSAglCGSEPYMAPEVFTSGS-YDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDS 211
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
190-436 6.06e-25

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: 104.39  E-value: 6.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGETLALNEriMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKS-KKPFRGPKERARALRE--VEAHAALGQHPNIVRYYSSWEEGGHLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHL---SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSkKK 346
Cdd:cd13997   78 QMELCENGSLQDALeelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLE-TS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGhSPFrQHKTKDKHEIdRMTltvnvELPDTF----SPELK 422
Cdd:cd13997  157 GDVEEGDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATG-EPL-PRNGQQWQQL-RQG-----KLPLPPglvlSQELT 228
                        250
                 ....*....|....
gi 148539879 423 SLLEGLLQRDVSKR 436
Cdd:cd13997  229 RLLKVMLDPDPTRR 242
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
197-452 6.48e-25

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: 104.30  E-value: 6.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKkrikmkqGETLALN-ERIMLSLVSTGDcPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14665    8 IGSGNFGVARLMRDKQTKELVAVKYIER-------GEKIDENvQREIINHRSLRH-PNIVRFKEVILTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISdlglACDFSKKK-------PH 348
Cdd:cd14665   80 GGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLK----ICDFGYSKssvlhsqPK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKgTAYDSS-ADWFSLGCMLFKLLRGHSPFRQ-HKTKDKHEIDRMTLTVNVELPDT--FSPELKSL 424
Cdd:cd14665  156 STVGTPAYIAPEVLLK-KEYDGKiADVWSCGVTLYVMLVGAYPFEDpEEPRNFRKTIQRILSVQYSIPDYvhISPECRHL 234
                        250       260
                 ....*....|....*....|....*...
gi 148539879 425 LEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14665  235 ISRIFVADPATRITI-----PEIRNHEW 257
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
196-450 9.38e-25

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: 104.80  E-value: 9.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKK----RIK-MKQGETLAL--NERIMLSLVSTgdcpfivcmtyaFHTPDKLC 268
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHpghsRSRvFREVETLHQcqGHPNILQLIEY------------FEDDERFY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL---LDEHGHARISDLGLA--CDFS 343
Cdd:cd14090   77 LVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGsgIKLS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 K------KKPHAS--VGTHGYMAPEVLQ----KGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK----DKHEIDR--- 404
Cdd:cd14090  157 StsmtpvTTPELLtpVGSAEYMAPEVVDafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEdcgwDRGEACQdcq 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 405 -MTLTV----NVELPDT----FSPELKSLLEGLLQRDVSKRLgchggGSQEVKEH 450
Cdd:cd14090  237 eLLFHSiqegEYEFPEKewshISAEAKDLISHLLVRDASQRY-----TAEQVLQH 286
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
191-437 9.46e-25

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: 104.72  E-value: 9.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKS--KRDPSEEIEI-------LLRYGQHPNIITLKDVYDDGKHVYLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA---RISDLGLAcdfskKK 346
Cdd:cd14175   74 TELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNPeslRICDFGFA-----KQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVG-------THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI-DRM---TLTVNVELPD 415
Cdd:cd14175  149 LRAENGllmtpcyTANFVAPEVLKR-QGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEIlTRIgsgKFTLSGGNWN 227
                        250       260
                 ....*....|....*....|..
gi 148539879 416 TFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14175  228 TVSDAAKDLVSKMLHVDPHQRL 249
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
195-437 1.04e-24

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: 105.12  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNerimlslVSTGDcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAALK-------LCEGH-PNIVKLHEVYHDQLHTFLVMELL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGlacdFSKKKP---- 347
Cdd:cd14179   85 KGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFG----FARLKPpdnq 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 --HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH--------EIDRMTLTVNVELPDTF 417
Cdd:cd14179  161 plKTPCFTLHYAAPELLNY-NGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCtsaeeimkKIKQGDFSFEGEAWKNV 239
                        250       260
                 ....*....|....*....|
gi 148539879 418 SPELKSLLEGLLQRDVSKRL 437
Cdd:cd14179  240 SQEAKDLIQGLLTVDPNKRI 259
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
189-466 1.14e-24

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: 104.43  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkqgETLALNERIMLSLVSTGDC--PFIVCMTYAFhTPDK 266
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTD-------PNPDVQKQILRELEINKSCasPYIVKYYGAF-LDEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFI---LDLMNGGDLH--YH--LSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd06621   73 DSSIgiaMEYCEGGSLDsiYKkvKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNV---ELPD- 415
Cdd:cd06621  153 GELVNSLAGTFTGTSYYMAPERIQ-GGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLGPIELLSYIVNMpnpELKDe 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 416 -----TFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFKGVDWQHVYLQKY 466
Cdd:cd06621  232 pengiKWSESFKDFIEKCLEKDGTRR-----PGPWQMLAHPWIKAQEKKKVNMAKF 282
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
191-436 1.32e-24

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: 103.66  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLdkKRI---KMKQGETL-ALNERIMLSLVstgDCPFIVCMTYAFHTPDK 266
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVL--KEIsvgELQPDETVdANREAKLLSKL---DHPAIVKFHDSFVEKES 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQH----GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGHARISDLGLACDF 342
Cdd:cd08222   77 FCIVTEYCEGGDLDDKISEYkksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRIL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASV--GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRghspfRQHKTKDKHEIDRMTLTVNVE---LPDTF 417
Cdd:cd08222  156 MGTSDLATTftGTPYYMSPEVL-KHEGYNSKSDIWSLGCILYEMCC-----LKHAFDGQNLLSVMYKIVEGEtpsLPDKY 229
                        250
                 ....*....|....*....
gi 148539879 418 SPELKSLLEGLLQRDVSKR 436
Cdd:cd08222  230 SKELNAIYSRMLNKDPALR 248
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
197-452 1.41e-24

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: 104.00  E-value: 1.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrikMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06641   12 IGKGSFGEVFKGIDNRTQKVVAIKIID-----LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF--SKKKPHASVGTH 354
Cdd:cd06641   87 GSA-LDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLtdTQIKRN*FVGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQ-HKTKDKHEIDRMTLTVnveLPDTFSPELKSLLEGLLQRDV 433
Cdd:cd06641  166 FWMAPEVI-KQSAYDSKADIWSLGITAIELARGEPPHSElHPMKVLFLIPKNNPPT---LEGNYSKPLKEFVEACLNKEP 241
                        250
                 ....*....|....*....
gi 148539879 434 SKRlgchgGGSQEVKEHSF 452
Cdd:cd06641  242 SFR-----PTAKELLKHKF 255
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
197-452 2.37e-24

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: 103.21  E-value: 2.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrikMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06640   12 IGKGSFGEVFKGIDNRTQQVVAIKIID-----LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF--SKKKPHASVGTH 354
Cdd:cd06640   87 GSA-LDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLtdTQIKRNTFVGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPfrqhkTKDKHEIDRMTLTVNVELPD---TFSPELKSLLEGLLQR 431
Cdd:cd06640  166 FWMAPEVIQQ-SAYDSKADIWSLGITAIELAKGEPP-----NSDMHPMRVLFLIPKNNPPTlvgDFSKPFKEFIDACLNK 239
                        250       260
                 ....*....|....*....|.
gi 148539879 432 DVSKRlgchgGGSQEVKEHSF 452
Cdd:cd06640  240 DPSFR-----PTAKELLKHKF 255
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
197-390 2.53e-24

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: 102.77  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLAL--NERIMLSlvstgDC--PFIVCMTYAFHTPDKLCFILD 272
Cdd:cd06613    8 IGSGTYGDVYKARNIATGELAAVKV-----IKLEPGDDFEIiqQEISMLK-----ECrhPNIVAYFGSYLRRDKLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLH--YHLSqhGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK--KKPH 348
Cdd:cd06613   78 YCGGGSLQdiYQVT--GPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAtiAKRK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148539879 349 ASVGTHGYMAPEVLQ--KGTAYDSSADWFSLGCMLFKLLRGHSP 390
Cdd:cd06613  156 SFIGTPYWMAPEVAAveRKGGYDGKCDIWALGITAIELAELQPP 199
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
189-436 2.57e-24

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: 103.22  E-value: 2.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLalNERIM--LSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd14046    6 TDFEELQVLGKGAFGQVVKVRNKLDGRYYAIK-----KIKLRSESKN--NSRILreVMLLSRLNHQHVVRYYQAWIERAN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLhYHLSQHGVFSEK-EMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd14046   79 LYIQMEYCEKSTL-RDLIDSGLFQDTdRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHAS--------------------VGTHGYMAPEVLQKGTA-YDSSADWFSLGCMLFKLLRghsPFrqhKTK-DKHEID 403
Cdd:cd14046  158 VELATqdinkstsaalgssgdltgnVGTALYVAPEVQSGTKStYNEKVDMYSLGIIFFEMCY---PF---STGmERVQIL 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148539879 404 RMTLTVNVELPDTF----SPELKSLLEGLLQRDVSKR 436
Cdd:cd14046  232 TALRSVSIEFPPDFddnkHSKQAKLIRWLLNHDPAKR 268
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
195-437 2.65e-24

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: 103.01  E-value: 2.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKR-----IKMKQGEtlalnerimLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14097    7 RKLGQGSFGVVIEATHKETQTKWAIKKINREKagssaVKLLERE---------VDILKHVNHAHIIHLEEVFETPKRMYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL----LDEHG---HARISDLGLACD- 341
Cdd:cd14097   78 VMELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNdklNIKVTDFGLSVQk 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 --FSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQhKTKDK--HEIDRMTLTVNVELPDTF 417
Cdd:cd14097  158 ygLGEDMLQETCGTPIYMAPEVIS-AHGYSQQCDIWSIGVIMYMLLCGEPPFVA-KSEEKlfEEIRKGDLTFTQSVWQSV 235
                        250       260
                 ....*....|....*....|
gi 148539879 418 SPELKSLLEGLLQRDVSKRL 437
Cdd:cd14097  236 SDAAKNVLQQLLKVDPAHRM 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
191-453 2.72e-24

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: 103.41  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGET----LALNE-RIMLSLvstgDCPFIV-----CMTYA 260
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALK-----KIRMENEKEgfpiTAIREiKLLQKL----DHPNVVrlkeiVTSKG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 261 FHTPDKLCF-ILDLMNGgDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL 338
Cdd:cd07840   72 SAKYKGSIYmVFEYMDH-DLTGLLDNPEVkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 ACDFSKKKPHA---SVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrQHKTkdkhEIDRM--------TL 407
Cdd:cd07840  151 ARPYTKENNADytnRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIF-QGKT----ELEQLekifelcgSP 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 408 TVNV-----ELP----------------DTF----SPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07840  226 TEENwpgvsDLPwfenlkpkkpykrrlrEVFknviDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
191-437 3.39e-24

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: 102.46  E-value: 3.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIkmkqGETLALNERIMLSLVSTgdCPFIVCMTY-AFHTPDKLCF 269
Cdd:cd14078    5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAL----GDDLPRVKTEIEALKNL--SHQHICRLYhVIETDNKIFM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd14078   79 VLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 ---SVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd14078  159 letCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVM---ALYRKIQSGKYEEPEWLSPSSKLLLD 235
                        250
                 ....*....|.
gi 148539879 427 GLLQRDVSKRL 437
Cdd:cd14078  236 QMLQVDPKKRI 246
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
197-437 3.44e-24

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


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 102.37  E-value: 3.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGC-RKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14121    3 LGSGTYATVYKAyRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKL----KHPHIVELKDFQWDEEHIYLIMEYCS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD--EHGHARISDLGLACDFSKK-KPHASVG 352
Cdd:cd14121   79 GGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSsrYNPVLKLADFGFAQHLKPNdEAHSLRG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidRMTLTVNVELPDT--FSPELKSLLEGLLQ 430
Cdd:cd14121  159 SPLYMAPEMILKKK-YDARVDLWSVGVILYECLFGRAPFASRSFEELEE--KIRSSKPIEIPTRpeLSADCRDLLLRLLQ 235

                 ....*..
gi 148539879 431 RDVSKRL 437
Cdd:cd14121  236 RDPDRRI 242
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
191-454 3.60e-24

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: 103.35  E-value: 3.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKC-LDKKRIKmkqgetlalnER---IMLSLvstgDCPFIVCMTYAFHTPDK 266
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKvLQDKRYK----------NRelqIMRRL----KHPNIVKLKYFFYSSGE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 ------LCFILDLMNGgDLH----YHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISD 335
Cdd:cd14137   72 kkdevyLNLVMEYMPE-TLYrvirHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 336 LGLACDFSKKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD-------------KHE 401
Cdd:cd14137  151 FGSAKRLVPGEPNVSyICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDqlveiikvlgtptREQ 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 402 IDRM-------------TLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFFK 454
Cdd:cd14137  231 IKAMnpnytefkfpqikPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTA-----LEALAHPFFD 291
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
189-436 4.56e-24

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: 102.38  E-value: 4.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGK--EHMIQNEVSILRRVKH---PNIVLLIEEMDMPTELY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA----RISDLGLACdFSK 344
Cdd:cd14183   81 LVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGskslKLGDFGLAT-VVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQhKTKDKHEIDRMTLTVNVELP----DTFSPE 420
Cdd:cd14183  160 GPLYTVCGTPTYVAPEIIAE-TGYGLKVDIWAAGVITYILLCGFPPFRG-SGDDQEVLFDQILMGQVDFPspywDNVSDS 237
                        250
                 ....*....|....*.
gi 148539879 421 LKSLLEGLLQRDVSKR 436
Cdd:cd14183  238 AKELITMMLQVDVDQR 253
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
188-452 5.47e-24

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: 102.35  E-value: 5.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQG------------------ETLALNERIM--LSLVS 247
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGfprrppprgaraapegctQPRGPIERVYqeIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 248 TGDCPFIVCMTYAFHTP--DKLCFILDLMNGGDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL 325
Cdd:cd14199   81 KLDHPNVVKLVEVLDDPseDHLYMVFELVKQGPV-MEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 326 DEHGHARISDLGLACDFSKKKPHAS--VGTHGYMAPEVLQK------GTAYDSSADWFSLGCMLFkllrGHSPFRQHKTK 397
Cdd:cd14199  160 GEDGHIKIADFGVSNEFEGSDALLTntVGTPAFMAPETLSEtrkifsGKALDVWAMGVTLYCFVF----GQCPFMDERIL 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 398 DKHEIDRmtlTVNVELPDT--FSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14199  236 SLHSKIK---TQPLEFPDQpdISDDLKDLLFRMLDKNPESRISV-----PEIKLHPW 284
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
197-397 6.38e-24

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: 101.57  E-value: 6.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKAdTGKMYAMKCLDKKRIKMKQGetlALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14161   11 LGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQD---LLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK-PHASVGTHG 355
Cdd:cd14161   87 GDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKfLQTYCGSPL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148539879 356 YMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK 397
Cdd:cd14161  167 YASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYK 208
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
197-454 1.62e-23

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: 100.59  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMD---LRKQQRRELLFNE---VVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH--ASVGTH 354
Cdd:cd06648   89 GAL-TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRrkSLVGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd06648  168 YWMAPEVISR-LPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRMLVRDPA 246
                        250       260
                 ....*....|....*....|
gi 148539879 435 KRlgchgGGSQEVKEHSFFK 454
Cdd:cd06648  247 QR-----ATAAELLNHPFLA 261
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
197-453 1.63e-23

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: 100.97  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLalnERIMLS--LVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAK-----IIQIESEEEL---EDFMVEidILSECKHPNIVGLYEAYFYENKLWILIEFC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDL-HYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK--KKPHASV 351
Cdd:cd06611   85 DGGALdSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKStlQKRDTFI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQ----KGTAYDSSADWFSLGCMLFKLLRGHSPfrqhktkdKHEIDRMTLTVNV--------ELPDTFSP 419
Cdd:cd06611  165 GTPYWMAPEVVAcetfKDNPYDYKADIWSLGITLIELAQMEPP--------HHELNPMRVLLKIlksepptlDQPSKWSS 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 420 ELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd06611  237 SFNDFLKSCLVKDPDDRPTA-----AELLKHPFV 265
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
196-390 1.85e-23

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: 100.53  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCL-----DKKRIKMKQGETL-ALNERImlSLVSTGDCPFIV-CMTYAfHTPDKLC 268
Cdd:cd06629    8 LIGKGTYGRVYLAMNATTGEMLAVKQVelpktSSDRADSRQKTVVdALKSEI--DTLKDLDHPNIVqYLGFE-ETEDYFS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLacdfSKKKPH 348
Cdd:cd06629   85 IFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGI----SKKSDD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 349 AsVGTHG---------YMAPEVLQ-KGTAYDSSADWFSLGCMLFKLLRGHSP 390
Cdd:cd06629  161 I-YGNNGatsmqgsvfWMAPEVIHsQGQGYSAKVDIWSLGCVVLEMLAGRRP 211
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
252-453 2.16e-23

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: 100.31  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 252 PFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLS-------QHGVFS---------------EKEMRFYATEIILGLEHMH 309
Cdd:cd05576   51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSkflndkeIHQLFAdlderlaaasrfyipEECIQRWAAEMVVALDALH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 310 NRFVVYRDLKPANILLDEHGHARI------SDLGLACDfskkkphASVGTHGYMAPEVlqKGTAYDSSA-DWFSLGCMLF 382
Cdd:cd05576  131 REGIVCRDLNPNNILLNDRGHIQLtyfsrwSEVEDSCD-------SDAIENMYCAPEV--GGISEETEAcDWWSLGALLF 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 383 KLLRGHSPFRQHKTKdkheIDRMTltvNVELPDTFSPELKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFF 453
Cdd:cd05576  202 ELLTGKALVECHPAG----INTHT---TLNIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
191-437 2.47e-23

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: 100.67  E-value: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKMKQGETLALNErimlslvstgdcPFIVCMTYAFHTPDK 266
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLkktvDKKIVRTEIGVLLRLSH------------PNIIKLKEIFETPTE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH---ARISDLGLACDFS 343
Cdd:cd14085   73 ISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASV-GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkDKHEIDRmtlTVNVELP------DT 416
Cdd:cd14085  153 QQVTMKTVcGTPGYCAPEIL-RGCAYGPEVDMWSVGVITYILLCGFEPFYDERG-DQYMFKR---ILNCDYDfvspwwDD 227
                        250       260
                 ....*....|....*....|.
gi 148539879 417 FSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14085  228 VSLNAKDLVKKLIVLDPKKRL 248
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
195-429 3.43e-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: 99.71  E-value: 3.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmKQGETLALNERIMLSLVSTGDCPFIVCMTYafHTPDKLCFI 270
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVpfdpDSQETS-KEVNALECEIQLLKNLRHDRIVQYYGCLRD--PEEKKLSIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA------CdFSK 344
Cdd:cd06653   85 VEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkriqtiC-MSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkdKHEIDRM-TLTVNVELPDTFSPELKS 423
Cdd:cd06653  164 TGIKSVTGTPYWMSPEVIS-GEGYGRKADVWSVACTVVEMLTEKPPWAEYEA--MAAIFKIaTQPTKPQLPDGVSDACRD 240

                 ....*.
gi 148539879 424 LLEGLL 429
Cdd:cd06653  241 FLRQIF 246
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
195-436 5.48e-23

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: 98.91  E-value: 5.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL-----DKKRIKMKQGETLALnERImlslvstgDCPFIV-CMTYAFHTpDKLC 268
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIrfqdnDPKTIKEIADEMKVL-EGL--------DHPNLVrYYGVEVHR-EEVY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHyHLSQHGVFSEKEM-RFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA---CDFSK 344
Cdd:cd06626   76 IFMEYCQEGTLE-ELLRHGRILDEAViRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAvklKNNTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHAS----VGTHGYMAPEVL--QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHktkdKHEIDRMTLTVNVELP---- 414
Cdd:cd06626  155 TMAPGEvnslVGTPAYMAPEVItgNKGEGHGRAADIWSLGCVVLEMATGKRPWSEL----DNEWAIMYHVGMGHKPpipd 230
                        250       260
                 ....*....|....*....|...
gi 148539879 415 -DTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd06626  231 sLQLSPEGKDFLSRCLESDPKKR 253
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
197-456 5.56e-23

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: 99.72  E-value: 5.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkqGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETK------SEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLH-YHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK--KKPHASVGT 353
Cdd:cd06644   94 GAVDaIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKtlQRRDSFIGT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPfrqhktkdKHEIDRMTLTVNV--------ELPDTFSPEL 421
Cdd:cd06644  174 PYWMAPEVVmcetMKDTPYDYKADIWSLGITLIEMAQIEPP--------HHELNPMRVLLKIaksepptlSQPSKWSMEF 245
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFKGV 456
Cdd:cd06644  246 RDFLKTALDKHPETR-----PSAAQLLEHPFVSSV 275
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
197-411 7.69e-23

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: 98.88  E-value: 7.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQgETLALNERIMLSLVStgDCPFIVCMTYAFH--TPDKLCFILDLM 274
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLE-QVNNLREIQALRRLS--PHPNILRLIEVLFdrKTGRLALVFELM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEhGHARISDLGLACDFSKKKPHAS-VGT 353
Cdd:cd07831   83 DMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGSCRGIYSKPPYTEyIST 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 354 HGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNV 411
Cdd:cd07831  162 RWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLF-----PGTNELDQIAKIHDV 214
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
189-436 8.11e-23

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: 99.43  E-value: 8.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKA-DTGKMYAMKCLDKKRI--KMKQGETLA--LNE-RIMLSLvstgDCPFIVCMTYAFH 262
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVRKADLssDNLKGSSRAniLKEvQIMKRL----SHPNIVKLLDFQE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL------------------ 324
Cdd:cd14096   77 SDEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkadd 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 325 ----LDEH-----------GHARISDLGLACDFSKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHS 389
Cdd:cd14096  157 detkVDEGefipgvggggiGIVKLADFGLSKQVWDSNTKTPCGTVGYTAPEVV-KDERYSKKVDMWALGCVLYTLLCGFP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 390 PF--RQHKTKDKhEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14096  236 PFydESIETLTE-KISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKR 283
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
187-436 8.67e-23

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: 99.34  E-value: 8.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd08229   22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKE---IDLLKQLNHPNVIKYYASFIEDNE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHL----SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd08229   99 LNIVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFF 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKK--PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP-DTFSP 419
Cdd:cd08229  179 SSKTtaAHSLVGTPYYMSPERIHE-NGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPsDHYSE 257
                        250
                 ....*....|....*..
gi 148539879 420 ELKSLLEGLLQRDVSKR 436
Cdd:cd08229  258 ELRQLVNMCINPDPEKR 274
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
197-437 8.75e-23

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: 99.56  E-value: 8.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALneRIMLSLvstgdcPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAAL--RLCQSH------PNIVALHEVLHDQYHTYLVMELLRG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA---RISDLGlacdFSKKKPHASVGT 353
Cdd:cd14180   86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGavlKVIDFG----FARLRPQGSRPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HG------YMAPEVLQKGtAYDSSADWFSLGCMLFKLLRGHSPFR--------QHKTKDKHEIDRMTLTVNVELPDTFSP 419
Cdd:cd14180  162 QTpcftlqYAAPELFSNQ-GYDESCDLWSLGVILYTMLSGQVPFQskrgkmfhNHAADIMHKIKEGDFSLEGEAWKGVSE 240
                        250
                 ....*....|....*...
gi 148539879 420 ELKSLLEGLLQRDVSKRL 437
Cdd:cd14180  241 EAKDLVRGLLTVDPAKRL 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
197-391 1.61e-22

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: 97.52  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLaLNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKAL-LKEAEKMERARH---SYVLPLLGVCVERRSLGLVMEYMEN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRF-YATEIILGLEHMHNRF--VVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV-- 351
Cdd:cd13978   77 GSLKSLLEREIQDVPWSLRFrIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRRrg 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 352 -----GTHGYMAPEVLQKGTA-YDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd13978  157 tenlgGTPIYMAPEAFDDFNKkPTSKSDVYSFAIVIWAVLTRKEPF 202
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
195-453 1.62e-22

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: 97.39  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNerimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVsKPHQREKIDKE----IELHRILHHKHVVQFYHYFEDKENIYILLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KKKPHASV 351
Cdd:cd14188   83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEplEHRRRTIC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQR 431
Cdd:cd14188  163 GTPNYLSPEVLNK-QGHGCESDIWALGCVMYTMLLGRPPF---ETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSK 238
                        250       260
                 ....*....|....*....|..
gi 148539879 432 DVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14188  239 NPEDRPSL-----DEIIRHDFF 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
191-450 1.63e-22

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: 97.46  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKML----NHPHIIKLYQVMETKDMLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS 350
Cdd:cd14071   78 TEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 -VGTHGYMAPEVLQkGTAYDS-SADWFSLGCMLFKLLRGHSPF--------RQHKTKDKHEIdrmtltvnvelPDTFSPE 420
Cdd:cd14071  158 wCGSPPYAAPEVFE-GKEYEGpQLDIWSLGVVLYVLVCGALPFdgstlqtlRDRVLSGRFRI-----------PFFMSTD 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 421 LKSLLEGLLQRDVSKRLGChgggsQEVKEH 450
Cdd:cd14071  226 CEHLIRRMLVLDPSKRLTI-----EQIKKH 250
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
191-452 1.78e-22

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: 97.53  E-value: 1.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikMKQGETLA---LNERimlSLVStgdcPFIVCMTYAFHTPDKL 267
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERG---LKIDENVQreiINHR---SLRH----PNIIRFKEVVLTPTHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISdlglACDF--SK- 344
Cdd:cd14662   72 AIVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLK----ICDFgySKs 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 ----KKPHASVGTHGYMAPEVLQKgTAYD-SSADWFSLGCMLFKLLRGHSPFR-QHKTKD-KHEIDRMtLTVNVELPD-- 415
Cdd:cd14662  148 svlhSQPKSTVGTPAYIAPEVLSR-KEYDgKVADVWSCGVTLYVMLVGAYPFEdPDDPKNfRKTIQRI-MSVQYKIPDyv 225
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148539879 416 TFSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14662  226 RVSQDCRHLLSRIFVANPAKRITI-----PEIKNHPW 257
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
189-453 1.97e-22

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: 96.91  E-value: 1.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVY-------GCRKADTGKMYAMKCLDK----KRIkmkqgetlaLNERIMLSLVstGDCPFIVCM 257
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYkaedklhDLYDRNKGRLVALKHIYPtsspSRI---------LNELECLERL--GGSNNVSGL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 258 TYAFHTPDKLCFILDLMNGGDLHYHLSQhgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH-GHARISDL 336
Cdd:cd14019   70 ITAFRNEDQVVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 337 GLACDFSKKKP-HAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhkTKDKHEIDRMtltvnVELP 414
Cdd:cd14019  147 GLAQREEDRPEqRAPrAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPF----FFSSDDIDAL-----AEIA 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148539879 415 DTF-SPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd14019  218 TIFgSDEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
191-492 1.99e-22

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: 98.75  E-value: 1.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMK--------CLDKKRIkmkqgetlaLNE-RIMLSLvstgDCPFIVCMTYAF 261
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKkisnvfddLIDAKRI---------LREiKILRHL----KHENIIGLLDIL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 HTPDKLCF-----ILDLMnGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDL 336
Cdd:cd07834   69 RPPSPEEFndvyiVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 337 GLA--CDFSKKKPHAS--VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNV- 411
Cdd:cd07834  148 GLArgVDPDEDKGFLTeyVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLF-----PGRDYIDQLNLIVEVl 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 412 --------------------------------ELPDTFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFKgvdwq 459
Cdd:cd07834  223 gtpseedlkfissekarnylkslpkkpkkplsEVFPGASPEAIDLLEKMLVFNPKKRI-----TADEALAHPYLA----- 292
                        330       340       350
                 ....*....|....*....|....*....|...
gi 148539879 460 hvylqkyppPLIPPRGEVNAADAFDIGSFDEED 492
Cdd:cd07834  293 ---------QLHDPEDEPVAKPPFDFPFFDDEE 316
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
193-436 2.10e-22

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 101.10  E-value: 2.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 193 VHRIIGRGGFGEVYGCRKADTGKMYAMKCLD-----KKRIKMKQGETLALNERIMLSLV--------STGDCPFIVCMty 259
Cdd:PTZ00283  36 ISRVLGSGATGTVLCAKRVSDGEPFAVKVVDmegmsEADKNRAQAEVCCLLNCDFFSIVkchedfakKDPRNPENVLM-- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 260 afhtpdkLCFILDLMNGGDLHYHLSQHG----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISD 335
Cdd:PTZ00283 114 -------IALVLDYANAGDLRQEIKSRAktnrTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGD 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 336 LGlacdFSKKKPhASV---------GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMT 406
Cdd:PTZ00283 187 FG----FSKMYA-ATVsddvgrtfcGTPYYVAPEIWRR-KPYSKKADMFSLGVLLYELLTLKRPF---DGENMEEVMHKT 257
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148539879 407 LTVNVE-LPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:PTZ00283 258 LAGRYDpLPPSISPEMQEIVTALLSSDPKRR 288
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
187-436 2.18e-22

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: 98.22  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQGETLALNERIMLSL---VSTGDCPFIV-CMTYAFH 262
Cdd:cd06618   13 DLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVK-------QMRRSGNKEENKRILMDLdvvLKSHDCPYIVkCYGYFIT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPD-KLCfiLDLMNG-GDLHYHLSQHGvFSEKEMRFYATEIILGLEHM---HNrfVVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd06618   86 DSDvFIC--MELMSTcLDKLLKRIQGP-IPEDILGKMTVSIVKALHYLkekHG--VIHRDVKPSNILLDESGNVKLCDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKKPHA-SVGTHGYMAPEVL--QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkdkhEIDRMTLTVNVELP 414
Cdd:cd06618  161 ISGRLVDSKAKTrSAGCAAYMAPERIdpPDNPKYDIRADVWSLGISLVELATGQFPYRNCKT----EFEVLTKILNEEPP 236
                        250       260
                 ....*....|....*....|....*..
gi 148539879 415 -----DTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd06618  237 slppnEGFSPDFCSFVDLCLTKDHRYR 263
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
191-415 2.41e-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: 97.49  E-value: 2.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCR-KADTGKMYAMKCLDKKRIKMKQGETLaLNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSeRVPTGKVYAVKKLKPNYAGAKDRLRR-LEEVSILRELTLDGHDNIVQLIDSWEYHGHLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSE-KEMRFYAT--EIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd14052   81 QTELCENGSLDVFLSELGLLGRlDEFRVWKIlvELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLIR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 347 PHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFkllrghspfrqhktkdkhEIdrmtlTVNVELPD 415
Cdd:cd14052  161 GIEREGDREYIAPEILSEHM-YDKPADIFSLGLILL------------------EA-----AANVVLPD 205
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
197-436 3.50e-22

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: 97.02  E-value: 3.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkqGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTK------SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLH-YHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK--KKPHASVGT 353
Cdd:cd06643   87 GAVDaVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRtlQRRDSFIGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPfrqhktkdKHEIDRMTLTVNV--------ELPDTFSPEL 421
Cdd:cd06643  167 PYWMAPEVVmcetSKDRPYDYKADVWSLGVTLIEMAQIEPP--------HHELNPMRVLLKIaksepptlAQPSRWSPEF 238
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:cd06643  239 KDFLRKCLEKNVDAR 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
196-454 3.67e-22

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: 96.91  E-value: 3.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLA------LNERIMLSLVSTGdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd14182   10 ILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEVQelreatLKEIDILRKVSGH--PNIIQLKDTYETNTFFFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK-KKPH 348
Cdd:cd14182   88 VFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPgEKLR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQ-----KGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdKHEIDRMTLTVNVELP----DTFSP 419
Cdd:cd14182  168 EVCGTPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRK---QMLMLRMIMSGNYQFGspewDDRSD 244
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148539879 420 ELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:cd14182  245 TVKDLISRFLVVQPQKRY-----TAEEALAHPFFQ 274
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
197-466 4.25e-22

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: 97.05  E-value: 4.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSlvstGDCPFIVCMTYA-FHTPDklCFI-LDLM 274
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRS----SDCPYIVKFYGAlFREGD--CWIcMELM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGG-DLHY---HLSQHGVFSEKEMRFYATEIILGLEHMHNRF-VVYRDLKPANILLDEHGHARISDLGLACDF--SKKKP 347
Cdd:cd06616   88 DISlDKFYkyvYEVLDSVIPEEILGKIAVATVKALNYLKEELkIIHRDVKPSNILLDRNGNIKLCDFGISGQLvdSIAKT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HaSVGTHGYMAPEVLQKGTA---YDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkheIDRMTLTVNVELP-------DTF 417
Cdd:cd06616  168 R-DAGCRPYMAPERIDPSASrdgYDVRSDVWSLGITLYEVATGKFPYPKWNSV----FDQLTQVVKGDPPilsnseeREF 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 418 SPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFKGVDWQHVYLQKY 466
Cdd:cd06616  243 SPSFVNFVNLCLIKDESKR-----PKYKELLKHPFIKMYEERNVDVAAY 286
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
197-452 4.83e-22

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: 95.87  E-value: 4.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgetlalNERIMLSLVSTGDC---PFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQK-------TQRLLSREISSMEKlhhPNIIRLYEVVETLSKLHLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACdFSKK--KPHASV 351
Cdd:cd14075   83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFST-HAKRgeTLNTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 GTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQhKTKDKheIDRMTLTVNVELPDTFSPELKSLLEGLLQR 431
Cdd:cd14075  162 GSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRA-ETVAK--LKKCILEGTYTIPSYVSEPCQELIRGILQP 238
                        250       260
                 ....*....|....*....|.
gi 148539879 432 DVSKRLGChgggsQEVKEHSF 452
Cdd:cd14075  239 VPSDRYSI-----DEIKNSEW 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
196-436 5.00e-22

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: 96.53  E-value: 5.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGETLALNERIM---------------LSLVSTGDCPFIVCMTYA 260
Cdd:cd14000    1 LLGDGGFGSVY--RASYKGEPVAVKIFNKHTSSNFANVPADTMLRHLratdamknfrllrqeLTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 261 FHTPdkLCFILDLMNGGDLHyHLSQHGVFSEKEMRFYATEIIL-----GLEHMHNRFVVYRDLKPANILL-----DEHGH 330
Cdd:cd14000   79 GIHP--LMLVLELAPLGSLD-HLLQQDSRSFASLGRTLQQRIAlqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 331 ARISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKT----KDKHEIDRMT 406
Cdd:cd14000  156 IKIADYGISRQCCRMGAKGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKfpneFDIHGGLRPP 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 407 LTvnvELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14000  236 LK---QYECAPWPEVEVLMKKCWKENPQQR 262
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
195-436 5.38e-22

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: 96.16  E-value: 5.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRiKMKQGETLALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14197   15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRR-KGQDCRMEIIHEIAVLELAQ--ANPWVINLHEVYETASEMILVLEYA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH---GHARISDLGLACDFSKKKPHA 349
Cdd:cd14197   92 AGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SV-GTHGYMAPEVLqkgtAYD---SSADWFSLGCMLFKLLRGHSPFRqhkTKDKHE----IDRMTLTVNVELPDTFSPEL 421
Cdd:cd14197  172 EImGTPEYVAPEIL----SYEpisTATDMWSIGVLAYVMLTGISPFL---GDDKQEtflnISQMNVSYSEEEFEHLSESA 244
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:cd14197  245 IDFIKTLLIKKPENR 259
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
197-436 7.27e-22

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: 95.65  E-value: 7.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEtlalNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd08218    8 IGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKERE----ESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHL-SQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA--CDFSKKKPHASVG 352
Cdd:cd08218   84 GDLYKRInAQRGVlFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIArvLNSTVELARTCIG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD-KHEIDRMTLTvnvELPDTFSPELKSLLEGLLQR 431
Cdd:cd08218  164 TPYYLSPEICEN-KPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNlVLKIIRGSYP---PVPSRYSYDLRSLVSQLFKR 239

                 ....*
gi 148539879 432 DVSKR 436
Cdd:cd08218  240 NPRDR 244
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
191-454 7.84e-22

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: 96.46  E-value: 7.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLA-LNERImlSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEdLKREA--SICHMLKHPHIVELLETYSSDGMLYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHG----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLACDF 342
Cdd:cd14094   83 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKK--PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPE 420
Cdd:cd14094  163 GESGlvAGGRVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISES 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 421 LKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:cd14094  242 AKDLVRRMLMLDPAERI-----TVYEALNHPWIK 270
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
191-437 1.04e-21

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: 97.01  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMKQGETLalnerimlslVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKsKRDPTEEIEIL----------LRYGQHPNIITLKDVYDDGKYVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA---RISDLGLAcdfskK 345
Cdd:cd14176   91 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFA-----K 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVG-------THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP---- 414
Cdd:cd14176  166 QLRAENGllmtpcyTANFVAPEVLER-QGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSggyw 244
                        250       260
                 ....*....|....*....|...
gi 148539879 415 DTFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14176  245 NSVSDTAKDLVSKMLHVDPHQRL 267
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
197-452 1.26e-21

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: 95.51  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrikMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06642   12 IGKGSFGEVYKGIDNRTKEVVAIKIID-----LEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK--KPHASVGTH 354
Cdd:cd06642   87 GSA-LDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTqiKRNTFVGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIdRMTLTVNVELPDT----FSPELKSLLEGLLQ 430
Cdd:cd06642  166 FWMAPEVI-KQSAYDFKADIWSLGITAIELAKGEPPN-----SDLHPM-RVLFLIPKNSPPTlegqHSKPFKEFVEACLN 238
                        250       260
                 ....*....|....*....|..
gi 148539879 431 RDVSKRlgchgGGSQEVKEHSF 452
Cdd:cd06642  239 KDPRFR-----PTAKELLKHKF 255
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
198-391 1.38e-21

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: 94.89  E-value: 1.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 198 GRGGFGEVYGCRKADTGKMYamkcLDKKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNF----PAKIVPYQAEEKQGVLQEyEILKSL----HHERIMALHEAYITPRYLVLIAEFCSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF---SKKKPHASVGT 353
Cdd:cd14111   84 KELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFnplSLRQLGRRTGT 163
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148539879 354 HGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14111  164 LEYMAPEMV-KGEPVGPPADIWSIGVLTYIMLSGRSPF 200
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
196-437 1.62e-21

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: 95.48  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14173    9 VLGEGAYARVQTCINLITNKEYAVKIIEKR-----PGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDL--HYHLSQHgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGHaRISDLGLaCDF---------SK 344
Cdd:cd14173   84 GGSIlsHIHRRRH--FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILC-EHPN-QVSPVKI-CDFdlgsgiklnSD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHAS------VGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD-------KHEIDRMTL 407
Cdd:cd14173  159 CSPISTpelltpCGSAEYMAPEVVeafnEEASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDcgwdrgeACPACQNML 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148539879 408 TVNV-----ELPDT----FSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14173  239 FESIqegkyEFPEKdwahISCAAKDLISKLLVRDAKQRL 277
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
190-437 1.65e-21

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: 94.52  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmkQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd14087    2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC----RGREVCESELNVLRRVRH---TNIIQLIEVFETKERVYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR---ISDLGLAcDFSKKK 346
Cdd:cd14087   75 VMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSkimITDFGLA-STRKKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PH----ASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDTFSPEL 421
Cdd:cd14087  154 PNclmkTTCGTPEYIAPEILLR-KPYTQSVDMWAVGVIAYILLSGTMPFDdDNRTRLYRQILRAKYSYSGEPWPSVSNLA 232
                        250
                 ....*....|....*.
gi 148539879 422 KSLLEGLLQRDVSKRL 437
Cdd:cd14087  233 KDFIDRLLTVNPGERL 248
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
195-393 1.77e-21

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: 94.73  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL--DKKRIKMKQgETLALNERIML--SLVSTGDCPFIVCMTyafHTPDK-LCF 269
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSK-EVNALECEIQLlkNLLHERIVQYYGCLR---DPQERtLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA------CdFS 343
Cdd:cd06652   84 FMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASkrlqtiC-LS 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQ 393
Cdd:cd06652  163 GTGMKSVTGTPYWMSPEVIS-GEGYGRKADIWSVGCTVVEMLTEKPPWAE 211
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
197-437 1.94e-21

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: 94.48  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14105   13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsRRGVSREDIER-EVSILRQVLHPNIITLHDVFENKTDVVLILELVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE----HGHARISDLGLACDFSKKKPHASV 351
Cdd:cd14105   92 GGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHKIEDGNEFKNI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 -GTHGYMAPEVLqkgtAYDS---SADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDTF---SPEL-KS 423
Cdd:cd14105  172 fGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPF---LGDTKQETLANITAVNYDFDDEYfsnTSELaKD 244
                        250
                 ....*....|....
gi 148539879 424 LLEGLLQRDVSKRL 437
Cdd:cd14105  245 FIRQLLVKDPRKRM 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
188-437 2.09e-21

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: 94.84  E-value: 2.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSV--HRIIGRGGFGEVYGCRKADTGKMYAMKCL-DKKRikmkqgetlALNERIMLSLVSTGDCPFIVCMTYA---- 260
Cdd:cd14171    3 LEEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKILlDRPK---------ARTEVRLHMMCSGHPNIVQIYDVYAnsvq 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 261 ----FHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARI 333
Cdd:cd14171   74 fpgeSSPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 334 SDLGLAC--DFSKKKPHAsvgTHGYMAPEVL---------QKGT-------AYDSSADWFSLGCMLFKLLRGHSPF---R 392
Cdd:cd14171  154 CDFGFAKvdQGDLMTPQF---TPYYVAPQVLeaqrrhrkeRSGIptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFyseH 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 393 QHKTKDKhEIDRMTLTVNVELPDT----FSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14171  231 PSRTITK-DMKRKIMTGSYEFPEEewsqISEMAKDIVRKLLCVDPEERM 278
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
209-436 2.13e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 98.17  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 209 RKADTGKMYAMKCLDKK-----RIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHL 283
Cdd:PTZ00267  77 RNPTTAAFVATRGSDPKekvvaKFVMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQI 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 284 SQ----HGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP----HASVGTHG 355
Cdd:PTZ00267 157 KQrlkeHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSldvaSSFCGTPY 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 356 YMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVE-LPDTFSPELKSLLEGLLQRDVS 434
Cdd:PTZ00267 237 YLAPELWER-KRYSKKADMWSLGVILYELLTLHRPF---KGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPA 312

                 ..
gi 148539879 435 KR 436
Cdd:PTZ00267 313 LR 314
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
197-453 2.20e-21

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: 94.90  E-value: 2.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQG--ETLALNERIMLSLVStgDCPFIVCMTYAFHTPDK----LCFI 270
Cdd:cd07837    9 IGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEgvPSTALREVSLLQMLS--QSIYIVRLLDVEHVEENgkplLYLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGgDLHYHLSQHG-----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLACDFS- 343
Cdd:cd07837   84 FEYLDT-DLKKFIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLGLGRAFTi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 --KKKPHASVgTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLR------GHSPFRQ-------------------HKT 396
Cdd:cd07837  163 piKSYTHEIV-TLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRkqplfpGDSELQQllhifrllgtpneevwpgvSKL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 397 KDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07837  242 RDWHEYPQWKPQDLSRAVPDLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
190-430 2.77e-21

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: 94.34  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLALnerIMLSLVSTGDC--PFIVCMTYAFHTPDKL 267
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKV-----IKLEPGEDFAV---VQQEIIMMKDCkhSNIVAYFGSYLRRDKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLH--YHLSqhGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd06645   84 WICMEFCGGGSLQdiYHVT--GPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITAT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 --KPHASVGTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKL-----------------LRGHSPFRQHKTKDK----- 399
Cdd:cd06645  162 iaKRKSFIGTPYWMAPEVaaVERKGGYNQLCDIWAVGITAIELaelqppmfdlhpmralfLMTKSNFQPPKLKDKmkwsn 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148539879 400 --HEIDRMTLTVNvelpdtfsPELKSLLEGLLQ 430
Cdd:cd06645  242 sfHHFVKMALTKN--------PKKRPTAEKLLQ 266
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
197-435 3.22e-21

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: 93.88  E-value: 3.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRkADTGKMYAMKCLDKKriKMKQGETLALNERIMLSLVSTgdcPFIVcMTYAFHT-PDKLCFILDLMN 275
Cdd:cd14066    1 IGSGGFGTVYKGV-LENGTVVAVKRLNEM--NCAASKKEFLTELEMLGRLRH---PNLV-RLLGYCLeSDEKLLVYEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLsqHGVFSEKEMRFYA-TEIILG----LEHMHNRF---VVYRDLKPANILLDEHGHARISDLGLACDFSKK-- 345
Cdd:cd14066   74 NGSLEDRL--HCHKGSPPLPWPQrLKIAKGiargLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSes 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 --KPHASVGTHGYMAPEVLQKGTAYDSSaDWFSLGCMLFKLLRGHSPFRQHKTKDkheiDRMTLTVNVElpdtfsPELKS 423
Cdd:cd14066  152 vsKTSAVKGTIGYLAPEYIRTGRVSTKS-DVYSFGVVLLELLTGKPAVDENRENA----SRKDLVEWVE------SKGKE 220
                        250
                 ....*....|..
gi 148539879 424 LLEGLLQRDVSK 435
Cdd:cd14066  221 ELEDILDKRLVD 232
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
193-436 3.23e-21

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: 93.73  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 193 VHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd14070    6 IGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKK--KAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS----KKKPH 348
Cdd:cd14070   84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGilgySDPFS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:cd14070  164 TQCGSPAYAAPELLAR-KKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEMNPLPTDLSPGAISFLRSL 242

                 ....*...
gi 148539879 429 LQRDVSKR 436
Cdd:cd14070  243 LEPDPLKR 250
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
196-454 3.35e-21

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: 94.33  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14174    9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKN-----AGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGL--------ACD-FS 343
Cdd:cd14174   84 GGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLgsgvklnsACTpIT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLQ----KGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTK----DKHEIDRMTLTV------ 409
Cdd:cd14174  164 TPELTTPCGSAEYMAPEVVEvftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTdcgwDRGEVCRVCQNKlfesiq 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148539879 410 --NVELPDT----FSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:cd14174  244 egKYEFPDKdwshISSEAKDLISKLLVRDAKERL-----SAAQVLQHPWVQ 289
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
189-452 3.40e-21

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: 93.91  E-value: 3.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERImlsLVSTGDCPFIVCMTYAFHTP---- 264
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD---IIEDEEEEIKLEINI---LRKFSNHPNIATFYGAFIKKdppg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 --DKLCFILDLMNGG---DLHYHLSQHGVFSEKEMRFY-ATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL 338
Cdd:cd06608   80 gdDQLWLVMEYCGGGsvtDLVKGLRKKGKRLKEEWIAYiLRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 ACDFSKK--KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRM---TLT 408
Cdd:cd06608  160 SAQLDSTlgRRNTFIGTPYWMAPEVIacdqQPDASYDARCDVWSLGITAIELADGKPPLcDMHPMRALFKIPRNpppTLK 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148539879 409 VnvelPDTFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSF 452
Cdd:cd06608  240 S----PEKWSKEFNDFISECLIKNYEQR-----PFTEELLEHPF 274
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
197-452 3.72e-21

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: 93.67  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKC--------LDKKRIKMKQGETlALNERIM--LSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd14077    9 IGAGSMGKVKLAKHIRTGEKCAIKIiprasnagLKKEREKRLEKEI-SRDIRTIreAALSSLLNHPHICRLRDFLRTPNH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd14077   88 YYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNLYDPRR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 P-HASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRMTltvnVELPDTFSPELKSL 424
Cdd:cd14077  168 LlRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAkIKKGK----VEYPSYLSSECKSL 243
                        250       260
                 ....*....|....*....|....*...
gi 148539879 425 LEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14077  244 ISRMLVVDPKKRATL-----EQVLNHPW 266
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
194-401 4.05e-21

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: 93.33  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  194 HRIIGRGGFGEVY-GCRKADTGKMY---AMKCLdkKRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:pfam07714   4 GEKLGEGAFGEVYkGTLKGEGENTKikvAVKTL--KEGADEEEREDFLEEaSIMKKL----DHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  269 FILDLMNGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSKKKP 347
Cdd:pfam07714  78 IVTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLS-RDIYDDD 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  348 HASVGTHG-----YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFRQHKTKDKHE 401
Cdd:pfam07714 157 YYRKRGGGklpikWMAPESLKDGK-FTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLE 215
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
190-454 5.11e-21

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: 94.02  E-value: 5.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd06655   20 KYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKE---LIINEILVMKELKN---PNIVNFLDSFLVGDELFV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQhGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd06655   94 VMEYLAGGSLTDVVTE-TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 S--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEG 427
Cdd:cd06655  173 StmVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNR 251
                        250       260
                 ....*....|....*....|....*..
gi 148539879 428 LLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd06655  252 CLEMDVEKR-----GSAKELLQHPFLK 273
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
197-436 5.61e-21

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: 92.72  E-value: 5.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKrikMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQH----PQYITLHDTYESPTSYILVLELMDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH---GHARISDLGLACDFS-KKKPHASVG 352
Cdd:cd14115   74 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISgHRHVHHLLG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDTF----SPELKSLLEGL 428
Cdd:cd14115  154 NPEFAAPEVIQ-GTPVSLATDIWSIGVLTYVMLSGVSPFLD---ESKEETCINVCRVDFSFPDEYfgdvSQAARDFINVI 229

                 ....*...
gi 148539879 429 LQRDVSKR 436
Cdd:cd14115  230 LQEDPRRR 237
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
196-453 5.89e-21

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: 93.49  E-value: 5.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKM-KQGETLA-LNERIMLSLVSTGDCPFIVCMTYAFHTPD-----KLC 268
Cdd:cd07838    6 EIGEGAYGTVYKARDLQDGRFVALKKV---RVPLsEEGIPLStIREIALLKQLESFEHPNVVRLLDVCHGPRtdrelKLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGgDLHYHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd07838   83 LVFEHVDQ-DLATYLDKCpkPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSFEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS-VGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLT-------VNVELP-DT 416
Cdd:cd07838  162 ALTSvVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQlGKIFDVIGLpseeewpRNSALPrSS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 417 FS-----------PEL----KSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07838  241 FPsytprpfksfvPEIdeegLDLLKKMLTFNPHKRI-----SAFEALQHPYF 287
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
195-474 6.00e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 94.89  E-value: 6.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL-----DKKRIKMKQgetlalneriMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:PLN00034  80 NRIGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVRRQICR----------EIEILRDVNHPNVVKCHDMFDHNGEIQV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLhyhlSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK-KP- 347
Cdd:PLN00034 150 LLEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTmDPc 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEV----LQKGtAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKTKDKHEID-RMTLTVNVELPDTFSPEL 421
Cdd:PLN00034 226 NSSVGTIAYMSPERintdLNHG-AYDGYAgDIWSLGVSILEFYLGRFPFGVGRQGDWASLMcAICMSQPPEAPATASREF 304
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 422 KSLLEGLLQRDVSKRLgchggGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPR 474
Cdd:PLN00034 305 RHFISCCLQREPAKRW-----SAMQLLQHPFILRAQPGQGQGGPNLHQLLPPP 352
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
189-437 6.30e-21

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: 93.06  E-value: 6.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVH--RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSLVSTgdcPFIVCMTYAFHTPDK 266
Cdd:cd14190    2 STFSIHskEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKE---MVLLEIQVMNQLNH---RNLIQLYEAIETPNE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDL-------HYHLSqhgvfsEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL-DEHGH-ARISDLG 337
Cdd:cd14190   76 IVLFMEYVEGGELferivdeDYHLT------EVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFS-KKKPHASVGTHGYMAPEVLQKGTAYDSSADWfSLGCMLFKLLRGHSPFRQhktkdkheiDRMTLTVNVEL--- 413
Cdd:cd14190  150 LARRYNpREKLKVNFGTPEFLSPEVVNYDQVSFPTDMW-SMGVITYMLLSGLSPFLG---------DDDTETLNNVLmgn 219
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148539879 414 ----PDTF---SPELKSLLEGLLQRDVSKRL 437
Cdd:cd14190  220 wyfdEETFehvSDEAKDFVSNLIIKERSARM 250
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
197-437 7.28e-21

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: 93.54  E-value: 7.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKIIDKS--KRDPSEEIEI-------LLRYGQHPNIITLKDVYDDGKFVYLVMELMRG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA---RISDLGLAcdfskKKPHASVG 352
Cdd:cd14178   82 GELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNPesiRICDFGFA-----KQLRAENG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 -------THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP----DTFSPEL 421
Cdd:cd14178  157 llmtpcyTANFVAPEVLKR-QGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSggnwDSISDAA 235
                        250
                 ....*....|....*.
gi 148539879 422 KSLLEGLLQRDVSKRL 437
Cdd:cd14178  236 KDIVSKMLHVDPHQRL 251
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
195-436 1.16e-20

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: 92.77  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL--------DKKRIKMKQgetlALNE-RIMLSLvstgDCPFIVCMTYAF-HTP 264
Cdd:cd13990    6 NLLGKGGFSEVYKAFDLVEQRYVACKIHqlnkdwseEKKQNYIKH----ALREyEIHKSL----DHPRIVKLYDVFeIDT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLDE---HGHARISDLGLA 339
Cdd:cd13990   78 DSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSgnvSGEIKITDFGLS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKPHAS--------VGTHGYMAPEVLQKGTAY---DSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTL 407
Cdd:cd13990  158 KIMDDESYNSDgmeltsqgAGTYWYLPPECFVVGKTPpkiSSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAIlEENTILK 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148539879 408 TVNVELPD--TFSPELKSLLEGLLQRDVSKR 436
Cdd:cd13990  238 ATEVEFPSkpVVSSEAKDFIRRCLTYRKEDR 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
187-454 1.18e-20

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: 93.20  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGE-----------TLALNER----IMLSLVSTG-- 249
Cdd:cd07845    5 SVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALK-----KVRMDNERdgipisslreiTLLLNLRhpniVELKEVVVGkh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 250 -DCPFIVcMTYAFHtpdKLCFILDLMNGgdlhyhlsqhgVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH 328
Cdd:cd07845   80 lDSIFLV-MEYCEQ---DLASLLDNMPT-----------PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 329 GHARISDLGLACDFSKKKPHAS--VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLrGHSPFRQHKTkdkhEIDRMT 406
Cdd:cd07845  145 GCLKIADFGLARTYGLPAKPMTpkVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELL-AHKPLLPGKS----EIEQLD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 407 LTVNV-------------ELPDTFSPELK-------------------SLLEGLLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd07845  220 LIIQLlgtpnesiwpgfsDLPLVGKFTLPkqpynnlkhkfpwlseaglRLLNFLLMYDPKKR-----ATAEEALESSYFK 294
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
189-437 1.21e-20

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: 92.39  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKL 267
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsRRGVSREDIER-EVSILKEIQHPNVITLHEVYENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI-LLDE---HGHARISDLGLA--CD 341
Cdd:cd14194   84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRnvpKPRIKIIDFGLAhkID 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FSKKKPHAsVGTHGYMAPEVLQkgtaYDS---SADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTF- 417
Cdd:cd14194  164 FGNEFKNI-FGTPEFVAPEIVN----YEPlglEADMWSIGVITYILLSGASPFL---GDTKQETLANVSAVNYEFEDEYf 235
                        250       260
                 ....*....|....*....|...
gi 148539879 418 ---SPELKSLLEGLLQRDVSKRL 437
Cdd:cd14194  236 sntSALAKDFIRRLLVKDPKKRM 258
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
191-437 1.41e-20

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: 91.94  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14196    7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsRRGVSREEIER-EVSILRQVLHPNIITLHDVYENRTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI-LLDEHG---HARISDLGLACDFSKK 345
Cdd:cd14196   86 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIEDG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASV-GTHGYMAPEVLQkgtaYDS---SADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDTF---S 418
Cdd:cd14196  166 VEFKNIfGTPEFVAPEIVN----YEPlglEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVSYDFDEEFfshT 238
                        250       260
                 ....*....|....*....|
gi 148539879 419 PEL-KSLLEGLLQRDVSKRL 437
Cdd:cd14196  239 SELaKDFIRKLLVKETRKRL 258
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
188-440 1.44e-20

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: 91.88  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMK------CLDKKRIKmkqgetlalNErimLSLVSTGDCPFIVCMTYAF 261
Cdd:cd14114    1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKfimtphESDKETVR---------KE---IQIMNQLHHPKLINLHDAF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 HTPDKLCFILDLMNGGDLHYHLS-QHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD--EHGHARISDLGL 338
Cdd:cd14114   69 EDDNEMVLILEFLSGGELFERIAaEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 AcdfSKKKPHASV----GTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktkdKHEIDRMTLTvNVELP 414
Cdd:cd14114  149 A---THLDPKESVkvttGTAEFAAPEIVE-REPVGFYTDMWAVGVLSYVLLSGLSPF-------AGENDDETLR-NVKSC 216
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148539879 415 D---------TFSPELKSLLEGLLQRDVSKRLGCH 440
Cdd:cd14114  217 DwnfddsafsGISEEAKDFIRKLLLADPNKRMTIH 251
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
151-454 1.61e-20

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: 92.48  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 151 EEICESLRgDIFQKFMESDKFTRFCQwknvelnihltmnefsvhriIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK 230
Cdd:cd06654    3 EEILEKLR-SIVSVGDPKKKYTRFEK--------------------IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKK 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 231 QgetLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQhGVFSEKEMRFYATEIILGLEHMHN 310
Cdd:cd06654   62 E---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHS 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 311 RFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGH 388
Cdd:cd06654  135 NQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGE 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 389 SPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd06654  214 PPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR-----GSAKELLQHQFLK 274
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
196-426 2.44e-20

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: 91.20  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVY-GCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14148    1 IIGVGGFGKVYkGLWRGEEVAVKAAR-QDPDEDIAVTAENVRQEARLFWMLQH----PNIIALRGVCLNPPHLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVV---YRDLKPANILLDEHGH--------ARISDLGLACDFS 343
Cdd:cd14148   76 RGGALNRALAGKKV-PPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEPIEnddlsgktLKITDFGLAREWH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRqhktkdkhEIDRMTLTVNVEL-------PDT 416
Cdd:cd14148  155 KTTKMSAAGTYAWMAPEVI-RLSLFSKSSDVWSFGVLLWELLTGEVPYR--------EIDALAVAYGVAMnkltlpiPST 225
                        250
                 ....*....|
gi 148539879 417 FSPELKSLLE 426
Cdd:cd14148  226 CPEPFARLLE 235
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
197-436 2.56e-20

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: 91.19  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQ----VTHE---LGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA---RISDLGLACDF-SKKKPHASVG 352
Cdd:cd14113   88 GRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKptiKLADFGDAVQLnTTYYIHQLLG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTvnveLPDTF----SPELKSLLEG 427
Cdd:cd14113  168 SPEFAAPEIIL-GNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETcLNICRLDFS----FPDDYfkgvSQKAKDFVCF 242

                 ....*....
gi 148539879 428 LLQRDVSKR 436
Cdd:cd14113  243 LLQMDPAKR 251
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
197-436 2.60e-20

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: 91.61  E-value: 2.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLvstGDCPFIVCMTYAFH-----TPDKLCFIL 271
Cdd:cd06638   26 IGKGTYGKVFKVLNKKNGSKAAVKILDPIH---DIDEEIEAEYNILKAL---SDHPNVVKFYGMYYkkdvkNGDQLWLVL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGG---DLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF--SKK 345
Cdd:cd06638  100 ELCNGGsvtDLVKGFLKRGeRMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLtsTRL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQ-HKTKDKHEIDRmTLTVNVELPDTFSPE 420
Cdd:cd06638  180 RRNTSVGTPFWMAPEVIaceqQLDSTYDARCDVWSLGITAIELGDGDPPLADlHPMRALFKIPR-NPPPTLHQPELWSNE 258
                        250
                 ....*....|....*.
gi 148539879 421 LKSLLEGLLQRDVSKR 436
Cdd:cd06638  259 FNDFIRKCLTKDYEKR 274
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
197-418 2.65e-20

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: 91.52  E-value: 2.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGETLALNERIMLSLvsTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14198   16 LGRGKFAVVRQCISKSTGQEYAAKFL-KKRRRGQDCRAEILHEIAVLEL--AKSNPRVVNLHEVYETTSEIILILEYAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE---HGHARISDLGLacdfSKKKPHAS- 350
Cdd:cd14198   93 GEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDIKIVDFGM----SRKIGHACe 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 351 ----VGTHGYMAPEVLQkgtaYD---SSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELP-DTFS 418
Cdd:cd14198  169 lreiMGTPEYLAPEILN----YDpitTATDMWNIGVIAYMLLTHESPF---VGEDNQETFLNISQVNVDYSeETFS 237
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
197-452 3.11e-20

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: 91.62  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14177   12 IGVGSYSVCKRCIHRATNMEFAVKIIDKS--KRDPSEEIEI-------LMRYGQHPNIITLKDVYDDGRYVYLVTELMKG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA---RISDLGLAcdfskKKPHASVG 352
Cdd:cd14177   83 GELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANAdsiRICDFGFA-----KQLRGENG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 -------THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP----DTFSPEL 421
Cdd:cd14177  158 llltpcyTANFVAPEVLMR-QGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSggnwDTVSDAA 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148539879 422 KSLLEGLLQRDVSKRLgchggGSQEVKEHSF 452
Cdd:cd14177  237 KDLLSHMLHVDPHQRY-----TAEQVLKHSW 262
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
197-454 3.20e-20

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: 91.33  E-value: 3.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMkqgeTLALNE--RIMLSL-VS--TGDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd06617    9 LGRGAYGVVDKMRHVPTGTIMAVK-----RIRA----TVNSQEqkRLLMDLdISmrSVDCPYTVTFYGALFREGDVWICM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGG--DLHYHLSQHGVFSEKE-MRFYATEIILGLEHMHNRF-VVYRDLKPANILLDEHGHARISDLGLA---CDFSK 344
Cdd:cd06617   80 EVMDTSldKFYKKVYDKGLTIPEDiLGKIAVSIVKALEYLHSKLsVIHRDVKPSNVLINRNGQVKLCDFGISgylVDSVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHAsvGTHGYMAPEVL---QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHeidrmtLTVNVE-----LP-D 415
Cdd:cd06617  160 KTIDA--GCKPYMAPERInpeLNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQ------LKQVVEepspqLPaE 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148539879 416 TFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd06617  232 KFSPEFQDFVNKCLKKNYKER-----PNYPELLQHPFFE 265
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
197-454 3.38e-20

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 91.48  E-value: 3.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQGE----------TlALNE-RIMLSLvstgDCPFIVCMTYAFHTPD 265
Cdd:cd07841    8 LGEGTYAVVYKARDKETGRIVAIK-------KIKLGErkeakdginfT-ALREiKLLQEL----KHPNIIGLLDVFGHKS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMnGGDLHyhlsqhGVFSEKEMRF-------YATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL 338
Cdd:cd07841   76 NINLVFEFM-ETDLE------KVIKDKSIVLtpadiksYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 ACDF--SKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGhSPFRQHKTkdkhEIDRMTLTVNV----- 411
Cdd:cd07841  149 ARSFgsPNRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLR-VPFLPGDS----DIDQLGKIFEAlgtpt 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 412 --------ELPD--TFSP---------------ELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFFK 454
Cdd:cd07841  224 eenwpgvtSLPDyvEFKPfpptplkqifpaasdDALDLLQRLLTLNPNKRITA-----RQALEHPYFS 286
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
195-436 3.61e-20

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: 90.57  E-value: 3.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgETLALNERIMLSLVSTGDCpfivcMTYAFHTPD-KLCFI-LD 272
Cdd:cd08221    6 RVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKE-RRDALNEIDILSLLNHDNI-----ITYYNHFLDgESLFIeME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS 350
Cdd:cd08221   80 YCNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 --VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTVNV------ELPDTFSPELK 422
Cdd:cd08221  160 siVGTPYYMSPELVQ-GVKYNFKSDIWAVGCVLYELLTLKRTF--------DATNPLRLAVKIvqgeyeDIDEQYSEEII 230
                        250
                 ....*....|....
gi 148539879 423 SLLEGLLQRDVSKR 436
Cdd:cd08221  231 QLVHDCLHQDPEDR 244
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
200-454 4.26e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 90.69  E-value: 4.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 200 GGFGEVYGCRKADTGKMYAmkcldKKRIKMKQGETLALNERIMLSlvstgDCPFIVCMTYAFHTPDKLCFILDLMNGGDL 279
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFV-----QKIIKAKNFNAIEPMVHQLMK-----DNPNFIKLYYSVTTLKGHVLIMDYIKDGDL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 280 HYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH-GHARISDLGLacdfSKKKPHASV--GTHGY 356
Cdd:PHA03390  97 FDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYGL----CKIIGTPSCydGTLDY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 357 MAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTVNVELPDTF----SPELKSLLEGLLQRD 432
Cdd:PHA03390 173 FSPEKI-KGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDE---ELDLESLLKRQQKKLPFiknvSKNANDFVQSMLKYN 248
                        250       260
                 ....*....|....*....|..
gi 148539879 433 VSKRLGCHgggsQEVKEHSFFK 454
Cdd:PHA03390 249 INYRLTNY----NEIIKHPFLK 266
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
191-436 4.80e-20

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: 90.14  E-value: 4.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI------KMKQGETLALNERIMLSLVSTGDcPFIVCMTYAFHtp 264
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvdtwvRDRKLGTVPLEIHILDTLNKRSH-PNIVKLLDFFE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLM---NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD 341
Cdd:cd14004   79 DDEFYYLVMEkhgSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FSKKKPHASVGTHGYMAPEVLqKGTAYDSSA-DWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRmTLTVNVELPDTFSPE 420
Cdd:cd14004  159 IKSGPFDTFVGTIDYAAPEVL-RGNPYGGKEqDIWALGVLLYTLVFKENPF--------YNIEE-ILEADLRIPYAVSED 228
                        250
                 ....*....|....*.
gi 148539879 421 LKSLLEGLLQRDVSKR 436
Cdd:cd14004  229 LIDLISRMLNRDVGDR 244
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
189-410 6.11e-20

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: 90.09  E-value: 6.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLALNERIMLSLVSTGDCPfIVCMTYAFHTPDKLC 268
Cdd:cd06646    9 HDYELIQRVGSGTYGDVYKARNLHTGELAAVKI-----IKLEPGDDFSLIQQEIFMVKECKHCN-IVAYFGSYLSREKLW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLH--YHLSqhGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK- 345
Cdd:cd06646   83 ICMEYCGGGSLQdiYHVT--GPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATi 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 -KPHASVGTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKL-----------------LRGHSPFRQHKTKDK------ 399
Cdd:cd06646  161 aKRKSFIGTPYWMAPEVaaVEKNGGYNQLCDIWAVGITAIELaelqppmfdlhpmralfLMSKSNFQPPKLKDKtkwsst 240
                        250
                 ....*....|..
gi 148539879 400 -HEIDRMTLTVN 410
Cdd:cd06646  241 fHNFVKISLTKN 252
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-391 6.52e-20

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: 90.25  E-value: 6.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYG-CRKADTGKMYAMKcldkkRIKMKQgetLALNERIMLSLVSTGDC-------------PFIV 255
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKvRKKSNGQTLLALK-----EINMTN---PAFGRTEQERDKSVGDIisevniikeqlrhPNIV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 256 CMTYAFHTPDKLCFILDLMNGGDLHYHLS----QHGVFSEKEMRFYATEIILGLEHMHN-RFVVYRDLKPANILLDEHGH 330
Cdd:cd08528   73 RYYKTFLENDRLYIVMELIEGAPLGEHFSslkeKNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDK 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 331 ARISDLGLA----CDFSKKKphASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd08528  153 VTITDFGLAkqkgPESSKMT--SVVGTILYSCPEIVQN-EPYGEKADIWALGCILYQMCTLQPPF 214
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
151-454 7.49e-20

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: 90.55  E-value: 7.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 151 EEICESLRgDIFQKFMESDKFTRFCQwknvelnihltmnefsvhriIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK 230
Cdd:cd06656    2 EEILEKLR-SIVSVGDPKKKYTRFEK--------------------IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKK 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 231 QgetLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQhGVFSEKEMRFYATEIILGLEHMHN 310
Cdd:cd06656   61 E---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 311 RFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGH 388
Cdd:cd06656  134 NQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGE 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 389 SPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd06656  213 PPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRR-----GSAKELLQHPFLK 273
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
190-452 7.98e-20

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: 89.85  E-value: 7.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEV-YGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIM--LSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd14076    2 PYILGRTLGEGEFGKVkLGWPLPKANHRSGVQVAIKLIRRDTQQEN-CQTSKIMreINILKGLTHPNIVRLLDVLKTKKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd14076   81 IGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 P---HASVGTHGYMAPEVLQKGTAYD-SSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRM-TLTVNVEL--PDTFS 418
Cdd:cd14076  161 GdlmSTSCGSPCYAAPELVVSDSMYAgRKADIWSCGVILYAMLAGYLPFdDDPHNPNGDNVPRLyRYICNTPLifPEYVT 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 419 PELKSLLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14076  241 PKARDLLRRILVPNPRKRIRL-----SAIMRHAW 269
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
190-436 1.09e-19

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: 89.03  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKH----PNIVSYKESFEGEDGFLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 I-LDLMNGGDLHYHL-SQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd08223   77 IvMGFCEGGDLYTRLkEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS--VGTHGYMAPEvLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNV-ELPDTFSPELKS 423
Cdd:cd08223  157 DMATtlIGTPYYMSPE-LFSNKPYNHKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYKILEGKLpPMPKQYSPELGE 232
                        250
                 ....*....|...
gi 148539879 424 LLEGLLQRDVSKR 436
Cdd:cd08223  233 LIKAMLHQDPEKR 245
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
197-454 1.14e-19

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: 90.10  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMD---LRKQQRRELLFNEVVIMRDYHHEN---VVDMYNSYLVGDELWVVMEFLEG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS--VGTH 354
Cdd:cd06658  104 GAL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKslVGTP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd06658  183 YWMAPEVISR-LPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLRGFLDLMLVREPS 261
                        250       260
                 ....*....|....*....|
gi 148539879 435 KRlgchgGGSQEVKEHSFFK 454
Cdd:cd06658  262 QR-----ATAQELLQHPFLK 276
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
196-436 1.48e-19

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: 88.99  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgcRKADTGKMYAMKCLdKKRIKMKQGETLA--LNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14061    1 VIGVGGFGKVY--RGIWRGEEVAVKAA-RQDPDEDISVTLEnvRQEARLFWMLRH---PNIIALRGVCLQPPNLCLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRfYATEIILGLEHMHNR---FVVYRDLKPANILLDE--------HGHARISDLGLACDF 342
Cdd:cd14061   75 ARGGALNRVLAGRKIPPHVLVD-WAIQIARGMNYLHNEapvPIIHRDLKSSNILILEaienedleNKTLKITDFGLAREW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRqhktkdkhEID-----------RMTLTVNV 411
Cdd:cd14061  154 HKTTRMSAAGTYAWMAPEVIKSST-FSKASDVWSYGVLLWELLTGEVPYK--------GIDglavaygvavnKLTLPIPS 224
                        250       260
                 ....*....|....*....|....*
gi 148539879 412 ELPDTFspelKSLLEGLLQRDVSKR 436
Cdd:cd14061  225 TCPEPF----AQLMKDCWQPDPHDR 245
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
197-454 1.55e-19

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: 88.83  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKE---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQhGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KKKPHASVGTH 354
Cdd:cd06647   89 GSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRSTMVGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd06647  168 YWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVE 246
                        250       260
                 ....*....|....*....|
gi 148539879 435 KRlgchgGGSQEVKEHSFFK 454
Cdd:cd06647  247 KR-----GSAKELLQHPFLK 261
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
191-378 1.89e-19

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: 88.13  E-value: 1.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQGETLALNERIMlslvSTGDCPFIVCMTYAFHTPDKLcF 269
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKrSRSRFRGEKDRKRKLEEVERHE----KLGEHPNCVRFIKAWEEKGIL-Y 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH- 348
Cdd:cd14050   78 IQTELCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHd 157
                        170       180       190
                 ....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQkGTaYDSSADWFSLG 378
Cdd:cd14050  158 AQEGDPRYMAPELLQ-GS-FTKAADIFSLG 185
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
197-452 2.77e-19

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: 88.43  E-value: 2.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADtGKMYAMKC--LDKKRIKMKQGetlALNERIMLSLVStgDCPFIVCMtYAFHTPDKLCFILDLM 274
Cdd:cd14131    9 LGKGGSSKVYKVLNPK-KKIYALKRvdLEGADEQTLQS---YKNEIELLKKLK--GSDRIIQL-YDYEVTDEDDYLYMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGG--DLHYHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEhGHARISDLGLACDFSKKKPH-- 348
Cdd:cd14131   82 ECGeiDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAIQNDTTSiv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 --ASVGTHGYMAPEVLQKGTAYDS---------SADWFSLGCMLFKLLRGHSPFrQHKTKDKHEIDRMT-LTVNVELPDT 416
Cdd:cd14131  161 rdSQVGTLNYMSPEAIKDTSASGEgkpkskigrPSDVWSLGCILYQMVYGKTPF-QHITNPIAKLQAIIdPNHEIEFPDI 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148539879 417 FSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd14131  240 PNPDLIDVMKRCLQRDPKKRPSI-----PELLNHPF 270
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
189-453 3.39e-19

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: 88.53  E-value: 3.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQGET------LALNERIMLSLVSTgdcPFIVCMTYAFH 262
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIK-------KFKESEDdedvkkTALREVKVLRQLRH---ENIVNLKEAFR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd07833   71 RKGRLYLVFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARAL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHA---SVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF---------------------RQHKTKD 398
Cdd:cd07833  151 TARPASPltdYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFpgdsdidqlyliqkclgplppSHQELFS 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 399 KHEIDRMTLTVNVELPDT--------FSPELKSLLEGLLQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:cd07833  231 SNPRFAGVAFPEPSQPESlerrypgkVSSPALDFLKACLRMDPKERLTCD-----ELLQHPYF 288
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
197-457 3.92e-19

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: 88.27  E-value: 3.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCL--DKKRIKMKQgetlALNErimLSLVSTGDCPFIVCMTYAF-HTPDKLCFILDL 273
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVIhiDAKSSVRKQ----ILRE---LQILHECHSPYIVSFYGAFlNENNNIIICMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF-VVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVG 352
Cdd:cd06620   86 MDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHrIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSIADTFVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTL------TVNVELP-----DTFSPEL 421
Cdd:cd06620  166 TSTYMSPERIQ-GGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGIldllqrIVNEPPPrlpkdRIFPKDL 244
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148539879 422 KSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFKGVD 457
Cdd:cd06620  245 RDFVDRCLLKDPRER-----PSPQLLLDHDPFIQAV 275
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
197-396 4.41e-19

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: 88.27  E-value: 4.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQGETLALNERIMLSL-----VSTGDCP---FIVcmtyafhTPDKL 267
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkCRQELSPSDKNRERWCLEVQIMKKLnhpnvVSARDVPpelEKL-------SPNDL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFI-LDLMNGGDLHYHLSQHGVFS---EKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA---RISDLGLAC 340
Cdd:cd13989   74 PLLaMEYCSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRviyKLIDLGYAK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 341 DFSKKKPHAS-VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKT 396
Cdd:cd13989  154 ELDQGSLCTSfVGTLQYLAPELF-ESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQ 209
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
191-436 4.70e-19

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: 87.74  E-value: 4.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQGETLALNERIMLSLVSTgdcPFIV-CMTYAFHT---PDK 266
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALK---KILCHSKEDVKEAMREIENYRLFNH---PNILrLLDSQIVKeagGKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFI-LDLMNGGDLHYHL---SQHGVF-SEKEMRFYATEIILGLEHMHN---RFVVYRDLKPANILLDEHGHARISDLG- 337
Cdd:cd13986   76 EVYLlLPYYKRGSLQDEIerrLVKGTFfPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGs 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 --LACDFSKKKPHASV--------GTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDR 404
Cdd:cd13986  156 mnPARIEIEGRREALAlqdwaaehCTMPYRAPELfdVKSHCTIDEKTDIWSLGCTLYALMYGESPFeRIFQKGDSLALAV 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 405 MTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd13986  236 LSGNYSFPDNSRYSEELHQLVKSMLVVNPAER 267
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
196-452 4.88e-19

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: 87.49  E-value: 4.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgCRKADTGKMYAMK--CLDKKRIKMKQGETLALNERIML--SLVSTGDCPFI-VCMTyafhtpDKLCFI 270
Cdd:cd06631    8 VLGKGAYGTVY-CGLTSTGQLIAVKqvELDTSDKEKAEKEYEKLQEEVDLlkTLKHVNIVGYLgTCLE------DNVVSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 -LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA---CDFSKKK 346
Cdd:cd06631   81 fMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAkrlCINLSSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASV-----GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhktkdkhEIDRMTLTVNV--------EL 413
Cdd:cd06631  161 SQSQLlksmrGTPYWMAPEVINE-TGHGRKSDIWSIGCTVFEMATGKPPWA--------DMNPMAAIFAIgsgrkpvpRL 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148539879 414 PDTFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSF 452
Cdd:cd06631  232 PDKFSPEARDFVHACLTRDQDERP-----SAEQLLKHPF 265
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
197-436 5.36e-19

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: 87.98  E-value: 5.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETlALNERIM-LSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd06622    9 LGKGNYGSVYKVLHRPTGVTMAMK-----EIRLELDES-KFNQIIMeLDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGD---LHYHLSQHGVFSEKEMRFYATEIILGLEHM---HNrfVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd06622   83 AGSldkLYAGGVATEGIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLAKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKGTA-----YDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEidrmTLTVNVE-----LPDTFSP 419
Cdd:cd06622  161 NIGCQSYMAPERIKSGGPnqnptYTVQSDVWSLGLSILEMALGRYPYPPETYANIFA----QLSAIVDgdpptLPSGYSD 236
                        250
                 ....*....|....*..
gi 148539879 420 ELKSLLEGLLQRDVSKR 436
Cdd:cd06622  237 DAQDFVAKCLNKIPNRR 253
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
197-438 5.87e-19

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: 87.71  E-value: 5.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETL---ALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDL 273
Cdd:cd07870    8 LGEGSYATVYKGISRINGQLVALKV-----ISMKTEEGVpftAIREASLLKGLKHAN---IVLLHDIIHTKETLTFVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGgDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdFSKKKP----H 348
Cdd:cd07870   80 MHT-DLAQYMIQHpGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLA--RAKSIPsqtyS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGhSPFRQHKTKDKHEIDRMTLTVNVELPDT---------FSP 419
Cdd:cd07870  157 SEVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQG-QPAFPGVSDVFEQLEKIWTVLGVPTEDTwpgvsklpnYKP 235
                        250
                 ....*....|....*....
gi 148539879 420 ELKSLLEGLLQRDVSKRLG 438
Cdd:cd07870  236 EWFLPCKPQQLRVVWKRLS 254
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
196-452 6.97e-19

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: 87.08  E-value: 6.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQG--ETLALNERI-------MLSLVSTGDcpfiVCMTYAFHTPdk 266
Cdd:cd06624   15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPlhEEIALHSRLshknivqYLGSVSEDG----FFKIFMEQVP-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 lcfildlmnGGDLHYHL-SQHGVFSEKE--MRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH-GHARISDLGLACDF 342
Cdd:cd06624   89 ---------GGSLSALLrSKWGPLKDNEntIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYsGVVKISDFGTSKRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASV--GTHGYMAPEVLQKGT-AYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSP 419
Cdd:cd06624  160 AGINPCTETftGTLQYMAPEVIDKGQrGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMFKIHPEIPESLSE 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148539879 420 ELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSF 452
Cdd:cd06624  240 EAKSFILRCFEPDPDKR-----ATASDLLQDPF 267
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
197-391 7.26e-19

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: 87.35  E-value: 7.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGE----TLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFI-- 270
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALK-----KIRLETEDegvpSTAIRE---ISLLKELNHPNIVRLLDVVHSENKLYLVfe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 -LDLmnggDLHYHLSQHGVFSEKEMRF--YATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS---K 344
Cdd:cd07835   79 fLDL----DLKKYMDSSPLTGLDPPLIksYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGvpvR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 345 KKPHASVgTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd07835  155 TYTHEVV-TLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLF 200
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
197-453 7.56e-19

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: 87.39  E-value: 7.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMD---LRKQQRRELLFNEVVIMRDYQHEN---VVEMYNSYLVGDELWVVMEFLEG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS--VGTH 354
Cdd:cd06657  102 GAL-TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKslVGTP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd06657  181 YWMAPELISR-LPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPA 259
                        250
                 ....*....|....*....
gi 148539879 435 KRlgchgGGSQEVKEHSFF 453
Cdd:cd06657  260 QR-----ATAAELLKHPFL 273
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
195-395 7.78e-19

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: 87.06  E-value: 7.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLD---KKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYafHTPDKLCFIL 271
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD--RAEKTLTIFM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA------CdFSKK 345
Cdd:cd06651   91 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkrlqtiC-MSGT 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK 395
Cdd:cd06651  170 GIRSVTGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 218
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
191-453 9.49e-19

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 86.76  E-value: 9.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDcpfIVCMTYAFHTPD-KLCF 269
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKS---IIKTYEIFETSDgKVYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGlacdFSKKKPHA 349
Cdd:cd14165   80 VMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFG----FSKRCLRD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 S----------VGTHGYMAPEVLQkGTAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTVNVELPDT-- 416
Cdd:cd14165  156 EngrivlsktfCGSAAYAAPEVLQ-GIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVK---KMLKIQKEHRVRFPRSkn 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148539879 417 FSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14165  232 LTSECKDLIYRLLQPDVSQRLCI-----DEVLSHPWL 263
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
197-404 1.01e-18

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 87.36  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLvstGDCPFIVCMTYAFHTPDK-----LCFIL 271
Cdd:cd06639   30 IGKGTYGKVYKVTNKKDGSLAAVKILDPIS---DVDEEIEAEYNILRSL---PNHPNVVKFYGMFYKADQyvggqLWLVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGG---DLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KK 345
Cdd:cd06639  104 ELCNGGsvtELVKGLLKCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTsaRL 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539879 346 KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSP-FRQHKTKDKHEIDR 404
Cdd:cd06639  184 RRNTSVGTPFWMAPEVIaceqQYDYSYDARCDVWSLGITAIELADGDPPlFDMHPVKALFKIPR 247
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
191-436 1.28e-18

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: 86.10  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLR----SSTRARAFQERDILARLSH---RRLTCLLDQFETRKTLILI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGHARISDLGLACDFSKKKPH 348
Cdd:cd14107   77 LELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 AS-VGTHGYMAPEVLQKGTAYDSSADWfSLGCMLFKLLRGHSPFrqhktkdKHEIDRMTL------TVNVELPD--TFSP 419
Cdd:cd14107  157 FSkYGSPEFVAPEIVHQEPVSAATDIW-ALGVIAYLSLTCHSPF-------AGENDRATLlnvaegVVSWDTPEitHLSE 228
                        250
                 ....*....|....*..
gi 148539879 420 ELKSLLEGLLQRDVSKR 436
Cdd:cd14107  229 DAKDFIKRVLQPDPEKR 245
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
190-392 1.30e-18

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: 86.24  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYgcRKADTGKMYAMKCldKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14147    4 ELRLEEVIGIGGFGKVY--RGSWRGELVAVKA--ARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRF---VVYRDLKPANILLD--------EHGHARISDLGL 338
Cdd:cd14147   80 VMEYAAGGPLSRALAGRRV-PPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLqpienddmEHKTLKITDFGL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148539879 339 ACDFSKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd14147  159 AREWHKTTQMSAAGTYAWMAPEVI-KASTFSKGSDVWSFGVLLWELLTGEVPYR 211
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
197-394 1.56e-18

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: 85.90  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYgcRKADTGKMYAMKCLDK--KRIKMKQ---GETLALNER-------IMLSLVSTGDCPFIVCMTYAfhtp 264
Cdd:cd13979   11 LGSGGFGSVY--KATYKGETVAVKIVRRrrKNRASRQsfwAELNAARLRhenivrvLAAETGTDFASLGLIIMEYC---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 dklcfildlmNGGDLHYHL--SQHGVFSEKEMRfYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLG---LA 339
Cdd:cd13979   85 ----------GNGTLQQLIyeGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsvKL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKPHASV--GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPF---RQH 394
Cdd:cd13979  154 GEGNEVGTPRSHigGTYTYRAPELL-KGERVTPKADIYSFGITLWQMLTRELPYaglRQH 212
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
197-453 2.05e-18

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: 85.39  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNE-RIMLSLvstgDCPFIVCMTYAFHTPD--KLCFILD 272
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLrRIPNGEANVKREiQILRRL----NHRNVIKLVDVLYNEEkqKLYMVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGdlhyhlSQHGVFSEKEMRF-------YATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd14119   77 YCVGG------LQEMLDSAPDKRLpiwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KP----HASVGTHGYMAPEVLQKGTAYDS-SADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRMTLTVnvelPDTFSP 419
Cdd:cd14119  151 AEddtcTTSQGSPAFQPPEIANGQDSFSGfKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFEnIGKGEYTI----PDDVDP 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 420 ELKSLLEGLLQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:cd14119  227 DLQDLLRGMLEKDPEKRFTIE-----QIRQHPWF 255
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
190-436 2.15e-18

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 85.75  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIMLSLVstGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14139    1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIK-RSMRPFAGSSNEQLALHEVYAHAVL--GHHPHVVRYYSAWAEDDHMII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHG----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL------------------DE 327
Cdd:cd14139   78 QNEYCNGGSLQDAISENTksgnHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIchkmqsssgvgeevsneeDE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 328 HGHA----RISDLGLACDFSkkKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGcMLFKLLRGHSPFrQHKTKDKHEID 403
Cdd:cd14139  158 FLSAnvvyKIGDLGHVTSIN--KPQVEEGDSRFLANEILQEDYRHLPKADIFALG-LTVALAAGAEPL-PTNGAAWHHIR 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 404 RMTL-TVNVELPDTFspelKSLLEGLLQRDVSKR 436
Cdd:cd14139  234 KGNFpDVPQELPESF----SSLLKNMIQPDPEQR 263
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
197-453 2.39e-18

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: 86.19  E-value: 2.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMD---LRKQQRRELLFNEVVIMRDYQH---PNVVEMYKSYLVGEELWVLMEYLQG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP--HASVGTH 354
Cdd:cd06659  103 GALTDIVSQTR-LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPkrKSLVGTP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVS 434
Cdd:cd06659  182 YWMAPEVISR-CPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVLRDFLERMLVRDPQ 260
                        250
                 ....*....|....*....
gi 148539879 435 KRlgchgGGSQEVKEHSFF 453
Cdd:cd06659  261 ER-----ATAQELLDHPFL 274
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
197-436 2.49e-18

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: 85.45  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgetlALNERIMLSLvSTGDCPFIVcMTY--AFHTPDKLCFILDLM 274
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLK-----DFLREYNISL-ELSVHPHII-KTYdvAFETEDYYVFAQEYA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHL-SQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISdlglACDFSKKKPHASV-- 351
Cdd:cd13987   74 PYGDLFSIIpPQVGL-PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVK----LCDFGLTRRVGSTvk 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 ---GTHGYMAPEVLQ----KGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK--HEIDRMTLTVNVELPDT---FSP 419
Cdd:cd13987  149 rvsGTIPYTAPEVCEakknEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQfyEEFVRWQKRKNTAVPSQwrrFTP 228
                        250
                 ....*....|....*..
gi 148539879 420 ELKSLLEGLLQRDVSKR 436
Cdd:cd13987  229 KALRMFKKLLAPEPERR 245
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
195-437 3.01e-18

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: 85.43  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL-DKKRIKMKqgetlalnerIMLSLVSTGdCPFIVCMTYAF----HTPDKLCF 269
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALKLLyDSPKARRE----------VEHHWRASG-GPHIVHILDVYenmhHGKRCLLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHARISDLGLACDFSK 344
Cdd:cd14172   79 IMECMEGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKP-HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD-----KHEIdRMTltvNVELPD--- 415
Cdd:cd14172  159 QNAlQTPCYTPYYVAPEVLGP-EKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAispgmKRRI-RMG---QYGFPNpew 233
                        250       260
                 ....*....|....*....|...
gi 148539879 416 -TFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14172  234 aEVSEEAKQLIRHLLKTDPTERM 256
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
197-472 5.09e-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: 5.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKMKQgetlALNERIMLSLVSTGDC--PFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06650   13 LGAGNGGVVFKVSHKPSGLVMARKLI---HLEIKP----AIRNQIIRELQVLHECnsPYIVGFYGAFYSDGEISICMEHM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF-VVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGT 353
Cdd:cd06650   86 DGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkheidrmtltvnVELPDTFSPELKSLLEGLLQRDV 433
Cdd:cd06650  166 RSYMSPERLQ-GTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKE------------LELMFGCQVEGDAAETPPRPRTP 232
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148539879 434 SKRLGCHGGGSQevKEHSFFKGVDwqhvYLQKYPPPLIP 472
Cdd:cd06650  233 GRPLSSYGMDSR--PPMAIFELLD----YIVNEPPPKLP 265
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
195-437 6.48e-18

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: 84.26  E-value: 6.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERimlslvsTGDCPFIVCM--TYA--FHTPDKLCFI 270
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNP---KARREVELHWR-------ASGCPHIVRIidVYEntYQGRKCLLVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLglaCDFS-KKKP 347
Cdd:cd14089   77 MECMEGGELFSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKL---TDFGfAKET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVG------THGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDT---- 416
Cdd:cd14089  154 TTKKSlqtpcyTPYYVAPEVLGPEK-YDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKKRIRNGQYEFPNPewsn 232
                        250       260
                 ....*....|....*....|.
gi 148539879 417 FSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14089  233 VSEEAKDLIRGLLKTDPSERL 253
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
196-381 6.80e-18

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: 83.81  E-value: 6.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQgetLALNERIML----SLVSTGDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd13983    8 VLGRGSFKTVYRAFDTEEGIEVAWN-----EIKLRK---LPKAERQRFkqeiEILKSLKHPNIIKFYDSWESKSKKEVIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 --DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLD-EHGHARISDLGLACDFSKKK 346
Cdd:cd13983   80 itELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQSF 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148539879 347 PHASVGTHGYMAPEVLQKGtaYDSSADWFSLG-CML 381
Cdd:cd13983  160 AKSVIGTPEFMAPEMYEEH--YDEKVDIYAFGmCLL 193
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
191-453 1.12e-17

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: 83.47  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGetlaLNERIMLSLVSTGDCP---FIVCMTYAFHTPDKL 267
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQS----LDEIRLLELLNKKDKAdkyHIVRLKDVFYFKNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDL--MNGGDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS--DLGLACdFS 343
Cdd:cd14133   77 CIVFELlsQNLYEFLKQNKFQY-LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKiiDFGSSC-FL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkhEIDRMTLTVNveLPDTF------ 417
Cdd:cd14133  155 TQRLYSYIQSRYYRAPEVIL-GLPYDEKIDMWSLGCILAELYTGEPLFPGASEVD--QLARIIGTIG--IPPAHmldqgk 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148539879 418 --SPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd14133  230 adDELFVDFLKKLLEIDPKERP-----TASQALSHPWL 262
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
194-394 1.14e-17

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: 83.71  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 194 HRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMkqgETLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd13991   11 QLRIGRGSFGEVHRMEDKQTGFQCAVK-----KVRL---EVFRAEE---LMACAGLTSPRVVPLYGAVREGPWVNIFMDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG-HARISDLGLACDFSKKKPHASV- 351
Cdd:cd13991   80 KEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPDGLGKSLf 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 352 ------GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQH 394
Cdd:cd13991  160 tgdyipGTETHMAPEVV-LGKPCDAKVDVWSSCCMMLHMLNGCHPWTQY 207
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
191-439 1.24e-17

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: 83.13  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlalNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKE------NIRQEISIMNCLHHPKLVQCVDAFEEKANIVMV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA-RISDLGLACDF-SKKK 346
Cdd:cd14191   78 LEMVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTKiKLIDFGLARRLeNAGS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDTFSPELKSLL 425
Cdd:cd14191  158 LKVLFGTPEFVAPEVINY-EPIGYATDMWSIGVICYILVSGLSPFMgDNDNETLANVTSATWDFDDEAFDEISDDAKDFI 236
                        250
                 ....*....|....
gi 148539879 426 EGLLQRDVSKRLGC 439
Cdd:cd14191  237 SNLLKKDMKARLTC 250
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
194-441 1.32e-17

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: 83.09  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 194 HRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQ---GETLALNERIMLSLVSTGDcpfivcmtyAFHTPDKLCFI 270
Cdd:cd14192    9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREevkNEINIMNQLNHVNLIQLYD---------AFESKTNLTLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDL-------HYHLSqhgvfsEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHA-RISDLGLACD 341
Cdd:cd14192   80 MEYVDGGELfdritdeSYQLT------ELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNQiKIIDFGLARR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FS-KKKPHASVGTHGYMAPEVLQkgtaYDSSA---DWFSLGCMLFKLLRGHSPFRqhktkDKHEIDRMTLTVNVEL---P 414
Cdd:cd14192  154 YKpREKLKVNFGTPEFLAPEVVN----YDFVSfptDMWSVGVITYMLLSGLSPFL-----GETDAETMNNIVNCKWdfdA 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 415 DTF---SPELKSLLEGLLQRDVSKRLGCHG 441
Cdd:cd14192  225 EAFenlSEEAKDFISRLLVKEKSCRMSATQ 254
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
197-391 1.73e-17

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: 84.16  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkrikMKQGETLALNERIM--LSLVSTGDCPFIVCMTYAFHTP-DKLCFILDL 273
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKKI------MKPFSTPVLAKRTYreLKLLKHLRHENIISLSDIFISPlEDIYFVTEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MnGGDLHYHLSQHGVfsEKE-MRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdfSKKKPHAS-- 350
Cdd:cd07856   92 L-GTDLHRLLTSRPL--EKQfIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLA---RIQDPQMTgy 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148539879 351 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd07856  166 VSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLF 206
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
184-392 1.82e-17

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: 83.17  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 184 IHLTMNEFSVHRIIGRGGFGEVYgcRKADTGKMYAMKCLdKKRIKMKQGETLAlNERIMLSLVSTGDCPFIVCMTYAFHT 263
Cdd:cd14145    1 LEIDFSELVLEEIIGIGGFGKVY--RAIWIGDEVAVKAA-RHDPDEDISQTIE-NVRQEAKLFAMLKHPNIIALRGVCLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRfYATEIILGLEHMHNRFVV---YRDLKPANILL---DEHGHA-----R 332
Cdd:cd14145   77 EPNLCLVMEFARGGPLNRVLSGKRIPPDILVN-WAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekVENGDLsnkilK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 333 ISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd14145  156 ITDFGLAREWHRTTKMSAAGTYAWMAPEVIRSSM-FSKGSDVWSYGVLLWELLTGEVPFR 214
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
190-455 2.04e-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: 83.95  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkriKMKQG-ETLALNERIM--LSLVSTGDCPFIVCMTYAFHTP-- 264
Cdd:cd07855    6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIK-------KIPNAfDVVTTAKRTLreLKILRHFKHDNIIAIRDILRPKvp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 ----DKLCFILDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA- 339
Cdd:cd07855   79 yadfKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMAr 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKPHAS-----VGTHGYMAPEVLQKGTAYDSSADWFSLGC----MLFK--LLRGHSPFRQHK-------TKDKHE 401
Cdd:cd07855  158 GLCTSPEEHKYfmteyVATRWYRAPELMLSLPEYTQAIDMWSVGCifaeMLGRrqLFPGKNYVHQLQliltvlgTPSQAV 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 402 IDRM------TLTVN------VELPDTF---SPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFKG 455
Cdd:cd07855  238 INAIgadrvrRYIQNlpnkqpVPWETLYpkaDQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAK 301
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
197-437 2.83e-17

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: 82.36  E-value: 2.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKM-KQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSsRRGVSREEIER-EVNILREIQHPNIITLHDIFENKTDVVLILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI-LLDEHG---HARISDLGLACDFSKKKPHASV 351
Cdd:cd14195   92 GGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVpnpRIKLIDFGIAHKIEAGNEFKNI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 -GTHGYMAPEVLQkgtaYDS---SADWFSLGCMLFKLLRGHSPFR-QHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLE 426
Cdd:cd14195  172 fGTPEFVAPEIVN----YEPlglEADMWSIGVITYILLSGASPFLgETKQETLTNISAVNYDFDEEYFSNTSELAKDFIR 247
                        250
                 ....*....|.
gi 148539879 427 GLLQRDVSKRL 437
Cdd:cd14195  248 RLLVKDPKKRM 258
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
197-424 2.88e-17

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: 83.20  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKMKQGETL-ALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd07869   13 LGEGSYATVYKGKSKVNGKLVALKVI---RLQEEEGTPFtAIREASLLKGLKHAN---IVLLHDIIHTKETLTLVFEYVH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GgDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdFSKKKPHAS---- 350
Cdd:cd07869   87 T-DLCQYMDKHpGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA--RAKSVPSHTysne 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539879 351 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdKHEIDRMTLTVNVELPDTFsPELKSL 424
Cdd:cd07869  164 VVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDI-QDQLERIFLVLGTPNEDTW-PGVHSL 235
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
196-426 3.58e-17

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: 82.01  E-value: 3.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgcRKADTGKMYAMKCldKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14146    1 IIGVGGFGKVY--RATWKGQEVAVKA--ARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLS-QHGVFSEKEMRF--------YATEIILGLEHMHNRFVV---YRDLKPANILL------DEHGHA--RISD 335
Cdd:cd14146   77 GGTLNRALAaANAAPGPRRARRipphilvnWAVQIARGMLYLHEEAVVpilHRDLKSSNILLlekiehDDICNKtlKITD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 336 LGLACDFSKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFR---QHKTKDKHEIDRMTLTVNVE 412
Cdd:cd14146  157 FGLAREWHRTTKMSAAGTYAWMAPEVI-KSSLFSKGSDIWSYGVLLWELLTGEVPYRgidGLAVAYGVAVNKLTLPIPST 235
                        250
                 ....*....|....
gi 148539879 413 LPDTFSPELKSLLE 426
Cdd:cd14146  236 CPEPFAKLMKECWE 249
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
197-437 3.90e-17

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: 82.17  E-value: 3.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldKKRI--KMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd07860    8 IGEGTYGVVYKARNKLTGEVVALK---KIRLdtETEGVPSTAIRE---ISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGgDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS---KKKPHA 349
Cdd:cd07860   82 HQ-DLKKFMdaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGvpvRTYTHE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVgTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVN-------VELPD------ 415
Cdd:cd07860  161 VV-TLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQlFRIFRTLGTPDevvwpgvTSMPDykpsfp 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148539879 416 ------------TFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd07860  240 kwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRI 273
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
197-454 4.60e-17

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: 81.83  E-value: 4.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGETLALNERImlSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKF-----VKVKGADQVLVKKEI--SILNIARHRNILRLHESFESHEELVMIFEFISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH--GHARISDLGLACDFskkKPHASVG- 352
Cdd:cd14104   81 VDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQL---KPGDKFRl 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 ---THGYMAPEVLQKGTAyDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-IDRMTLTVNVELPDTFSPELKSLLEGL 428
Cdd:cd14104  158 qytSAEFYAPEVHQHESV-STATDMWSLGCLVYVLLSGINPFEAETNQQTIEnIRNAEYAFDDEAFKNISIEALDFVDRL 236
                        250       260
                 ....*....|....*....|....*.
gi 148539879 429 LQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:cd14104  237 LVKERKSRM-----TAQEALNHPWLK 257
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
197-453 4.61e-17

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: 81.59  E-value: 4.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGETLALNERI-MLSLVSTgdcPFIVCMTYAFHTPDK--LCFIL-- 271
Cdd:cd14033    9 IGRGSFKTVY--RGLDTETTVEVAWCELQTRKLSKGERQRFSEEVeMLKGLQH---PNIVRFYDSWKSTVRghKCIILvt 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLD-EHGHARISDLGLACDFSKKKPH 348
Cdd:cd14033   84 ELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHEIDRmTLTVNVElPDTFS----PELKSL 424
Cdd:cd14033  164 SVIGTPEFMAPEMYEE--KYDEAVDVYAFGMCILEMATSEYPYSE--CQNAAQIYR-KVTSGIK-PDSFYkvkvPELKEI 237
                        250       260
                 ....*....|....*....|....*....
gi 148539879 425 LEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14033  238 IEGCIRTDKDERFTI-----QDLLEHRFF 261
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
188-441 4.65e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 85.56  E-value: 4.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIvcMTYAFHTPDKL 267
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYI--DRFLNKANQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  268 CFILDLMNGGDLHYHLSQ----HGVFSEKEMRFYATEIILGLEHMHN-------RFVVYRDLKPANILLDE--------- 327
Cdd:PTZ00266   90 YILMEFCDAGDLSRNIQKcykmFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTgirhigkit 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  328 ------HGH--ARISDLGLACDFS-KKKPHASVGTHGYMAPEVLQKGT-AYDSSADWFSLGCMLFKLLRGHSPFrqHKTK 397
Cdd:PTZ00266  170 aqannlNGRpiAKIGDFGLSKNIGiESMAHSCVGTPYYWSPELLLHETkSYDDKSDMWALGCIIYELCSGKTPF--HKAN 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 148539879  398 DKHEIDRmTLTVNVELP-DTFSPELKSLLEGLLQRDVSKR---LGCHG 441
Cdd:PTZ00266  248 NFSQLIS-ELKRGPDLPiKGKSKELNILIKNLLNLSAKERpsaLQCLG 294
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
197-391 4.74e-17

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: 81.50  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14110   11 INRGRFSVVRQCEEKRSGQMLAAKIIPYK----PEDKQLVLREYQVLRRLSH---PRIAQLHSAYLSPRHLVLIEELCSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTHGY 356
Cdd:cd14110   84 PELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDY 163
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148539879 357 ---MAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14110  164 vetMAPELLE-GQGAGPQTDIWAIGVTAFIMLSADYPV 200
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
196-436 5.47e-17

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: 81.15  E-value: 5.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgcRKADTGKMYAMKCLDKKrikmkQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLcfILDLMN 275
Cdd:cd14068    1 LLGDGGFGSVY--RAVYRGEDVAVKIFNKH-----TSFRLLRQELVVLSHLHH---PSLVALLAAGTAPRML--VMELAP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHyHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL-----DEHGHARISDLGLACDFSKKKPH 348
Cdd:cd14068   69 KGSLD-ALLQQdnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 349 ASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQhKTKDKHEIDRmtLTVNVELPDTFS-------PEL 421
Cdd:cd14068  148 TSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTCGERIVE-GLKFPNEFDE--LAIQGKLPDPVKeygcapwPGV 224
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:cd14068  225 EALIKDCLKENPQCR 239
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
190-436 7.60e-17

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: 81.05  E-value: 7.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRI----KMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPD 265
Cdd:cd14101    1 QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVqqwsKLPGVNPVPNEVALLQSVGGGPGHRGVIRLLDWFEIPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDL-MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLACDFs 343
Cdd:cd14101   81 GFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASV-GTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQhktkdkheiDRMTLTVNVELPDTFSPELK 422
Cdd:cd14101  160 KDSMYTDFdGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFER---------DTDILKAKPSFNKRVSNDCR 230
                        250
                 ....*....|....
gi 148539879 423 SLLEGLLQRDVSKR 436
Cdd:cd14101  231 SLIRSCLAYNPSDR 244
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
197-405 8.14e-17

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: 81.59  E-value: 8.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQGE-TLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALK---EIRLEHEEGApCTAIRE---VSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GgDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdFSKKKPHAS---- 350
Cdd:cd07871   87 S-DLKQYLDNCGnLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA--RAKSVPTKTysne 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 351 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRM 405
Cdd:cd07871  164 VVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEElHLIFRL 219
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
197-391 1.55e-16

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: 80.23  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADtGKMYAMKCLDKKRikmKQGETLALNERI-MLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14664    1 IGRGGAGTVYKGVMPN-GTLVAVKRLKGEG---TQGGDHGFQAEIqTLGMIRHRN---IVRLRGYCSNPTTNLLVYEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVFSEK---EMRF-YATEIILGLEHMHNR---FVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd14664   74 NGSLGELLHSRPESQPPldwETRQrIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSH 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 349 AS---VGTHGYMAPEVLQKGTAyDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14664  154 VMssvAGSYGYIAPEYAYTGKV-SEKSDVYSYGVVLLELITGKRPF 198
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
197-391 2.22e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 80.96  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGET-------------LALNE-RIMLSLvstgDCPFIVCMTYAFH 262
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKV--KIIEISNDVTkdrqlvgmcgihfTTLRElKIMNEI----KHENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCFILDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:PTZ00024  91 EGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRY 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 343 ---------SKKKPHAS-------VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:PTZ00024 170 gyppysdtlSKDETMQRreemtskVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLF 234
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
190-436 2.27e-16

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: 79.84  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETlalnERIMLSLVSTgDCPFIV----CMTYAFHTPD 265
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIK-----RVKLNNEKA----EREVKALAKL-DHPNIVryngCWDGFDYDPE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 -----------KLCFI-LDLMNGGDLH-----------YHLSQHGVFSEkemrfyateIILGLEHMHNRFVVYRDLKPAN 322
Cdd:cd14047   77 tsssnssrsktKCLFIqMEFCEKGTLEswiekrngeklDKVLALEIFEQ---------ITKGVEYIHSKKLIHRDLKPSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 323 ILLDEHGHARISDLGLACDFSKKKPHA-SVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLrghspfrqHKTKDKHE 401
Cdd:cd14047  148 IFLVDTGKVKIGDFGLVTSLKNDGKRTkSKGTLSYMSPEQISSQD-YGKEVDIYALGLILFELL--------HVCDSAFE 218
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148539879 402 IDRMTLTV-NVELPDTFSPELK---SLLEGLLQRDVSKR 436
Cdd:cd14047  219 KSKFWTDLrNGILPDIFDKRYKiekTIIKKMLSKKPEDR 257
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
197-385 2.63e-16

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: 79.07  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkrikmkqgETLALNERIMLSLVSTGDC---PFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKE-----------LKRFDEQRSFLKEVKLMRRlshPNILRFIGVCVKDNKLNFITEY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR---ISDLGLA--------CD 341
Cdd:cd14065   70 VNGGTLEELLKSMDEqLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLArempdektKK 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148539879 342 FSKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd14065  150 PDRKKRLTVVGSPYWMAPEML-RGESYDEKVDVFSFGIVLCEII 192
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
197-405 3.01e-16

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: 79.96  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKM-KQGETL---ALNE-RIMLSLV-------------STGDCPFIVcMT 258
Cdd:cd07843   13 IEEGTYGVVYRARDKKTGEIVALK-----KLKMeKEKEGFpitSLREiNILLKLQhpnivtvkevvvgSNLDKIYMV-ME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 259 YAFHtpdKLCFILDLMNGGdlhyhlsqhgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL 338
Cdd:cd07843   87 YVEH---DLKSLMETMKQP-----------FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 339 ACDF-SKKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRM 405
Cdd:cd07843  153 AREYgSPLKPYTQlVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLF-----PGKSEIDQL 216
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
197-453 3.12e-16

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: 79.38  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGETLALNERImlSLVSTGDCPFIVCMTYAFHT--PDKLCFIL--D 272
Cdd:cd14031   18 LGRGAFKTVY--KGLDTETWVEVAWCELQDRKLTKAEQQRFKEEA--EMLKGLQHPNIVRFYDSWESvlKGKKCIVLvtE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLD-EHGHARISDLGLACDFSKKKPHA 349
Cdd:cd14031   94 LMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTSFAKS 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHEIDRmTLTVNVElPDTFS----PELKSLL 425
Cdd:cd14031  174 VIGTPEFMAPEMYEE--HYDESVDVYAFGMCMLEMATSEYPYSE--CQNAAQIYR-KVTSGIK-PASFNkvtdPEVKEII 247
                        250       260
                 ....*....|....*....|....*...
gi 148539879 426 EGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14031  248 EGCIRQNKSERLSI-----KDLLNHAFF 270
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
197-431 4.00e-16

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: 79.62  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMK-CldKKRIKMKQGETLALNERIMLSL-----VSTGDCPFIVcmtYAFHTPDKLCFI 270
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKqC--RQELSPKNRERWCLEIQIMKRLnhpnvVAARDVPEGL---QKLAPNDLPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQH----GVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGHAR----ISDLGLACDF 342
Cdd:cd14038   77 MEYCQGGDLRKYLNQFenccGL-REGAILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGEQRlihkIIDLGYAKEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHAS-VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF-------RQH-KTKDKHEIDrmtLTVNVEL 413
Cdd:cd14038  155 DQGSLCTSfVGTLQYLAPELLEQ-QKYTVTVDYWSFGTLAFECITGFRPFlpnwqpvQWHgKVRQKSNED---IVVYEDL 230
                        250       260
                 ....*....|....*....|....*.
gi 148539879 414 PDT--FSP------ELKSLLEGLLQR 431
Cdd:cd14038  231 TGAvkFSSvlptpnNLNGILAGKLER 256
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
197-472 4.44e-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: 80.09  E-value: 4.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKMKQgetlALNERIMLSLVSTGDC--PFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06649   13 LGAGNGGVVTKVQHKPSGLIMARKLI---HLEIKP----AIRNQIIRELQVLHECnsPYIVGFYGAFYSDGEISICMEHM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF-VVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGT 353
Cdd:cd06649   86 DGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI-DRMTLTVNVELPDTFSPElksllegllQRD 432
Cdd:cd06649  166 RSYMSPERLQ-GTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIfGRPVVDGEEGEPHSISPR---------PRP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148539879 433 VSKRLGCHGGGSQEVKehSFFKGVDwqhvYLQKYPPPLIP 472
Cdd:cd06649  236 PGRPVSGHGMDSRPAM--AIFELLD----YIVNEPPPKLP 269
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
197-475 5.13e-16

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: 79.40  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKMKQgetlALNERIMLSLVSTGDC--PFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd06615    9 LGAGNGGVVTKVLHRPSGLIMARKLI---HLEIKP----AIRNQIIRELKVLHECnsPYIVGFYGAFYSDGEISICMEHM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMH-NRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGT 353
Cdd:cd06615   82 DGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMtltvnvelpdtFSPELKSLLEGLLQRDV 433
Cdd:cd06615  162 RSYMSPERLQ-GTHYTVQSDIWSLGLSLVEMAIGRYPI---PPPDAKELEAM-----------FGRPVSEGEAKESHRPV 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 148539879 434 SkrlgchGGGSQEVKEHSFFKGVDwqhvYLQKYPPPLIPPRG 475
Cdd:cd06615  227 S------GHPPDSPRPMAIFELLD----YIVNEPPPKLPSGA 258
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
197-380 5.38e-16

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: 79.00  E-value: 5.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGE----TLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd07861    8 IGEGTYGVVYKGRNKKTGQIVAMK-----KIRLESEEegvpSTAIRE---ISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGgDLHYHLSQ--HGVFSEKE-MRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS---KKK 346
Cdd:cd07861   80 FLSM-DLKKYLDSlpKGKYMDAElVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGipvRVY 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 148539879 347 PHASVgTHGYMAPEVLQKGTAYDSSADWFSLGCM 380
Cdd:cd07861  159 THEVV-TLWYRAPEVLLGSPRYSTPVDIWSIGTI 191
RGS cd07440
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ...
59-173 5.49e-16

Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.


Pssm-ID: 188659 [Multi-domain]  Cd Length: 113  Bit Score: 74.35  E-value: 5.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  59 FNQKIGFLLFKDFCLNEINEAVpqVKFYEEIKEYEKLDNEED-RLCRSRQIYDAYIMKELlSCSHPFSKQAVEHVQSHLS 137
Cdd:cd07440    1 LRDPYGLEYFRQFLKSEHCEEN--LEFWLAVEKFKKTTSSDEeLKSKAKEIYDKYISKDA-PKEINIPESIREEIEENLE 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 148539879 138 KKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTR 173
Cdd:cd07440   78 EPYPDPDCFDEAQEHILNLLEKDSYPRFLKSDLYLK 113
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
196-393 8.76e-16

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: 78.38  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKC--LDKkrikmkqgeTLALNERIM--LSLVSTGDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd06619    8 ILGHGNGGTVYKAYHLLTRRILAVKVipLDI---------TVELQKQIMseLEILYKCDSPYIIGFYGAFFVENRISICT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLhyhlSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV 351
Cdd:cd06619   79 EFMDGGSL----DVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYV 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148539879 352 GTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQ 393
Cdd:cd06619  155 GTNAYMAPERIS-GEQYGIHSDVWSLGISFMELALGRFPYPQ 195
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
188-436 1.02e-15

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: 77.93  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAF------ 261
Cdd:cd14049    5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGL----QHPNIVGYHTAWmehvql 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 --HTPDKLCFiLDLMNGGDLHYHLSQHGVFSEKEMRFYATEIIL--------GLEHMHNRFVVYRDLKPANILLdeHG-- 329
Cdd:cd14049   81 mlYIQMQLCE-LSLWDWIVERNKRPCEEEFKSAPYTPVDVDVTTkilqqlleGVTYIHSMGIVHRDLKPRNIFL--HGsd 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 330 -HARISDLGLAC--------DFSKKKPHAS------VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRghsPFrqh 394
Cdd:cd14049  158 iHVRIGDFGLACpdilqdgnDSTTMSRLNGlthtsgVGTCLYAAPEQLE-GSHYDFKSDMYSIGVILLELFQ---PF--- 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148539879 395 kTKDKHEIDRMTLTVNVELPDTFS---PELKSLLEGLLQRDVSKR 436
Cdd:cd14049  231 -GTEMERAEVLTQLRNGQIPKSLCkrwPVQAKYIKLLTSTEPSER 274
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
300-453 1.35e-15

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 77.31  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 300 EIILGLEHMHNRFVVYRDLKPANILLD---EHGHAR--ISDLGLacdfSKK----------KPHASvGTHGYMAPEVLQK 364
Cdd:cd13982  107 QIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRamISDFGL----CKKldvgrssfsrRSGVA-GTSGWIAPEMLSG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 365 GTAYDSSA--DWFSLGCMLFKLL-RGHSPF-----RQHKTKdKHEIDRMTLTVNVElpdtFSPELKSLLEGLLQRDVSKR 436
Cdd:cd13982  182 STKRRQTRavDIFSLGCVFYYVLsGGSHPFgdkleREANIL-KGKYSLDKLLSLGE----HGPEAQDLIERMIDFDPEKR 256
                        170
                 ....*....|....*..
gi 148539879 437 lgchgGGSQEVKEHSFF 453
Cdd:cd13982  257 -----PSAEEVLNHPFF 268
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
197-430 1.63e-15

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: 77.65  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIM-----LSLVSTGDCPfiVCMTYAFHtpDKLCFIL 271
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIK-SCRLELSVKNKDRWCHEIQIMkklnhPNVVKACDVP--EEMNFLVN--DVPLLAM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGV---FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA---RISDLGLACDFSKK 345
Cdd:cd14039   76 EYCSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGYAKDLDQG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHAS-VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQH----------KTKDKHEI---DRMT----L 407
Cdd:cd14039  156 SLCTSfVGTLQYLAPELFE-NKSYTVTVDYWSFGTMVFECIAGFRPFLHNlqpftwhekiKKKDPKHIfavEEMNgevrF 234
                        250       260
                 ....*....|....*....|...
gi 148539879 408 TVNVELPDTFSPELKSLLEGLLQ 430
Cdd:cd14039  235 STHLPQPNNLCSLIVEPMEGWLQ 257
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
189-446 2.20e-15

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: 76.60  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 268
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKR--DGRKVRKAAKNEINILKMVKH---PNILQLVDVFETRKEYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD---EHGHARISDLGLACDFSK- 344
Cdd:cd14088   76 IFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKLENGl 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 -KKPhasVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-----IDRMTLTVNVELP---- 414
Cdd:cd14088  156 iKEP---CGTPEYLAPEVVGR-QRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknLFRKILAGDYEFDspyw 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 415 DTFSPELKSLLEGLLQRDVSKRLGCHGGGSQE 446
Cdd:cd14088  232 DDISQAAKDLVTRLMEVEQDQRITAEEAISHE 263
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
197-453 2.82e-15

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: 76.75  E-value: 2.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKMKQGE-TLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIVALKEI---HLDAEEGTpSTAIRE---ISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GgDLHYHLSQHGV---FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KKKPHAS 350
Cdd:cd07836   82 K-DLKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGipVNTFSNE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVN-------VELPD------- 415
Cdd:cd07836  161 VVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQlLKIFRIMGTPTestwpgiSQLPEykptfpr 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 416 -----------TFSPELKSLLEGLLQRDVSKRLGCHgggsqEVKEHSFF 453
Cdd:cd07836  241 yppqdlqqlfpHADPLGIDLLHRLLQLNPELRISAH-----DALQHPWF 284
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
197-391 2.84e-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: 76.32  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADtgkmyamkcldkKRIKMKQGETLALNERIMLSL--VSTGDCPFIVCMTYAFHTPDKLCFILDLM 274
Cdd:cd14058    1 VGRGSFGVVCKARWRN------------QIVAVKIIESESEKKAFEVEVrqLSRVDHPNIIKLYGACSNQKPVCLVMEYA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLsqHG------VFSEKEMRfYATEIILGLEHMHN---RFVVYRDLKPANILLDEHGHA-RISDLGLACDFSK 344
Cdd:cd14058   69 EGGSLYNVL--HGkepkpiYTAAHAMS-WALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDIST 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 345 KKPHASvGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14058  146 HMTNNK-GSAAWMAPEVFE-GSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
197-453 3.25e-15

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 76.97  E-value: 3.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQGE-TLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALK---EIRLEHEEGApCTAIREVSLLKDLKHAN---IVTLHDIIHTEKSLTLVFEYLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GgDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KKKPHASVG 352
Cdd:cd07873   84 K-DLKQYLDDCGnSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSipTKTYSNEVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVEL------------------ 413
Cdd:cd07873  163 TLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQlHFIFRILGTPTEETwpgilsneefksynypky 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 148539879 414 -PDTF---SPELKS----LLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07873  243 rADALhnhAPRLDSdgadLLSKLLQFEGRKRI-----SAEEAMKHPYF 285
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
197-399 3.30e-15

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: 76.61  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAmkCLDKKRIKM-KQGETLA-LNERIMLSLVSTGDCP-----FIVCMTYAFHTPDKLCF 269
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGGRFV--ALKRVRVQTgEEGMPLStIREVAVLRHLETFEHPnvvrlFDVCTVSRTDRETKLTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGgDLHYHLSQ---HGVFSE--KEMRFyatEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd07862   87 VFEHVDQ-DLTTYLDKvpePGVPTEtiKDMMF---QLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSF 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 345 KKPHAS-VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd07862  163 QMALTSvVVTLWYRAPEVLLQ-SSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQ 217
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
191-454 3.34e-15

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: 76.68  E-value: 3.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLD---------KKRIKMKQGETLALNERIMLSLVSTGDCPFIvcmtyaf 261
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDvtgdeeeeiKQEINMLKKYSHHRNIATYYGAFIKKNPPGM------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 htPDKLCFILDLMNGGDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd06637   81 --DDQLWLVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKK--KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNVEL 413
Cdd:cd06637  159 AQLDRTvgRRNTFIGTPYWMAPEVIacdeNPDATYDFKSDLWSLGITAIEMAEGAPPL-----CDMHPMRALFLIPRNPA 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148539879 414 P----DTFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFK 454
Cdd:cd06637  234 PrlksKKWSKKFQSFIESCLVKNHSQR-----PSTEQLMKHPFIR 273
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
191-393 3.43e-15

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: 75.78  E-value: 3.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVY-GCRKADtGKMYAMKCLDKKRI----KMKQGETLALnERIMLSLVSTGDCPFIVCMTYaFHTPD 265
Cdd:cd14100    2 YQVGPLLGSGGFGSVYsGIRVAD-GAPVAIKHVEKDRVsewgELPNGTRVPM-EIVLLKKVGSGFRGVIRLLDW-FERPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNG-GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLACDFS 343
Cdd:cd14100   79 SFVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLK 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 344 KKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQ 393
Cdd:cd14100  159 DTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEH 208
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
191-391 4.02e-15

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: 76.81  E-value: 4.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL-DKKRIKMKqgetlALNERIMLSLVSTGDCP---FIVCMTYAFHTPDK 266
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIrNKKRFHQQ-----ALVEVKILKHLNDNDPDdkhNIVRYKDSFIFRGH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMnGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS--DLGLACdF 342
Cdd:cd14210   90 LCIVFELL-SINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKviDFGSSC-F 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 343 SKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14210  168 EGEKVYTYIQSRFYRAPEVIL-GLPYDTAIDMWSLGCILAELYTGYPLF 215
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
191-423 4.08e-15

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: 76.20  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDkkrIKMKQGETLALnERIMLSLVSTGDCPFIVCMTYAFHTP----DK 266
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKL-EINMLKKYSHHRNIATYYGAFIKKSPpghdDQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd06636   94 LWLVMEFCGAGSVTDLVknTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 K--KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLtvnveLPDTFS 418
Cdd:cd06636  174 TvgRRNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPL-----CDMHPMRALFL-----IPRNPP 243

                 ....*
gi 148539879 419 PELKS 423
Cdd:cd06636  244 PKLKS 248
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
195-436 4.11e-15

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: 75.99  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL---DKKR-----IKMKQGETLALNERImLSLVSTgdcpfIVCMTYAFHTPDK 266
Cdd:cd13975    6 RELGRGQYGVVYACDSWGGHFPCALKSVvppDDKHwndlaLEFHYTRSLPKHERI-VSLHGS-----VIDYSYGGGSSIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGgDLHYHLsQHGVFSEKEMRFyATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLaCdfskkK 346
Cdd:cd13975   80 VLLIMERLHR-DLYTGI-KAGLSLEERLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGF-C-----K 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS-----VGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGH----SPFRQHKTKDkHEIDRMTLTVNVELPDTF 417
Cdd:cd13975  151 PEAMmsgsiVGTPIHMAPELFSG--KYDNSVDVYAFGILFWYLCAGHvklpEAFEQCASKD-HLWNNVRKGVRPERLPVF 227
                        250
                 ....*....|....*....
gi 148539879 418 SPELKSLLEGLLQRDVSKR 436
Cdd:cd13975  228 DEECWNLMEACWSGDPSQR 246
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
197-386 4.71e-15

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: 76.15  E-value: 4.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkRIKMKQgETLALN---ERIMLSLVSTGDCPFIV-----CMTYAFHTPDKLC 268
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSV---RVQTNE-DGLPLStvrEVALLKRLEAFDHPNIVrlmdvCATSRTDRETKVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGgDLHYHLSQ---HGVFSEKeMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd07863   84 LVFEHVDQ-DLRTYLDKvppPGLPAET-IKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQ 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148539879 346 KP-HASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR 386
Cdd:cd07863  162 MAlTPVVVTLWYRAPEVLLQST-YATPVDMWSVGCIFAEMFR 202
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
197-453 7.39e-15

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: 75.50  E-value: 7.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETL---ALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd07844    8 LGEGSYATVYKGRSKLTGQLVALK-----EIRLEHEEGApftAIRE---ASLLKDLKHANIVTLHDIIHTKKTLTLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGgDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdFSKKKPHAS-- 350
Cdd:cd07844   80 LDT-DLKQYMDDCGgGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA--RAKSVPSKTys 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 --VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHkTKDKHEIDRMTLTVNVELPDTFS---------- 418
Cdd:cd07844  157 neVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGS-TDVEDQLHKIFRVLGTPTEETWPgvssnpefkp 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 419 ---------------------PELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07844  236 ysfpfypprplinhaprldriPHGEELALKFLQYEPKKRI-----SAAEAMKHPYF 286
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
197-395 7.39e-15

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: 74.87  E-value: 7.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYG--CRkadtGKMYAMKCLDKKRIKMKQGETLALNErimLSLVSTGDCPFIVCMTYA-FHTPDKLCFILDL 273
Cdd:cd14064    1 IGSGSFGKVYKgrCR----NKIVAIKRYRANTYCSKSDVDMFCRE---VSILCRLNHPCVIQFVGAcLDDPSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLS-QHGVFSEKEMRFYATEIILGLEHMHN--RFVVYRDLKPANILLDEHGHARISDLG-------LACDFS 343
Cdd:cd14064   74 VSGGSLFSLLHeQKRVIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGesrflqsLDEDNM 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 344 KKKPhasvGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK 395
Cdd:cd14064  154 TKQP----GNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLK 201
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
196-391 9.18e-15

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: 74.95  E-value: 9.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQ---GETLALNERIMLSLVSTGDcpfivcmtyAFHTPDKLCFILD 272
Cdd:cd14193   11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEevkNEIEVMNQLNHANLIQLYD---------AFESRNDIVLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHL-SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGHARISDLGLACDFS-KKKPH 348
Cdd:cd14193   82 YVDGGELFDRIiDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKpREKLR 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 349 ASVGTHGYMAPEVLQkgtaYDSSA---DWFSLGCMLFKLLRGHSPF 391
Cdd:cd14193  162 VNFGTPEFLAPEVVN----YEFVSfptDMWSLGVIAYMLLSGLSPF 203
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
188-450 1.52e-14

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


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 74.53  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLalNERIM--LSLVSTGDCPFIVCMTYAF-HTP 264
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVK-----RIRLPNNELA--REKVLreVRALAKLDHPGIVRYFNAWlERP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DK----------LCFILDLMNGGDLHYHLSQHGVFSEKEmRFYATEIIL----GLEHMHNRFVVYRDLKPANILLDEHGH 330
Cdd:cd14048   78 PEgwqekmdevyLYIQMQLCRKENLKDWMNRRCTMESRE-LFVCLNIFKqiasAVEYLHSKGLIHRDLKPSNVFFSLDDV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 331 ARISDLGLACDFSKKKPHAS--------------VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRghsPFRQHKT 396
Cdd:cd14048  157 VKVGDFGLVTAMDQGEPEQTvltpmpayakhtgqVGTRLYMSPEQI-HGNQYSEKVDIFALGLILFELIY---SFSTQME 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148539879 397 KDKHEIDRMTLTVNVELPDTFsPELKSLLEGLLQRDVSKRLGCHgggsqEVKEH 450
Cdd:cd14048  233 RIRTLTDVRKLKFPALFTNKY-PEERDMVQQMLSPSPSERPEAH-----EVIEH 280
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
197-456 1.71e-14

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: 75.03  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd07872   14 LGEGTYATVFKGRSKLTENLVALK-----EIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 gDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KKKPHASVGT 353
Cdd:cd07872   89 -DLKQYMDDCGnIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSvpTKTYSNEVVT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 354 HGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVEL------------------- 413
Cdd:cd07872  168 LWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDElHLIFRLLGTPTEETwpgissndefknynfpkyk 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 414 PDTF---SPELKS----LLEGLLQRDVSKRLgchggGSQEVKEHSFFKGV 456
Cdd:cd07872  248 PQPLinhAPRLDTegieLLTKFLQYESKKRI-----SAEEAMKHAYFRSL 292
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
249-391 1.79e-14

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 76.76  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 249 GDCPFIVcMTYafhtpdklcfildlMNGGDLHYHLSQHGVFSEKE-MRfYATEIILGLEHMHNRFVVYRDLKPANILLDE 327
Cdd:NF033483  79 GGIPYIV-MEY--------------VDGRTLKDYIREHGPLSPEEaVE-IMIQILSALEHAHRNGIVHRDIKPQNILITK 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 328 HGHARISDLGLACDFSkkkphAS--------VGTHGYMAPEvlQ-KGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:NF033483 143 DGRVKVTDFGIARALS-----STtmtqtnsvLGTVHYLSPE--QaRGGTVDARSDIYSLGIVLYEMLTGRPPF 208
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
187-454 1.94e-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: 74.50  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 187 TMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL---DKKRIKMkqgETLalnerIMLSLVSTgdcPFIVCMTYAFHT 263
Cdd:cd14132   16 SQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkpvKKKKIKR---EIK-----ILQNLRGG---PNIVKLLDVVKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKL--CFILDLMNGGDLhYHLSQhgVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLAc 340
Cdd:cd14132   85 PQSKtpSLIFEYVNNTDF-KTLYP--TLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGLA- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 341 DFSKKKPHAS--VGTHGYMAPEVLQKGTAYDSSADWFSLGCML----FK---LLRGHS---------------------- 389
Cdd:cd14132  161 EFYHPGQEYNvrVASRYYKGPELLVDYQYYDYSLDMWSLGCMLasmiFRkepFFHGHDnydqlvkiakvlgtddlyayld 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 390 ------PFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGCHgggsqEVKEHSFFK 454
Cdd:cd14132  241 kygielPPRLNDILGRHSKKPWERFVNSENQHLVTPEALDLLDKLLRYDHQERITAK-----EAMQHPYFD 306
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
188-384 2.57e-14

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: 74.07  E-value: 2.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRIK-MKQGETL-ALNE-RIMLSLVSTGdcpfIVCMTYAF--- 261
Cdd:cd07864    6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDnEKEGFPItAIREiKILRQLNHRS----VVNLKEIVtdk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 -----HTPDKLCFIL-------DLMngGDLHYHLSQhgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG 329
Cdd:cd07864   79 qdaldFKKDKGAFYLvfeymdhDLM--GLLESGLVH---FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 330 HARISDLGLACDFSK--KKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKL 384
Cdd:cd07864  154 QIKLADFGLARLYNSeeSRPYTNkVITLWYRPPELLLGEERYGPAIDVWSCGCILGEL 211
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
197-436 2.90e-14

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 73.59  E-value: 2.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIMLSLVstGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14051    8 IGSGEFGSVYKCINRLDGCVYAIK-KSKKPVAGSVDEQNALNEVYAHAVL--GKHPHVVRYYSAWAEDDHMIIQNEYCNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQH----GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--------------DEHGHA------- 331
Cdd:cd14051   85 GSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFIsrtpnpvsseeeeeDFEGEEdnpesne 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 332 ---RISDLGLACdfSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFkLLRGHSPFRQHKtKDKHEIDRMtlt 408
Cdd:cd14051  165 vtyKIGDLGHVT--SISNPQVEEGDCRFLANEILQENYSHLPKADIFALALTVY-EAAGGGPLPKNG-DEWHEIRQG--- 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 409 vnvELPD--TFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14051  238 ---NLPPlpQCSPEFNELLRSMIHPDPEKR 264
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
191-437 3.35e-14

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: 74.52  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMK-CLDKKrikmkQGETLAlnER----IMLsLVSTGDCPFIVCMtYAFHTPD 265
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAF-----RNATDA--QRtfreIMF-LQELNDHPNIIKL-LNVIRAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 K---LCFILDLMNGgDLHyHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd07852   80 NdkdIYLVFEYMET-DLH-AVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHAS-------VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRG---------------------------- 387
Cdd:cd07852  158 SQLEEDDEnpvltdyVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGkplfpgtstlnqlekiievigrpsaedi 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 388 ---HSPFRQHKTKDKHEIDRMTLtvnVELPDTFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd07852  238 esiQSPFAATMLESLPPSRPKSL---DELFPKASPDALDLLKKLLVFNPNKRL 287
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
191-436 3.63e-14

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: 73.07  E-value: 3.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVY-GCRKADtGKMYAMKCLDKKRIK---MKQGETLALnERIMLSLVSTGDCPFIVCMTYaFHTPDK 266
Cdd:cd14102    2 YQVGSVLGSGGFGTVYaGSRIAD-GLPVAVKHVVKERVTewgTLNGVMVPL-EIVLLKKVGSGFRGVIKLLDW-YERPDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMN-GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLACDFSK 344
Cdd:cd14102   79 FLIVMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQhktkdkheiDRMTLTVNVELPDTFSPELKSL 424
Cdd:cd14102  159 TVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQ---------DEEILRGRLYFRRRVSPECQQL 229
                        250
                 ....*....|..
gi 148539879 425 LEGLLQRDVSKR 436
Cdd:cd14102  230 IKWCLSLRPSDR 241
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
190-436 3.65e-14

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: 73.14  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMK---CLDKKRIKmkqgetLALNER-IMLSLvstGDCPFIVCM---TYAFH 262
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKrmyFNDEEQLR------VAIKEIeIMKRL---CGHPNIVQYydsAILSS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCFILDLMNGGDLHYHLSQ--HGVFSEKEMRFYATEIILGLEHMH--NRFVVYRDLKPANILLDEHGHARISDLGL 338
Cdd:cd13985   72 EGRKEVLLLMEYCPGSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHsqSPPIIHRDIKIENILFSNTGRFKLCDFGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 339 ACDFSKKKPHAS-VG----------THGYMAPEVLQKGTAY--DSSADWFSLGCMLFKLLRGHSPFrqhktkDKHEIDR- 404
Cdd:cd13985  152 ATTEHYPLERAEeVNiieeeiqkntTPMYRAPEMIDLYSKKpiGEKADIWALGCLLYKLCFFKLPF------DESSKLAi 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148539879 405 MTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd13985  226 VAGKYSIPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
197-399 3.66e-14

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: 72.81  E-value: 3.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYgcrKADTGKMYAMKCLDKKRIKMKQGETLAlNERIMLSlvSTGDCPFIVCMTYAfhTPDKLCFILDLMNG 276
Cdd:cd14062    1 IGSGSFGTVY---KGRWHGDVAVKKLNVTDPTPSQLQAFK-NEVAVLR--KTRHVNILLFMGYM--TKPQLAIVTQWCEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK-------KPH 348
Cdd:cd14062   73 SSLYKHLHVLETkFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWsgsqqfeQPT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 349 ASVgthGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd14062  153 GSI---LWMAPEVirMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQ 202
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
197-390 3.76e-14

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 73.24  E-value: 3.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGE----TLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd07839    8 IGEGTYGTVFKAKNRETHEIVALK-----RVRLDDDDegvpSSALRE---ICLLKELKHKNIVRLYDVLHSDKKLTLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFS--KKKPHAS 350
Cdd:cd07839   80 YCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGipVRCYSAE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 148539879 351 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSP 390
Cdd:cd07839  160 VVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRP 199
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
189-405 4.21e-14

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: 73.49  E-value: 4.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLC 268
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKET-TLRELKMLRTLKQEN---IVELKEAFRRRGKLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYhLSQH--GVFSEKeMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd07848   77 LVFEYVEKNMLEL-LEEMpnGVPPEK-VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGS 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 347 PH---ASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRM 405
Cdd:cd07848  155 NAnytEYVATRWYRSPELLL-GAPYGKAVDMWSVGCILGELSDGQPLF-----PGESEIDQL 210
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
190-436 4.42e-14

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: 73.13  E-value: 4.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQGETLALNERIMLSLVstGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14138    6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAGSVDEQNALREVYAHAVL--GQHSHVVRYYSAWAEDDHMLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQH----GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---------------DEHGH 330
Cdd:cd14138   83 QNEYCNGGSLADAISENyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegdeDEWAS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 331 AR----ISDLGLACDFSkkKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKlLRGHSPFRQHKTKdKHEIDRMT 406
Cdd:cd14138  163 NKvifkIGDLGHVTRVS--SPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVC-AAGAEPLPTNGDQ-WHEIRQGK 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 407 LTvnvELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14138  239 LP---RIPQVLSQEFLDLLKVMIHPDPERR 265
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
185-436 4.87e-14

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: 73.55  E-value: 4.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNE-FSVHRIIGRGGFGEVYGCRKADTGKMYAMKC--LDK--KRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMT 258
Cdd:cd14040    1 HPTLNErYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKswRDEKKENYHKHACREyRIHKEL----DHPRIVKLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 259 YAFH-TPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMH--NRFVVYRDLKPANILLDEH---GHAR 332
Cdd:cd14040   77 DYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 333 ISDLGLACDFSKKK--------PHASVGTHGYMAPEVLQKGT---AYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDKHE 401
Cdd:cd14040  157 ITDFGLSKIMDDDSygvdgmdlTSQGAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDI 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148539879 402 IDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14040  236 LQENTILKATEVQFPVKPVVSNEAKAFIRRCLAYR 270
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
195-426 4.96e-14

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: 73.30  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADtgKMYAMKCLDKKRIKMKQGETLALNERIML-------SLVSTGDCPfivcmtyafHTPDKL 267
Cdd:cd14158   21 NKLGEGGFGVVFKGYIND--KNVAVKKLAAMVDISTEDLTKQFEQEIQVmakcqheNLVELLGYS---------CDGPQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLS--QHGVFSEKEMRFYATE-IILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdfsK 344
Cdd:cd14158   90 CLVYTYMPNGSLLDRLAclNDTPPLSWHMRCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLA----R 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHAS--------VGTHGYMAPEVLQKGTAYDSsaDWFSLGCMLFKLLRGHSPFRQHKT-------KDKHEIDRMTLT- 408
Cdd:cd14158  166 ASEKFSqtimteriVGTTAYMAPEALRGEITPKS--DIFSFGVVLLEIITGLPPVDENRDpqllldiKEEIEDEEKTIEd 243
                        250
                 ....*....|....*....
gi 148539879 409 -VNVELPDTFSPELKSLLE 426
Cdd:cd14158  244 yVDKKMGDWDSTSIEAMYS 262
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
273-392 5.10e-14

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: 73.87  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMnGGDLHyHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA--CDfskKKPHAS 350
Cdd:cd07851  101 LM-GADLN-NIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLArhTD---DEMTGY 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148539879 351 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd07851  176 VATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFP 217
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
191-452 8.13e-14

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: 73.21  E-value: 8.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADT--GKMYAMKCLDK---KRIKMKQgetlALNErIMLsLVSTGDCPFIVC---MTYAFH 262
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITNvfsKKILAKR----ALRE-LKL-LRHFRGHKNITClydMDIVFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TP-DKLCFILDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACD 341
Cdd:cd07857   76 GNfNELYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 342 FS----KKKPHAS--VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNV---- 411
Cdd:cd07857  155 FSenpgENAGFMTeyVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVF-----KGKDYVDQLNQILQVlgtp 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 412 --------------------------ELPDTF---SPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSF 452
Cdd:cd07857  230 deetlsrigspkaqnyirslpnipkkPFESIFpnaNPLALDLLEKLLAFDPTKRISV-----EEALEHPY 294
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
196-453 9.48e-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: 72.79  E-value: 9.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKM---KQGETL-ALNERIMLSLVSTgdcPFIVCMTYAFHTP------D 265
Cdd:cd07865   19 KIGQGTFGEVFKARHRKTGQIVALK-----KVLMeneKEGFPItALREIKILQLLKH---ENVVNLIEICRTKatpynrY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCF--ILDLMNGgDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd07865   91 KGSIylVFEFCEH-DLAGLLSNKNVkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHAS------VGTHGYMAPEVLQKGTAYDSSADWFSLGCML------FKLLRGHSpfRQHK-----------TKDK 399
Cdd:cd07865  170 SLAKNSQPnrytnrVVTLWYRPPELLLGERDYGPPIDMWGAGCIMaemwtrSPIMQGNT--EQHQltlisqlcgsiTPEV 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 400 H-EIDRMTLTVNVELP--------DTFSPELKS-----LLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07865  248 WpGVDKLELFKKMELPqgqkrkvkERLKPYVKDpyaldLIDKLLVLDPAKRI-----DADTALNHDFF 310
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
185-440 1.06e-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: 72.40  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNE-FSVHRIIGRGGFGEVYGCRKADTGKMYAMKC--LDK--KRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMT 258
Cdd:cd14041    1 HPTLNDrYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKnwRDEKKENYHKHACREyRIHKEL----DHPRIVKLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 259 YAFH-TPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHN--RFVVYRDLKPANILL---DEHGHAR 332
Cdd:cd14041   77 DYFSlDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 333 ISDLGLAcDFSKKKPHASV----------GTHGYMAPEVLQKGT---AYDSSADWFSLGCMLFKLLRGHSPFRQHKT-KD 398
Cdd:cd14041  157 ITDFGLS-KIMDDDSYNSVdgmeltsqgaGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSqQD 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148539879 399 KHEIDRMTLTVNVELPDT--FSPELKSLLEGLLQRDVSKRLGCH 440
Cdd:cd14041  236 ILQENTILKATEVQFPPKpvVTPEAKAFIRRCLAYRKEDRIDVQ 279
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
197-453 1.21e-13

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: 72.35  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldkkRIKM---KQGETL-ALNERIMLSLVSTGDCPFIVCMTYAF---HTPDKLCF 269
Cdd:cd07866   16 LGEGTFGEVYKARQIKTGRVVALK-----KILMhneKDGFPItALREIKILKKLKHPNVVPLIDMAVERpdkSKRKRGSV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 --ILDLMNGgDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd07866   91 ymVTPYMDH-DLSGLLENPSVkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDGPP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PH-------------ASVGTHGYMAPEVLQKGTAYDSSADWFSLGCML---FK---LLRGHSPFRQ-HKT---------- 396
Cdd:cd07866  170 PNpkggggggtrkytNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFaemFTrrpILQGKSDIDQlHLIfklcgtptee 249
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 397 -----------KDKHEIDRMTLTVNvELPDTFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07866  250 twpgwrslpgcEGVHSFTNYPRTLE-ERFGKLGPEGLDLLSKLLSLDPYKRL-----TASDALEHPYF 311
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
197-437 1.58e-13

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: 71.00  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkrikMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDK-LCFILDLMN 275
Cdd:cd14109   12 EKRAAQGAPFHVTERSTGRNFLAQL-------RYGDPFLMREVDIHNSL----DHPNIVQMHDAYDDEKLaVTVIDNLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYH--LSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGHARISDLGLACDFSKKKPHASV-G 352
Cdd:cd14109   81 TIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKLTTLIyG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFrqHKTKDKH---EIDRMTLTVNVELPDTFSPELKSLLEGLL 429
Cdd:cd14109  160 SPEFVSPEIV-NSYPVTLATDMWSVGVLTYVLLGGISPF--LGDNDREtltNVRSGKWSFDSSPLGNISDDARDFIKKLL 236

                 ....*...
gi 148539879 430 QRDVSKRL 437
Cdd:cd14109  237 VYIPESRL 244
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
195-401 1.70e-13

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: 70.95  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQgetlALNE-RIMLSLvstGDCPFIvCMTYAFHTPDKL-CFILD 272
Cdd:cd14016    6 KKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSKHPQ----LEYEaKVYKLL---QGGPGI-PRLYWFGQEGDYnVMVMD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMnGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR---ISDLGLAC-------- 340
Cdd:cd14016   77 LL-GPSLEDLFNKCGrKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKkyrdprtg 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 341 ---DFSKKKPH------ASVGTHgymapevlqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE 401
Cdd:cd14016  156 khiPYREGKSLtgtaryASINAH---------LGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKE 216
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
277-453 1.81e-13

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: 70.45  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL-------ACDFSKKKPHa 349
Cdd:cd14022   69 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLedayilrGHDDSLSDKH- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 svGTHGYMAPEVLQKGTAYD-SSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTVNVE-----LPDTFSPELKS 423
Cdd:cd14022  148 --GCPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF--------HDIEPSSLFSKIRrgqfnIPETLSPKAKC 217
                        170       180       190
                 ....*....|....*....|....*....|
gi 148539879 424 LLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd14022  218 LIRSILRREPSERL-----TSQEILDHPWF 242
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
269-391 2.30e-13

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: 72.00  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMnGGDLHyHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDfSKKKPH 348
Cdd:cd07878   97 LVTNLM-GADLN-NIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ-ADDEMT 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 148539879 349 ASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd07878  174 GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALF 216
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
253-386 3.52e-13

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 70.38  E-value: 3.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 253 FIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRF--------VVYRDLKPANIL 324
Cdd:cd14056   54 FIAADIKSTGSWTQLWLITEYHEHGSLYDYLQRNTL-DTEEALRLAYSAASGLAHLHTEIvgtqgkpaIAHRDLKSKNIL 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 325 LDEHGHARISDLGLACDFSKKK------PHASVGTHGYMAPEVLQK---GTAYDS--SADWFSLGCMLFKLLR 386
Cdd:cd14056  133 VKRDGTCCIADLGLAVRYDSDTntidipPNPRVGTKRYMAPEVLDDsinPKSFESfkMADIYSFGLVLWEIAR 205
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
289-453 3.67e-13

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: 71.22  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 289 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSKKKPHASVGTHGYMAPEVLQKGTAY 368
Cdd:cd07877  117 LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA-RHTDDEMTGYVATRWYRAPEIMLNWMHY 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 369 DSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVEL------------------------PDTF---SPE 420
Cdd:cd07877  196 NQTVDIWSVGCIMAELLTGRTLFPGTDHIDQlKLILRLVGTPGAELlkkissesarnyiqsltqmpkmnfANVFigaNPL 275
                        170       180       190
                 ....*....|....*....|....*....|...
gi 148539879 421 LKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07877  276 AVDLLEKMLVLDSDKRI-----TAAQALAHAYF 303
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
191-436 5.57e-13

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: 69.63  E-value: 5.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkqGETLALNERIM---LSLVSTGDCPFIVCMTYAFHTPD-K 266
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKS------GGPEEFIQRFLpreLQIVERLDHKNIIHVYEMLESADgK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGHARISDLGLACDFSKKK 346
Cdd:cd14163   76 IYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 347 PHAS---VGTHGYMAPEVLQkGTAYDS-SADWFSLGCMLFKLLRGHSPFrqhktkDKHEIDRMTLTVN--VELPD--TFS 418
Cdd:cd14163  155 RELSqtfCGSTAYAAPEVLQ-GVPHDSrKGDIWSMGVVLYVMLCAQLPF------DDTDIPKMLCQQQkgVSLPGhlGVS 227
                        250
                 ....*....|....*...
gi 148539879 419 PELKSLLEGLLQRDVSKR 436
Cdd:cd14163  228 RTCQDLLKRLLEPDMVLR 245
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
289-453 6.09e-13

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: 70.70  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 289 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSKKKPHASVGTHGYMAPEVLQKGTAY 368
Cdd:cd07879  114 LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLA-RHADAEMTGYVVTRWYRAPEVILNWMHY 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 369 DSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNV----------------------ELPD----------- 415
Cdd:cd07879  193 NQTVDIWSVGCIMAEMLTGKTLF-----KGKDYLDQLTQILKVtgvpgpefvqkledkaaksyikSLPKyprkdfstlfp 267
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148539879 416 TFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFF 453
Cdd:cd07879  268 KASPQAVDLLEKMLELDVDKRL-----TATEALEHPYF 300
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
191-436 6.12e-13

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: 69.50  E-value: 6.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVygcrKADTGKMY----AMKCLDKKRIKMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDK 266
Cdd:cd14164    2 YTLGTTIGEGSFSKV----KLATSQKYcckvAIKIVDRRRASPDFVQKFLPRE---LSILRRVNHPNIVQMFECIEVANG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG-HARISDLGLAcDFSKK 345
Cdd:cd14164   75 RLYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFA-RFVED 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KP---HASVGTHGYMAPEVLQkGTAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKTKD-KHEIDRMTLTVNVELpdtfSPE 420
Cdd:cd14164  154 YPelsTTFCGSRAYTPPEVIL-GTPYDPKKyDVWSLGVVLYVMVTGTMPFDETNVRRlRLQQRGVLYPSGVAL----EEP 228
                        250
                 ....*....|....*.
gi 148539879 421 LKSLLEGLLQRDVSKR 436
Cdd:cd14164  229 CRALIRTLLQFNPSTR 244
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
191-391 6.45e-13

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: 70.50  E-value: 6.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTGD---CPFIVCMTYAFHTPDKL 267
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQ----ALVEVKILDALRRKDrdnSHNVIHMKEYFYFRNHL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMnGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS--DLGLACdFS 343
Cdd:cd14225  121 CITFELL-GMNLYELIKKNNFqgFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSIKviDFGSSC-YE 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148539879 344 KKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14225  199 HQRVYTYIQSRFYRSPEVIL-GLPYSMAIDMWSLGCILAELYTGYPLF 245
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
197-454 6.61e-13

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: 69.69  E-value: 6.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDK----LCFILD 272
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQH----PNIVRFYDSWESTVKgkkcIVLVTE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLD-EHGHARISDLGLACDFSKKKPHA 349
Cdd:cd14030  109 LMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAKS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 SVGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHEIDRmTLTVNVElPDTFS----PELKSLL 425
Cdd:cd14030  189 VIGTPEFMAPEMYEE--KYDESVDVYAFGMCMLEMATSEYPYSE--CQNAAQIYR-RVTSGVK-PASFDkvaiPEVKEII 262
                        250       260
                 ....*....|....*....|....*....
gi 148539879 426 EGLLQRDVSKRLGChgggsQEVKEHSFFK 454
Cdd:cd14030  263 EGCIRQNKDERYAI-----KDLLNHAFFQ 286
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
197-453 6.92e-13

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: 69.71  E-value: 6.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmkqgeTLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILD 272
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIKKFveseDDPVIK-----KIALREIRMLKQLKH---PNLVNLIEVFRRKRKLHLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHyHLSQH--GVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS 350
Cdd:cd07847   81 YCDHTVLN-ELEKNprGV-PEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 --VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHS--PFR------------------QHKT--KDKHEIDRMT 406
Cdd:cd07847  159 dyVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPlwPGKsdvdqlylirktlgdlipRHQQifSTNQFFKGLS 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148539879 407 LTVNVEL-------PDTFSPELkSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd07847  239 IPEPETRepleskfPNISSPAL-SFLKGCLQMDPTERLSC-----EELLEHPYF 286
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
197-391 8.56e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 70.09  E-value: 8.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMK--------CLDKKR----IK----MKQGETLALNERIMLSLVSTGDCPFIVcmtya 260
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKkianafdnRIDAKRtlreIKllrhLDHENVIAIKDIMPPPHREAFNDVYIV----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 261 fhtpdklcfiLDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC 340
Cdd:cd07858   88 ----------YELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 341 DFSKKKPHAS--VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd07858  157 TTSEKGDFMTeyVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLF 209
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
197-397 1.18e-12

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: 69.33  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTG--KMYAMKCLDKKRIKMKQGETLALNERImlslvstgDCPFIVCMTYAF--HTPDKLCFILD 272
Cdd:cd07867   10 VGRGTYGHVYKAKRKDGKdeKEYALKQIEGTGISMSACREIALLREL--------KHPNVIALQKVFlsHSDRKVWLLFD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLH---YHLSQHGvfSEKEMRFYAT-------EIILGLEHMHNRFVVYRDLKPANILL----DEHGHARISDLGL 338
Cdd:cd07867   82 YAEHDLWHiikFHRASKA--NKKPMQLPRSmvksllyQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGF 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 339 ACDF-SKKKPHAS----VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF--RQHKTK 397
Cdd:cd07867  160 ARLFnSPLKPLADldpvVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFhcRQEDIK 225
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
276-454 1.20e-12

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: 69.60  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHyHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDfSKKKPHASVGTHG 355
Cdd:cd07880  103 GTDLG-KLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ-TDSEMTGYVVTRW 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 356 YMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVE----------------LPD--- 415
Cdd:cd07880  181 YRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQlMEIMKVTGTPSKEfvqklqsedaknyvkkLPRfrk 260
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 416 --------TFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:cd07880  261 kdfrsllpNANPLAVNVLEKMLVLDAESRI-----TAAEALAHPYFE 302
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
269-411 1.34e-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: 69.64  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGgDLHYHL-SQHgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP 347
Cdd:cd07849   85 IVQELMET-DLYKLIkTQH--LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHD 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 348 HAS-----VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNV 411
Cdd:cd07849  162 HTGflteyVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLF-----PGKDYLHQLNLILGI 225
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
191-418 1.80e-12

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: 69.04  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL--------DKKRIkmkqgetlaLNERIMLSLVSTGDcpfIVCMTYAFH 262
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIndvfehvsDATRI---------LREIKLLRLLRHPD---IVEIKHIML 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCF-----ILDLMnGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd07859   70 PPSRREFkdiyvVFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKKPHAS-----VGTHGYMAPEVLQK-GTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDK-HEIDRMTLTVN 410
Cdd:cd07859  149 LARVAFNDTPTAIfwtdyVATRWYRAPELCGSfFSKYTPAIDIWSIGCIFAEVLTGKPLF---PGKNVvHQLDLITDLLG 225

                 ....*...
gi 148539879 411 VELPDTFS 418
Cdd:cd07859  226 TPSPETIS 233
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
277-437 1.86e-12

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: 67.77  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGHARISDLGLAcDFSKKKPHASVGTH 354
Cdd:cd14023   69 GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsdEERTQLRLESLEDT-HIMKGEDDALSDKH 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 G---YMAPEVLQK-GTAYDSSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTVNVE-----LPDTFSPELKSLL 425
Cdd:cd14023  148 GcpaYVSPEILNTtGTYSGKSADVWSLGVMLYTLLVGRYPF--------HDSDPSALFSKIRrgqfcIPDHVSPKARCLI 219
                        170
                 ....*....|..
gi 148539879 426 EGLLQRDVSKRL 437
Cdd:cd14023  220 RSLLRREPSERL 231
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
178-399 1.90e-12

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 69.68  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 178 KNVELNIHLTMNE-FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRiKMKQGETLALNERIMLSLVSTGDCPFIVC 256
Cdd:PTZ00036  54 KMIDNDINRSPNKsYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDP-QYKNRELLIMKNLNHINIIFLKDYYYTEC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 257 mtyaFHTPDKLCFILDLMN--GGDLHYHLSQHGVFSEKE----MRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH 330
Cdd:PTZ00036 133 ----FKKNEKNIFLNVVMEfiPQTVHKYMKHYARNNHALplflVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTH 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 331 A-RISDLGLACD-FSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:PTZ00036 209 TlKLCDFGSAKNlLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQ 279
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
298-398 1.96e-12

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 68.76  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 298 ATEIILGLEHMHNRF-VVYRDLKPANILLDEHG-HARISDLGLACdFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWF 375
Cdd:cd14136  125 ARQVLQGLDYLHTKCgIIHTDIKPENVLLCISKiEVKIADLGNAC-WTDKHFTEDIQTRQYRSPEVIL-GAGYGTPADIW 202
                         90       100
                 ....*....|....*....|...
gi 148539879 376 SLGCMLFKLLRGHSPFRQHKTKD 398
Cdd:cd14136  203 STACMAFELATGDYLFDPHSGED 225
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
196-453 2.32e-12

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: 68.22  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmkqgeTLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFIL 271
Cdd:cd07846    8 LVGEGSYGMVMKCRHKETGQIVAIKKFleseDDKMVK-----KIAMREIKMLKQLRHEN---LVNLIEVFRRKKRWYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS- 350
Cdd:cd07846   80 EFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTd 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 351 -VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFR--------QHKTK------DKHE--IDRMTLTVNVEL 413
Cdd:cd07846  160 yVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPgdsdidqlYHIIKclgnliPRHQelFQKNPLFAGVRL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 414 PD------------TFSPELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd07846  240 PEvkeveplerrypKLSGVVIDLAKKCLHIDPDKRPSC-----SELLHHEFF 286
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
196-387 2.34e-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: 68.82  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGetlaLNERIMLSLVST----GDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd14212    6 LLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQA----MLEIAILTLLNTkydpEDKHHIVRLLDHFMHHGHLCIVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMnGGDLHYHLSQ---HGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS--DLGLACdFSKKK 346
Cdd:cd14212   82 ELL-GVNLYELLKQnqfRG-LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKliDFGSAC-FENYT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148539879 347 PHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRG 387
Cdd:cd14212  159 LYTYIQSRFYRSPEVLL-GLPYSTAIDMWSLGCIAAELFLG 198
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
195-393 2.78e-12

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: 68.02  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL-------DKKRIK-MKQGETLAlNERIMLSLVSTGDCpfivcmtyafHTPDK 266
Cdd:cd14026    3 RYLSRGAFGTVSRARHADWRVTVAIKCLkldspvgDSERNClLKEAEILH-KARFSYILPILGIC----------NEPEF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVFSEKE--MRFYAT-EIILGLEHMHNRF--VVYRDLKPANILLDEHGHARISDLGLA-- 339
Cdd:cd14026   72 LGIVTEYMTNGSLNELLHEKDIYPDVAwpLRLRILyEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSkw 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539879 340 -----CDFSKKKPHASVGTHGYMAPEVLQKG--TAYDSSADWFSLGCMLFKLLRGHSPFRQ 393
Cdd:cd14026  152 rqlsiSQSRSSKSAPEGGTIIYMPPEEYEPSqkRRASVKHDIYSYAIIMWEVLSRKIPFEE 212
pknD PRK13184
serine/threonine-protein kinase PknD;
188-402 2.89e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 70.18  E-value: 2.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYgcrkadtgKMYAMKCLDK---KRIKmkqgETLALNE----------RIMLSLVSTGDCP-F 253
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVY--------LAYDPVCSRRvalKKIR----EDLSENPllkkrflreaKIAADLIHPGIVPvY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 254 IVCmtyafHTPDKLCFILDLMNGGDLHYHLS---QHGVFS----EKE-----MRFYATeIILGLEHMHNRFVVYRDLKPA 321
Cdd:PRK13184  69 SIC-----SDGDPVYYTMPYIEGYTLKSLLKsvwQKESLSkelaEKTsvgafLSIFHK-ICATIEYVHSKGVLHRDLKPD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 322 NILLDEHGHARISDLGLA------------CDFSKK--------KPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCML 381
Cdd:PRK13184 143 NILLGLFGEVVILDWGAAifkkleeedlldIDVDERnicyssmtIPGKIVGTPDYMAPERL-LGVPASESTDIYALGVIL 221
                        250       260
                 ....*....|....*....|....
gi 148539879 382 FKLLRGHSPFRQHKTK---DKHEI 402
Cdd:PRK13184 222 YQMLTLSFPYRRKKGRkisYRDVI 245
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
195-437 3.24e-12

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: 67.75  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEtlaLNERimlslvsTGDCPFIVCMTYAFHTPDK----LCFI 270
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVE---LHWR-------ASQCPHIVRIVDVYENLYAgrkcLLIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE---HGHARISDLGLAcdfSKK 345
Cdd:cd14170   78 MECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFA---KET 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHGY----MAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDT---- 416
Cdd:cd14170  155 TSHNSLTTPCYtpyyVAPEVLGP-EKYDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKTRIRMGQYEFPNPewse 233
                        250       260
                 ....*....|....*....|.
gi 148539879 417 FSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14170  234 VSEEVKMLIRNLLKTEPTQRM 254
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
197-437 3.34e-12

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: 67.34  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLAL--NERIMLslvstgdcpfivcMTYAFHTPDKLCFILDLM 274
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACfrHENIAE-------------LYGALLWEETVHLFMEAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGHARISDLGLACDFSKK--KPHASVG 352
Cdd:cd13995   79 EGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDvyVPKDLRG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEV-LQKGtaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE-----IDRMTLTVNvELPDTFSPELKSLLE 426
Cdd:cd13995  158 TEIYMSPEViLCRG--HNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPsylyiIHKQAPPLE-DIAQDCSPAMRELLE 234
                        250
                 ....*....|.
gi 148539879 427 GLLQRDVSKRL 437
Cdd:cd13995  235 AALERNPNHRS 245
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
195-391 4.10e-12

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 67.13  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCL------DKKRIKM--KQGETLALNERIMLSLVSTGDCPFIVCMTYafhtpdk 266
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPpslhvdDSERMELleEAKKMEMAKFRHILPVYGICSEPVGLVMEY------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 lcfildlMNGGDLHYHLSQHGVFSEKEMRFyATEIILGLEHMH--NRFVVYRDLKPANILLDEHGHARISDLGLA--CDF 342
Cdd:cd14025   75 -------METGSLEKLLASEPLPWELRFRI-IHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAkwNGL 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 343 SKKKPHASVGTHG---YMAPE-VLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14025  147 SHSHDLSRDGLRGtiaYLPPErFKEKNRCPDTKHDVYSFAIVIWGILTQKKPF 199
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
275-437 4.35e-12

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: 66.44  E-value: 4.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 NGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASV--- 351
Cdd:cd14024   67 HYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDDDSLtdk 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 -GTHGYMAPEVLQKGTAYDS-SADWFSLGCMLFKLLRGHSPFRQHK-TKDKHEIDRMTLTvnveLPDTFSPELKSLLEGL 428
Cdd:cd14024  147 hGCPAYVGPEILSSRRSYSGkAADVWSLGVCLYTMLLGRYPFQDTEpAALFAKIRRGAFS----LPAWLSPGARCLVSCM 222

                 ....*....
gi 148539879 429 LQRDVSKRL 437
Cdd:cd14024  223 LRRSPAERL 231
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
177-411 4.91e-12

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: 67.73  E-value: 4.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 177 WKNVELnihlTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTGDCP---F 253
Cdd:cd14226    5 VKNGEK----WMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELMNKHDTEnkyY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 254 IVCMTYAFHTPDKLCFILDL--MNGGDLHYHLSQHGVfSEKEMRFYATEIILGLehmhnRF-------VVYRDLKPANIL 324
Cdd:cd14226   77 IVRLKRHFMFRNHLCLVFELlsYNLYDLLRNTNFRGV-SLNLTRKFAQQLCTAL-----LFlstpelsIIHCDLKPENIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 325 LDEHGHA--RISDLGLACDFSKKKpHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEI 402
Cdd:cd14226  151 LCNPKRSaiKIIDFGSSCQLGQRI-YQYIQSRFYRSPEVLL-GLPYDLAIDMWSLGCILVEMHTGEPLF-----SGANEV 223

                 ....*....
gi 148539879 403 DRMTLTVNV 411
Cdd:cd14226  224 DQMNKIVEV 232
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
195-413 5.41e-12

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: 67.02  E-value: 5.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCR----KADTGKMYAMKCLDKkrikMKQGETLALNER---IMLSLvstgDCPFIVCMTYAFHTPDK- 266
Cdd:cd05038   10 KQLGEGHFGSVELCRydplGDNTGEQVAVKSLQP----SGEEQHMSDFKReieILRTL----DHEYIVKYKGVCESPGRr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 -LCFILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05038   82 sLRLIMEYLPSGSLRDYLQRHrDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 345 KKPHASVGTHG-----YMAPEVLQKGTAYDSSADWfSLGCMLFKLL----RGHSPFRQHKTKDKHEIDRMTLTVNVEL 413
Cdd:cd05038  162 DKEYYYVKEPGespifWYAPECLRESRFSSASDVW-SFGVTLYELFtygdPSQSPPALFLRMIGIAQGQMIVTRLLEL 238
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
197-385 5.49e-12

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 66.35  E-value: 5.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkrikmkqgETLALNERIML---SLVSTGDCPFI-----VCMTYAfhtpdKLC 268
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM-----------NTLSSNRANMLrevQLMNRLSHPNIlrfmgVCVHQG-----QLH 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGH-ARISDLGLACDF--- 342
Cdd:cd14155   65 ALTEYINGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYtAVVGDFGLAEKIpdy 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148539879 343 -SKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd14155  145 sDGKEKLAVVGSPYWMAPEVL-RGEPYNEKADVFSYGIILCEII 187
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
209-437 6.12e-12

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: 67.05  E-value: 6.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 209 RKADTGKMYAMKCL---DKKRIKM--KQGETLALNERIMLSLVSTGD----------------CPFIVCMTYAFHTPDKL 267
Cdd:cd13974   18 RKEGTDDFYTLKILtleEKGEETQedRQGKMLLHTEYSLLSLLHDQDgvvhhhglfqdraceiKEDKSSNVYTGRVRKRL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGD----------LHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH-ARISDL 336
Cdd:cd13974   98 CLVLDCLCAHDfsdktadlinLQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 337 GLAC------DFSKKKphasVGTHGYMAPEVLQkGTAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKtkdKHEIDRMTLTV 409
Cdd:cd13974  178 CLGKhlvsedDLLKDQ----RGSPAYISPDVLS-GKPYLGKPsDMWALGVVLFTMLYGQFPFYDSI---PQELFRKIKAA 249
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 410 NVELPDT--FSPELKSLLEGLLQRDVSKRL 437
Cdd:cd13974  250 EYTIPEDgrVSENTVCLIRKLLVLNPQKRL 279
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
267-394 6.33e-12

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: 66.53  E-value: 6.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQhgvfSEKEMRFY----------ATEIILGLEHMHNRFVVYRDLKPANILL-----DEHGHA 331
Cdd:cd14067   83 LCFALELAPLGSLNTVLEE----NHKGSSFMplghmltfkiAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINI 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 332 RISDLGLacdfSKKKPHASV----GTHGYMAPEVlQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQH 394
Cdd:cd14067  159 KLSDYGI----SRQSFHEGAlgveGTPGYQAPEI-RPRIVYDEKVDMFSYGMVLYELLSGQRPSLGH 220
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
197-385 6.50e-12

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: 67.31  E-value: 6.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCR--KADTGKMYAMKcldkkriKMKQGETL-------ALNERIMLSLVSTgdcPFIVCMTYAF-HTPDK 266
Cdd:cd07842    8 IGRGTYGRVYKAKrkNGKDGKEYAIK-------KFKGDKEQytgisqsACREIALLRELKH---ENVVSLVEVFlEHADK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFIL------DLmnGGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL----DEHGHARISD 335
Cdd:cd07842   78 SVYLLfdyaehDL--WQIIKFHRQAKRVsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 336 LGLACDFSKK-KPHAS----VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd07842  156 LGLARLFNAPlKPLADldpvVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELL 210
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
188-454 6.69e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 66.77  E-value: 6.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 188 MNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGE----TLALNERIMLSLVSTGDcpfIVCMTYAFHT 263
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALK-----KIRLEQEDegvpSTAIREISLLKEMQHGN---IVRLQDVVHS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFI---LDLmnggDLHYHLSQHGVFSEKE--MRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA-RISDLG 337
Cdd:PLN00009  73 EKRLYLVfeyLDL----DLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNAlKLADFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFS---KKKPHASVgTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK-HEIDRMTLTVNVE- 412
Cdd:PLN00009 149 LARAFGipvRTFTHEVV-TLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDElFKIFRILGTPNEEt 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 413 ------LPD------------------TFSPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:PLN00009 228 wpgvtsLPDyksafpkwppkdlatvvpTLEPAGVDLLSKMLRLDPSKRI-----TARAALEHEYFK 288
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
197-411 8.50e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 67.01  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKAD--TGKMYAMKCLDKKRIKMKQGETLALNERImlslvstgDCPFIVCMTYAF--HTPDKLCFILD 272
Cdd:cd07868   25 VGRGTYGHVYKAKRKDgkDDKDYALKQIEGTGISMSACREIALLREL--------KHPNVISLQKVFlsHADRKVWLLFD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGgDLHYHLSQHGVFSEKE---------MRFYATEIILGLEHMHNRFVVYRDLKPANILL----DEHGHARISDLGLA 339
Cdd:cd07868   97 YAEH-DLWHIIKFHRASKANKkpvqlprgmVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDF-SKKKPHAS----VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF--RQH--KTKDKHEIDRMTLTVN 410
Cdd:cd07868  176 RLFnSPLKPLADldpvVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFhcRQEdiKTSNPYHHDQLDRIFN 255

                 .
gi 148539879 411 V 411
Cdd:cd07868  256 V 256
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
189-399 1.04e-11

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 66.21  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAfhTPDKLC 268
Cdd:cd14149   12 SEVMLSTRIGSGSFGTVY------KGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYM--TKDNLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLS-QHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK--- 344
Cdd:cd14149   84 IVTQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsg 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 345 -KKPHASVGTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd14149  164 sQQVEQPTGSILWMAPEVirMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQ 221
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
191-407 1.26e-11

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: 65.31  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLdKKRIKMKQGetlALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFI-PVRAKKKTS---ARRE---LALLAELDHKSIVRFHDAFEKRRVVIIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG--HARISDLGLACDFSKKKP- 347
Cdd:cd14108   77 TELCHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPq 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 348 HASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhktkdKHEIDRMTL 407
Cdd:cd14108  156 YCKYGTPEFVAPEIVNQ-SPVSKVTDIWPVGVIAYLCLTGISPF-------VGENDRTTL 207
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
195-393 1.26e-11

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 66.69  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMYAMKCLDK--------KRikmkqgetlALNERIMLslvstgdCPF----IVCMTYAFH 262
Cdd:cd07853    6 RPIGYGAFGVVWSVTDPRDGKRVALKKMPNvfqnlvscKR---------VFRELKML-------CFFkhdnVLSALDILQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCF-----ILDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd07853   70 PPHIDPFeeiyvVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 338 LA----CDFSKKKPHASVgTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRG------HSPFRQ 393
Cdd:cd07853  149 LArveePDESKHMTQEVV-TQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRrilfqaQSPIQQ 213
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
198-436 1.28e-11

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: 64.98  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 198 GRGGFGEVYGCRKADTGKMYAMKcldkKRIKMKQgetlalnERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFILDLMNGG 277
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK----KLLKIEK-------EAEILSVLSHRN---IIQFYGAILEAPNYGIVTEYASYG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 278 DLHYHLSQHgvfSEKEMRF-----YATEIILGLEHMHNRF---VVYRDLKPANILLDEHGHARISDLGlACDFSKKKPHA 349
Cdd:cd14060   68 SLFDYLNSN---ESEEMDMdqimtWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFG-ASRFHSHTTHM 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 350 S-VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK-------TKDKHEidrmTLTVNVELPDTFSpel 421
Cdd:cd14060  144 SlVGTFPWMAPEVIQ-SLPVSETCDTYSYGVVLWEMLTREVPFKGLEglqvawlVVEKNE----RPTIPSSCPRSFA--- 215
                        250
                 ....*....|....*
gi 148539879 422 kSLLEGLLQRDVSKR 436
Cdd:cd14060  216 -ELMRRCWEADVKER 229
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
191-391 1.51e-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: 66.69  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL-DKKRIKMKQGETLALNERimLSLVSTGDCPFIVCMTYAFHTPDKLCF 269
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVrNEKRFHRQAAEEIRILEH--LKKQDKDNTMNVIHMLESFTFRNHICM 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDL--MNGGDLHYHLSQHGvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS--DLGLACdFSKK 345
Cdd:cd14224  145 TFELlsMNLYELIKKNKFQG-FSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIKviDFGSSC-YEHQ 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 346 KPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd14224  223 RIYTYIQSRFYRAPEVIL-GARYGMPIDMWSFGCILAELLTGYPLF 267
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
200-399 1.70e-11

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: 65.21  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 200 GGFGEVYGCRKADTGKMyAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcpfIVCMTYAFHTPDKLCFILDLMNGGDL 279
Cdd:cd14027    4 GGFGKVSLCFHRTQGLV-VLKTVYTGPNCIEHNEALLEEGKMMNRLRHSR----VVKLLGVILEEGKYSLVMEYMEKGNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 280 HYHLSQHGVFSEKEMRFyATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-------------CDFSKKK 346
Cdd:cd14027   79 MHVLKKVSVPLSVKGRI-ILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehNEQREVD 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 347 PHA--SVGTHGYMAPEVLQKGTAYDSS-ADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd14027  158 GTAkkNAGTLYYMAPEHLNDVNAKPTEkSDVYSFAIVLWAIFANKEPYENAINEDQ 213
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
196-363 1.77e-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: 65.54  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgcRKADTGKMYAMKCLDKKRIKMKQGET------LALNERIMlslvstgdcPFIVCMTYAFHTPDKLCF 269
Cdd:cd13998    2 VIGKGRFGEVW--KASLKNEPVAVKIFSSRDKQSWFREKeiyrtpMLKHENIL---------QFIAADERDTALRTELWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRFV---------VYRDLKPANILLDEHGHARISDLGLAC 340
Cdd:cd13998   71 VTAFHPNGSL*DYLSLH-TIDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKSKNILVKNDGTCCIADFGLAV 149
                        170       180
                 ....*....|....*....|....*....
gi 148539879 341 DFSK------KKPHASVGTHGYMAPEVLQ 363
Cdd:cd13998  150 RLSPstgeedNANNGQVGTKRYMAPEVLE 178
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
266-452 2.75e-11

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: 64.30  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH---ARISDLGLA--- 339
Cdd:cd14012   78 KVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGktl 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 ---CDFSKKKPHASVgthGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKheidrmtLTVNVELPdt 416
Cdd:cd14012  158 ldmCSRGSLDEFKQT---YWLPPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNP-------VLVSLDLS-- 225
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148539879 417 fsPELKSLLEGLLQRDVSKRLgchggGSQEVKEHSF 452
Cdd:cd14012  226 --ASLQDFLSKCLSLDPKKRP-----TALELLPHEF 254
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
193-436 2.78e-11

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: 64.61  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 193 VHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRI--KMKQGETLALNE-RIMLSL------VSTGDCpfivcmtYAFHT 263
Cdd:cd14037    7 IEKYLAEGGFAHVYLVKTSNGGNRAALK-----RVyvNDEHDLNVCKREiEIMKRLsghkniVGYIDS-------SANRS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFILDLM----NGGDLHY---HLsQHGvFSEKEMRFYATEIILGLEHMHNR--FVVYRDLKPANILLDEHGHARIS 334
Cdd:cd14037   75 GNGVYEVLLLMeyckGGGVIDLmnqRL-QTG-LTESEILKIFCDVCEAVAAMHYLkpPLIHRDLKVENVLISDSGNYKLC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 335 DLGLACdFSKKKPHASVG------------THGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTkdkh 400
Cdd:cd14037  153 DFGSAT-TKILPPQTKQGvtyveedikkytTLQYRAPEMidLYRGKPITEKSDIWALGCLLYKLCFYTTPFEESGQ---- 227
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148539879 401 eidRMTLTVNVELPD--TFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14037  228 ---LAILNGNFTFPDnsRYSKRLHKLIRYMLEEDPEKR 262
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
197-385 3.19e-11

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: 64.59  E-value: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkrIKMKQgETlalnERIMLSLVSTGDC---PFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKEL----IRFDE-ET----QRTFLKEVKVMRClehPNVLKFIGVLYKDKRLNFITEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGG---------DLHYHLSQHGVFsekemrfyATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA----- 339
Cdd:cd14221   72 IKGGtlrgiiksmDSHYPWSQRVSF--------AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvd 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 340 -----------CDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd14221  144 ektqpeglrslKKPDRKKRYTVVGNPYWMAPEMIN-GRSYDEKVDVFSFGIVLCEII 199
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
190-399 3.63e-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: 64.31  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAfhTPDKLCF 269
Cdd:cd14151    9 QITVGQRIGSGSFGTVY------KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--TKPQLAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLsqHGVFSEKEMRFY---ATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK-- 344
Cdd:cd14151   81 VTQWCEGSSLYHHL--HIIETKFEMIKLidiARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRws 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 345 --KKPHASVGTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd14151  159 gsHQFEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQ 217
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
277-385 3.94e-11

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 64.27  E-value: 3.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRF----------VVYRDLKPANILLDEHGHARISDLGLACDFSKKK 346
Cdd:cd14053   78 GSLCDYLKGN-VISWNELCKIAESMARGLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGK 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 347 P----HASVGTHGYMAPEVLQKGTAYDSSA----DWFSLGCMLFKLL 385
Cdd:cd14053  157 ScgdtHGQVGTRRYMAPEVLEGAINFTRDAflriDMYAMGLVLWELL 203
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
190-399 4.57e-11

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: 63.88  E-value: 4.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMtyAFHTPDKLCF 269
Cdd:cd14150    1 EVSMLKRIGTGSFGTVF------RGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFM--GFMTRPNFAI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLsqHGVfsekEMRFYATEII-------LGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd14150   73 ITQWCEGSSLYRHL--HVT----ETRFDTMQLIdvarqtaQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVK 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 343 SK-------KKPHASVgthGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 399
Cdd:cd14150  147 TRwsgsqqvEQPSGSI---LWMAPEVirMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQ 209
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
265-407 5.35e-11

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: 64.80  E-value: 5.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGgDLHyHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHARISDLGLA---- 339
Cdd:cd07854   89 NSVYIVQEYMET-DLA-NVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLArivd 166
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 CDFSKKKpHASVG--THGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTL 407
Cdd:cd07854  167 PHYSHKG-YLSEGlvTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLF-----AGAHELEQMQL 230
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
191-387 7.29e-11

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: 64.01  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEtlalNERIMLSLVSTGDCP------FIVCMTYAFHTp 264
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQ----IEVSILSRLSQENADefnfvrAYECFQHKNHT- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 dklCFILDLMNGGdlHYHLSQHGVFSE---KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG----HARISDLG 337
Cdd:cd14211   76 ---CLVFEMLEQN--LYDFLKQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRG 387
Cdd:cd14211  151 SASHVSKAVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVIAELFLG 199
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
268-392 7.97e-11

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: 62.51  E-value: 7.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP 347
Cdd:cd14059   57 CILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKST 136
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148539879 348 HAS-VGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd14059  137 KMSfAGTVAWMAPEVI-RNEPCSEKVDIWSFGVVLWELLTGEIPYK 181
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
277-437 8.30e-11

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: 62.83  E-value: 8.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGHARISDLGLAC--DFSKKKPHASVG 352
Cdd:cd13976   69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFadEERTKLRLESLEDAVilEGEDDSLSDKHG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THGYMAPEVLQKGTAYD-SSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTV-----NVELPDTFSPELKSLLE 426
Cdd:cd13976  149 CPAYVSPEILNSGATYSgKAADVWSLGVILYTMLVGRYPF--------HDSEPASLFAkirrgQFAIPETLSPRARCLIR 220
                        170
                 ....*....|.
gi 148539879 427 GLLQRDVSKRL 437
Cdd:cd13976  221 SLLRREPSERL 231
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
252-436 8.49e-11

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 63.49  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 252 PFIVCMTYAFHTPDKLCFILDLMNGGDLHYHL------SQHGVFSEKE-----------MRFYATEIILGLEHMHNRFVV 314
Cdd:cd05090   67 PNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLimrsphSDVGCSSDEDgtvkssldhgdFLHIAIQIAAGMEYLSSHFFV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 315 YRDLKPANILLDEHGHARISDLGL-----ACDFSKKKPHASVGTHgYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GH 388
Cdd:cd05090  147 HKDLAARNILVGEQLHVKISDLGLsreiySSDYYRVQNKSLLPIR-WMPPEAIMYGK-FSSDSDIWSFGVVLWEIFSfGL 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148539879 389 SPFRQHKTKDKHEIDRMTLTvnVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd05090  225 QPYYGFSNQEVIEMVRKRQL--LPCSEDCPPRMYSLMTECWQEIPSRR 270
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
197-436 8.59e-11

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: 63.03  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCR-KADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd05084    4 IGRGNFGEVFSGRlRADNTPVAVKSCRETLPPDLK--AKFLQEARILKQY----SHPNIVRLIGVCTQKQPIYIVMELVQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLacdfSKKKPHASVGTH 354
Cdd:cd05084   78 GGDFLTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGM----SREEEDGVYAAT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 355 GYM--------APEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPF---RQHKTKDkhEIDRmtlTVNVELPDTFSPELK 422
Cdd:cd05084  154 GGMkqipvkwtAPEALNYGR-YSSESDVWSFGILLWETFsLGAVPYanlSNQQTRE--AVEQ---GVRLPCPENCPDEVY 227
                        250
                 ....*....|....
gi 148539879 423 SLLEGLLQRDVSKR 436
Cdd:cd05084  228 RLMEQCWEYDPRKR 241
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
196-385 8.72e-11

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: 63.37  E-value: 8.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCR----KADTGKMYAMKCLDKKRIKMKQgeTLALNERIMLSLVSTgdcpFIVCMTYAFHTPDK--LCF 269
Cdd:cd05081   11 QLGKGNFGSVELCRydplGDNTGALVAVKQLQHSGPDQQR--DFQREIQILKALHSD----FIVKYRGVSYGPGRrsLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd05081   85 VMEYLPSGCLRDFLQRHrARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDY 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148539879 349 ASVGTHG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLL 385
Cdd:cd05081  165 YVVREPGqspifWYAPESLSD-NIFSRQSDVWSFGVVLYELF 205
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
197-392 9.88e-11

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: 63.66  E-value: 9.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKC---LDKKR---IKMKQGETLA-LNERIMLSLVSTGDcpfivcmtyAFHTPDKLcF 269
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVfnnLSFMRpldVQMREFEVLKkLNHKNIVKLFAIEE---------ELTTRHKV-L 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQ----HGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL--LDEHGHA--RISDLGLACD 341
Cdd:cd13988   71 VMELCPCGSLYTVLEEpsnaYGL-PESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGAARE 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 342 FSKKKPHASV-GTHGYMAPE-----VLQK--GTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd13988  150 LEDDEQFVSLyGTEEYLHPDmyeraVLRKdhQKKYGATVDLWSIGVTFYHAATGSLPFR 208
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
197-395 1.04e-10

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: 62.75  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEV---YGCRKADTGKMYAMKCLDKKRIKMKQGETLAlNERIMLSLvstgDCPFIVCMtYAFHTPDKLCFILDL 273
Cdd:cd05060    3 LGHGNFGSVrkgVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLR-EASVMAQL----DHPCIVRL-IGVCKGEPLMLVMEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGT 353
Cdd:cd05060   77 APLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148539879 354 HG-----YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFRQHK 395
Cdd:cd05060  157 AGrwplkWYAPECINYGK-FSSKSDVWSYGVTLWEAFsYGAKPYGEMK 203
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
197-454 1.08e-10

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: 63.52  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQgetlaLNERIMLSLvstGDCPFIVCMTYAFHTPDKLCFILD---- 272
Cdd:cd06633   29 IGHGSFGAVYFATNSHTNEVVAIK---KMSYSGKQ-----TNEKWQDII---KEVKFLQQLKHPNTIEYKGCYLKDhtaw 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 ------LMNGGDLhyhLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdfSKK 345
Cdd:cd06633   98 lvmeycLGSASDL---LEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA---SIA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHAS-VGTHGYMAPEV---LQKGTaYDSSADWFSLGCMLFKLLRGHSP-FRQHKTKDKHEI---DRMTLTVNvELPDTF 417
Cdd:cd06633  172 SPANSfVGTPYWMAPEVilaMDEGQ-YDGKVDIWSLGITCIELAERKPPlFNMNAMSALYHIaqnDSPTLQSN-EWTDSF 249
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148539879 418 spelKSLLEGLLQRDVSKRLgchggGSQEVKEHSFFK 454
Cdd:cd06633  250 ----RGFVDYCLQKIPQERP-----SSAELLRHDFVR 277
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
192-469 1.25e-10

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 63.08  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 192 SVHRIIGRG--GFGEVYGCRKADTGKMYAMK-----CLDKKRIKMKQGETL---ALNERIMLSLVSTgdcpFIVcmtyaf 261
Cdd:cd08216    1 ELLYEIGKCfkGGGVVHLAKHKPTNTLVAVKkinleSDSKEDLKFLQQEILtsrQLQHPNILPYVTS----FVV------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 htPDKLCFILDLMNGG---DLhyhLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDL 336
Cdd:cd08216   71 --DNDLYVVTPLMAYGscrDL---LKTHFPegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 337 GLACDFSKK-KPHASVgtHGY----------MAPEVLQKGTA-YDSSADWFSLGCMLFKLLRGHSPFRQ-HKTK---DK- 399
Cdd:cd08216  146 RYAYSMVKHgKRQRVV--HDFpksseknlpwLSPEVLQQNLLgYNEKSDIYSVGITACELANGVVPFSDmPATQmllEKv 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 400 -----HEIDRMTL-----------------TVNVELPD-----TFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSF 452
Cdd:cd08216  224 rgttpQLLDCSTYpleedsmsqsedsstehPNNRDTRDipyqrTFSEAFHQFVELCLQRDPELR-----PSASQLLAHSF 298
                        330
                 ....*....|....*..
gi 148539879 453 FKGVDWQHVYLQKYPPP 469
Cdd:cd08216  299 FKQCRRSNTSLLDLLKP 315
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
197-385 1.43e-10

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: 62.65  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKEL--IRCDEETQKTFLTEVKVMRSL----DHPNVLKFIGVLYKDKRLNLLTEFIEG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA----------------- 339
Cdd:cd14222   75 GTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekkkpppdkptt 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148539879 340 -----CDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd14222  155 kkrtlRKNDRKKRYTVVGNPYWMAPEMLN-GKSYDEKVDIFSFGIVLCEII 204
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
266-453 2.54e-10

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: 61.63  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFIL--DLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--VVYRDLKPANILLD-EHGHARISDLGLAC 340
Cdd:cd14032   76 KRCIVLvtELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLAT 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 341 DFSKKKPHASVGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGHSPFRQhkTKDKHEIDRmTLTVNVElPDTFS-- 418
Cdd:cd14032  156 LKRASFAKSVIGTPEFMAPEMYEE--HYDESVDVYAFGMCMLEMATSEYPYSE--CQNAAQIYR-KVTCGIK-PASFEkv 229
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 148539879 419 --PELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFF 453
Cdd:cd14032  230 tdPEIKEIIGECICKNKEERYEI-----KDLLSHAFF 261
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
196-386 2.63e-10

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 62.07  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYgcRKADTGKMYAMKCLDKK--RIKMKQGE---TLALNERIMLSlvstgdcpFIVCMTYAFHTPDKLCFI 270
Cdd:cd14143    2 SIGKGRFGEVW--RGRWRGEDVAVKIFSSReeRSWFREAEiyqTVMLRHENILG--------FIAADNKDNGTWTQLWLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRFyATEIILGLEHMHNRFV--------VYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd14143   72 SDYHEHGSLFDYLNRYTVTVEGMIKL-ALSIASGLAHLHMEIVgtqgkpaiAHRDLKSKNILVKKNGTCCIADLGLAVRH 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 343 SKKK------PHASVGTHGYMAPEVLQKG---TAYDS--SADWFSLGCMLFKLLR 386
Cdd:cd14143  151 DSATdtidiaPNHRVGTKRYMAPEVLDDTinmKHFESfkRADIYALGLVFWEIAR 205
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
189-387 3.67e-10

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: 62.03  E-value: 3.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEtLALNERIMLSLVSTGDCPFI---VCMTYAFHTpd 265
Cdd:cd14227   15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQ-IEVSILARLSTESADDYNFVrayECFQHKNHT-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 klCFILDLMNgGDLHYHLSQHGvFSE---KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHG----HARISDLGL 338
Cdd:cd14227   92 --CLVFEMLE-QNLYDFLKQNK-FSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFGS 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 339 ACDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRG 387
Cdd:cd14227  168 ASHVSKAVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVIAELFLG 215
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
195-392 3.78e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 61.97  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVygCRKADTgkMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFhTPDK-------L 267
Cdd:cd07876   27 KPIGSGAQGIV--CAAFDT--VLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVF-TPQKsleefqdV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNGgdlhyHLSQ--HGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGL---ACDF 342
Cdd:cd07876  102 YLVMELMDA-----NLCQviHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLartACTN 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHasVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd07876  177 FMMTPY--VVTRYYRAPEVIL-GMGYKENVDIWSVGCIMGELVKGSVIFQ 223
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
197-438 4.56e-10

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: 60.75  E-value: 4.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEV----YGCRKadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTyAFHTPDKLCFILD 272
Cdd:cd05116    3 LGSGNFGTVkkgyYQMKK--VVKTVAVKILKNEANDPALKDELLREANVMQQL----DNPYIVRMI-GICEAESWMLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVG 352
Cdd:cd05116   76 MAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 353 THG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLLR-GHSPFRQHKTKDKHEI----DRMtltvnvELPDTFSPELK 422
Cdd:cd05116  156 THGkwpvkWYAPECMNY-YKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMiekgERM------ECPAGCPPEMY 228
                        250
                 ....*....|....*.
gi 148539879 423 SLLEGLLQRDVSKRLG 438
Cdd:cd05116  229 DLMKLCWTYDVDERPG 244
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
266-386 5.28e-10

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 60.95  E-value: 5.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRF--------VVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd14144   67 QLYLITDYHENGSLYDFLRGN-TLDTQSMLKLAYSAACGLAHLHTEIfgtqgkpaIAHRDIKSKNILVKKNGTCCIADLG 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKK------KPHASVGTHGYMAPEVLQKGTAYDS-----SADWFSLGCMLFKLLR 386
Cdd:cd14144  146 LAVKFISEtnevdlPPNTRVGTKRYMAPEVLDESLNRNHfdaykMADMYSFGLVLWEIAR 205
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
560-649 5.61e-10

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 56.79  E-value: 5.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879   560 IMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQ--------NLLTMEQILSVEETQIKDKKCILFRIKGGKQFV 631
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGCTVREAPDPDSSKKPHCFEIKTSDRKTLL 81
                           90
                   ....*....|....*...
gi 148539879   632 LQCESDPEFVQWKKELNE 649
Cdd:smart00233  82 LQAESEEEREKWVEALRK 99
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
195-436 6.90e-10

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: 60.80  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCR----KADTGKMYAMKcldkkRIKMKQGETLALNER---IMLSLVSTGDCPFI-VCMTYAfhtPDK 266
Cdd:cd14205   10 QQLGKGNFGSVEMCRydplQDNTGEVVAVK-----KLQHSTEEHLRDFEReieILKSLQHDNIVKYKgVCYSAG---RRN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd14205   82 LRLIMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTHG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLL----RGHSP---FRQHKTKDK-------HEIDRMT 406
Cdd:cd14205  162 KEYYKVKEPGespifWYAPESLTE-SKFSVASDVWSFGVVLYELFtyieKSKSPpaeFMRMIGNDKqgqmivfHLIELLK 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 148539879 407 LTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14205  241 NNGRLPRPDGCPDEIYMIMTECWNNNVNQR 270
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
186-384 7.49e-10

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: 60.06  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVY-GCRKadtGKMYAMKCLdKKRIKMKQgeTLALNERIMLSLVStgdcPFIVCMTYAFHTP 264
Cdd:cd05039    3 INKKDLKLGELIGKGEFGDVMlGDYR---GQKVAVKCL-KDDSTAAQ--AFLAEASVMTTLRH----PNLVQLLGVVLEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDf 342
Cdd:cd05039   73 NGLYIVTEYMAKGSLVDYLRSRGraVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148539879 343 skkkphASVGTHG------YMAPEVLQKGTaYDSSADWFSLGCMLFKL 384
Cdd:cd05039  152 ------ASSNQDGgklpikWTAPEALREKK-FSTKSDVWSFGILLWEI 192
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
190-392 9.18e-10

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: 60.06  E-value: 9.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYgcrkadTGKMY---AMKCLDkkrIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFhTPDK 266
Cdd:cd14063    1 ELEIKEVIGKGRFGRVH------RGRWHgdvAIKLLN---IDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACM-DPPH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDeHGHARISDLGLacdFS-- 343
Cdd:cd14063   71 LAIVTSLCKGRTLYSLIHERkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGL---FSls 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 344 -----KKKPHASVGTHG---YMAPEVLQKGTA---------YDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd14063  147 gllqpGRREDTLVIPNGwlcYLAPEIIRALSPdldfeeslpFTKASDVYAFGTVWYELLAGRWPFK 212
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
265-384 1.11e-09

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 60.05  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHlsqhgvfsekemrfyatEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd14141   92 NELCHIAQTMARGLAYLH-----------------EDIPGLKDGHKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEA 154
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148539879 345 KKP----HASVGTHGYMAPEVLQKGTAYDSSA----DWFSLGCMLFKL 384
Cdd:cd14141  155 GKSagdtHGQVGTRRYMAPEVLEGAINFQRDAflriDMYAMGLVLWEL 202
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
561-647 1.56e-09

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 55.24  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 561 MHGYMLKLGNPFLTQWQRRYFYLFPNRLEW----RGEGESRQNLLTMEQILSVEETQIKDKKCIlFRI--KGGKQFVLQC 634
Cdd:cd00821    1 KEGYLLKRGGGGLKSWKKRWFVLFEGVLLYykskKDSSYKPKGSIPLSGILEVEEVSPKERPHC-FELvtPDGRTYYLQA 79
                         90
                 ....*....|...
gi 148539879 635 ESDPEFVQWKKEL 647
Cdd:cd00821   80 DSEEERQEWLKAL 92
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
197-385 1.65e-09

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 59.07  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLdkkriKMKQGETLALNErimLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIY-----KNDVDQHKIVRE---ISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR---ISDLGLA---CDFSKKKPH- 348
Cdd:cd14156   73 GCLEELLAREELpLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLArevGEMPANDPEr 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 148539879 349 --ASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLL 385
Cdd:cd14156  153 klSLVGSAFWMAPEML-RGEPYDRKVDVFSFGIVLCEIL 190
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
195-392 1.87e-09

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 59.02  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKADTGKMY---AMKCLDkkRIKMKQGETLALNERIMLSlvstgdcpfivcmtyAFHTPDKLCFI- 270
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSDGQKihcAVKSLN--RITDIEEVEQFLKEGIIMK---------------DFSHPNVLSLLg 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 ------------LDLMNGGDL-HYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd05058   64 iclpsegsplvvLPYMKHGDLrNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFG 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 338 LACDFSKKKpHASVGTHG-------YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFR 392
Cdd:cd05058  144 LARDIYDKE-YYSVHNHTgaklpvkWMALESLQTQK-FTTKSDVWSFGVLLWELMtRGAPPYP 204
PH pfam00169
PH domain; PH stands for pleckstrin homology.
560-649 2.10e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.26  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  560 IMHGYMLKLGNPFLTQWQRRYFYLFPNRLEW-----RGEGESRQNLLTMEQILSVEETQIKDKK---CILFRI---KGGK 628
Cdd:pfam00169   2 VKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYykddkSGKSKEPKGSISLSGCEVVEVVASDSPKrkfCFELRTgerTGKR 81
                          90       100
                  ....*....|....*....|.
gi 148539879  629 QFVLQCESDPEFVQWKKELNE 649
Cdd:pfam00169  82 TYLLQAESEEERKDWIKAIQS 102
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
279-440 2.47e-09

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 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 PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 58.80  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 279 LHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEhghariSDLGLACDFSKKKP------HASV- 351
Cdd:cd13980   84 LYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTS------WNWVYLTDFASFKPtylpedNPADf 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 352 ----GTHG----YMAPEVLQKGTAYDS-----------SADWFSLGCMLFKL-LRGHSPF--------RQHKTKDKHEID 403
Cdd:cd13980  158 syffDTSRrrtcYIAPERFVDALTLDAeserrdgeltpAMDIFSLGCVIAELfTEGRPLFdlsqllayRKGEFSPEQVLE 237
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 148539879 404 RMTltvnvelpdtfSPELKSLLEGLLQRDVSKRLGCH 440
Cdd:cd13980  238 KIE-----------DPNIRELILHMIQRDPSKRLSAE 263
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
302-459 3.18e-09

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 59.11  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 302 ILGLEHMHNRFVVYRDLKPANILLDEHGHARISDL-GLAC--------DFSKKKPHASVGTHGYMAPEVLQKG-TAYDSS 371
Cdd:cd08226  111 IKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLsHLYSmvtngqrsKVVYDFPQFSTSVLPWLSPELLRQDlHGYNVK 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 372 ADWFSLGCMLFKLLRGHSPFR-QHKTK------------------DKHEIDRM--------------------TLTVNVE 412
Cdd:cd08226  191 SDIYSVGITACELARGQVPFQdMRRTQmllqklkgppyspldifpFPELESRMknsqsgmdsgigesvatssmTRTMTSE 270
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 413 -----LPDTFSPELKSLLEGLLQRDVSKRlgchgGGSQEVKEHSFFKGVDWQ 459
Cdd:cd08226  271 rlqtpSSKTFSPAFHNLVELCLQQDPEKR-----PSASSLLSHSFFKQVKEQ 317
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
304-378 3.31e-09

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: 58.23  E-value: 3.31e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 304 GLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcdfSKKKPHAS-VGTHGYMAPEV---LQKGTaYDSSADWFSLG 378
Cdd:cd06607  113 GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA---SLVCPANSfVGTPYWMAPEVilaMDEGQ-YDGKVDVWSLG 187
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
267-436 3.55e-09

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: 57.96  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHLSQHGVF--SEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSK 344
Cdd:cd05083   73 LYIVMELMSKGNLVNFLRSRGRAlvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLA-KVGS 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPFRqhKTKDKHEIDRMTLTVNVELPDTFSPELKS 423
Cdd:cd05083  152 MGVDNSRLPVKWTAPEALKNKK-FSSKSDVWSYGVLLWEVFSyGRAPYP--KMSVKEVKEAVEKGYRMEPPEGCPPDVYS 228
                        170
                 ....*....|...
gi 148539879 424 LLEGLLQRDVSKR 436
Cdd:cd05083  229 IMTSCWEAEPGKR 241
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
297-436 3.90e-09

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 58.86  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 297 YATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTH----GYMAPE-VLQKgtAYDSS 371
Cdd:cd14207  185 YSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDArlplKWMAPEsIFDK--IYSTK 262
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 372 ADWFSLGCMLFKLLR-GHSPFRQHKTkDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd14207  263 SDVWSYGVLLWEIFSlGASPYPGVQI-DEDFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNER 327
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
189-387 4.18e-09

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: 58.95  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEtlaLNERIMLSLVSTGDCPFIVCMTY-AFHTPDKL 267
Cdd:cd14228   15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQ---IEVSILSRLSSENADEYNFVRSYeCFQHKNHT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 CFILDLMNgGDLHYHLSQHGvFSE---KEMRFYATEIILGLEHMHNRFVVYRDLKPANILL----DEHGHARISDLGLAC 340
Cdd:cd14228   92 CLVFEMLE-QNLYDFLKQNK-FSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSAS 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 341 DFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRG 387
Cdd:cd14228  170 HVSKAVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVIAELFLG 215
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
197-381 4.37e-09

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: 57.90  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGetlALNE-RIMLSLvstgDCPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRN---FLKEvKVMRSL----DHPNVLKFIGVLYKDKKLNLITEYIP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHL-SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA--------------- 339
Cdd:cd14154   74 GGTLKDVLkDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgnmsp 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 340 --CDFSKKKP-----HASVGTHGYMAPEVLqKGTAYDSSADWFSLGCML 381
Cdd:cd14154  154 seTLRHLKSPdrkkrYTVVGNPYWMAPEML-NGRSYDEKVDIFSFGIVL 201
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
191-387 4.40e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 58.50  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlalnERIMLSLVSTGDCP---FI---VCMTYAFHTp 264
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI----EVGILARLSNENADefnFVrayECFQHRNHT- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 dklCFILDLMNgGDLHYHLSQHGvFSE---KEMRFYATEIILGLEHMHNRFVVYRDLKPANILL----DEHGHARISDLG 337
Cdd:cd14229   77 ---CLVFEMLE-QNLYDFLKQNK-FSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRG 387
Cdd:cd14229  152 SASHVSKTVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVIAELFLG 200
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
309-385 5.01e-09

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 58.12  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 309 HNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKP----HASVGTHGYMAPEVLQKGTAYDSSA----DWFSLGCM 380
Cdd:cd14140  120 HKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPpgdtHGQVGTRRYMAPEVLEGAINFQRDSflriDMYAMGLV 199

                 ....*
gi 148539879 381 LFKLL 385
Cdd:cd14140  200 LWELV 204
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
277-386 5.94e-09

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 57.84  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLsQHGVFSEKEMRFYATEIILGLEHMHNRF--------VVYRDLKPANILLDEHGHARISDLGLACDFSKK--- 345
Cdd:cd14142   88 GSLYDYL-QRTTLDHQEMLRLALSAASGLVHLHTEIfgtqgkpaIAHRDLKSKNILVKSNGQCCIADLGLAVTHSQEtnq 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 148539879 346 ---KPHASVGTHGYMAPEVLQKGTAYDS-----SADWFSLGCMLFKLLR 386
Cdd:cd14142  167 ldvGNNPRVGTKRYMAPEVLDETINTDCfesykRVDIYAFGLVLWEVAR 215
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
189-394 6.90e-09

Catalytic domain of the Dual-specificity protein kinases, CDC-like 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. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 57.96  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL-------DKKRIKMKQGETLALNERIMLSLVstgdcpfiVCMTYAF 261
Cdd:cd14134   12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrnvekyrEAAKIEIDVLETLAEKDPNGKSHC--------VQLRDWF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 HTPDKLCFILDLMnGGDLHYHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL-----------DEH 328
Cdd:cd14134   84 DYRGHMCIVFELL-GPSLYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynpKKK 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 329 GHARIS--------DLGLACDFSKKkpHAS-VGTHGYMAPEV-LQKGTAYdsSADWFSLGCMLFKLLRGHSPFRQH 394
Cdd:cd14134  163 RQIRVPkstdikliDFGSATFDDEY--HSSiVSTRHYRAPEViLGLGWSY--PCDVWSIGCILVELYTGELLFQTH 234
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
217-388 7.01e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 58.47  E-value: 7.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 217 YAMKCLDKKR-----IKMKQGETLALNERIMLSLVStgdcPFIVCMTYAFHTPDKLCFILDLMNGgDLHYHLSQHGVFSE 291
Cdd:PHA03212 107 FAFACIDNKTcehvvIKAGQRGGTATEAHILRAINH----PSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAI 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 292 KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC---DFSKKKPHASVGTHGYMAPEVLQKgTAY 368
Cdd:PHA03212 182 CDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACfpvDINANKYYGWAGTIATNAPELLAR-DPY 260
                        170       180
                 ....*....|....*....|
gi 148539879 369 DSSADWFSLGCMLFKLLRGH 388
Cdd:PHA03212 261 GPAVDIWSAGIVLFEMATCH 280
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
191-426 7.86e-09

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK 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: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 57.27  E-value: 7.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCldkkRIKMKQGETLALNERIMLSLVStgdCPFiVCMTYAFHTPDKLCFI 270
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKV----ESKSQPKQVLKMEVAVLKKLQG---KPH-FCRLIGCGRTERYNYI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQH--GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR----ISDLGLAcdfsk 344
Cdd:cd14017   74 VMTLLGPNLAELRRSQprGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDErtvyILDFGLA----- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 345 KKPHASVGTHGYMA-PEVLQKGTA-YDSSA-----------DWFSLGCMLFKLLRGHSPFRqhKTKDKHEIDRMT-LTVN 410
Cdd:cd14017  149 RQYTNKDGEVERPPrNAAGFRGTVrYASVNahrnkeqgrrdDLWSWFYMLIEFVTGQLPWR--KLKDKEEVGKMKeKIDH 226
                        250
                 ....*....|....*.
gi 148539879 411 VELPDTFSPELKSLLE 426
Cdd:cd14017  227 EELLKGLPKEFFQILK 242
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
186-385 8.25e-09

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: 57.35  E-value: 8.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVY-----GCRKADTGKMYAMKCLDkkrikmkqgETLALNERIML----SLVSTGDCPFIVC 256
Cdd:cd05032    3 LPREKITLIRELGQGSFGMVYeglakGVVKGEPETRVAIKTVN---------ENASMRERIEFlneaSVMKEFNCHHVVR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 257 MTYAFHTPDKLCFILDLMNGGDLHYHLSQH----------GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD 326
Cdd:cd05032   74 LLGVVSTGQPTLVVMELMAKGDLKSYLRSRrpeaennpglGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 327 EHGHARISDLGLA-----CDFSKKkphasvGTHG-----YMAPEVLQKGTaYDSSADWFSLGCMLFKLL 385
Cdd:cd05032  154 EDLTVKIGDFGMTrdiyeTDYYRK------GGKGllpvrWMAPESLKDGV-FTTKSDVWSFGVVLWEMA 215
RGS_GRK5 cd08752
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 5 ...
61-178 1.03e-08

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 5 (GRK5); The RGS domain is an essential part of the GRK5 (G protein-coupled receptor kinase 5) protein, a membrane-associated serine/threonine protein kinases which phosphorylates G protein-coupled receptors (GPCRs) upon agonist stimulation. This phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events. GRK5 is a member of the GRK kinase family which include three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188706  Cd Length: 123  Bit Score: 53.86  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  61 QKIGFLLFKDFClneinEAVPQ----VKFYEEIKEYEkLDNEEDRLCRSRQIYDAYIMKELLSCSHPFSKQAVEHVQSHL 136
Cdd:cd08752    8 QPIGRLLFRQFC-----ETRPGlecyIQFLDSVAEYE-VTPDEKLGEKGKEIMTKYLTPKSPVFIPQVGQDLVSQTEEKL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148539879 137 SKKQVTStLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWK 178
Cdd:cd08752   82 LQKPCKE-LFSACTQSVHDYLRGEPFHEYLDSMYFDRFLQWK 122
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
200-391 1.37e-08

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: 56.69  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 200 GGFGEVYgcrkadTGKMYAMKCLDK----KRIKMKQGE---TLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCfiLD 272
Cdd:cd05043   17 GTFGRIF------HGILRDEKGKEEevlvKTVKDHASEiqvTMLLQESSLLYGLSHQNLLPILHVCIEDGEKPMVL--YP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 273 LMNGGDLHYHLSQ--HG------VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSK 344
Cdd:cd05043   89 YMNWGNLKLFLQQcrLSeannpqALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFP 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 345 KKPHaSVGTHGY-----MAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05043  169 MDYH-CLGDNENrpikwMSLESLVNKE-YSSASDVWSFGVLLWELMTlGQTPY 219
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
186-402 1.58e-08

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: 56.27  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVY-GCRKADTGKM---YAMKCLDKKRIKMKQGETLAlNERIMLSLvstgDCPFIV-----C 256
Cdd:cd05057    4 VKETELEKGKVLGSGAFGTVYkGVWIPEGEKVkipVAIKVLREETGPKANEEILD-EAYVMASV----DHPHLVrllgiC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 257 MTyafhtpDKLCFILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISD 335
Cdd:cd05057   79 LS------SQVQLITQLMPLGCLLDYVRNHrDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITD 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 336 LGLA--CDFSKKKPHASVGTH--GYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPFRQHKTKDKHEI 402
Cdd:cd05057  153 FGLAklLDVDEKEYHAEGGKVpiKWMALESIQYRI-YTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDL 223
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
197-392 1.77e-08

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: 55.91  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMK-C----LDKKRIKMKQGETLALNErimlslvstgDCPFIVCMTYAFHTPDKLCFIL 271
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKtCretlPPDLKRKFLQEARILKQY----------DHPNIVKLIGVCVQKQPIMIVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 272 DLMNGGDLHYHL-SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHAS 350
Cdd:cd05041   73 ELVPGGSLLTFLrKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 351 VGTH----GYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPFR 392
Cdd:cd05041  153 DGLKqipiKWTAPEALNYGR-YTSESDVWSFGILLWEIFSlGATPYP 198
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
190-384 1.81e-08

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 56.23  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRI-----IGRGGFGEVY-----GCRKADTGKMYAMKCLDKKRIKMKQGETlalneRIMLSLVSTGDCPFIVCMTY 259
Cdd:cd05048    1 EIPLSAVrfleeLGEGAFGKVYkgellGPSSEESAISVAIKTLKENASPKTQQDF-----RREAELMSDLQHPNIVCLLG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 260 AFHTPDKLCFILDLMNGGDLHYHLSQH----------------GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI 323
Cdd:cd05048   76 VCTKEQPQCMLFEYMAHGDLHEFLVRHsphsdvgvssdddgtaSSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNC 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 324 LLDEHGHARISDLGLACD-FSK---KKPHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKL 384
Cdd:cd05048  156 LVGDGLTVKISDFGLSRDiYSSdyyRVQSKSLLPVRWMPPEAILYGK-FTTESDVWSFGVVLWEI 219
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
292-437 2.10e-08

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 56.46  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 292 KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDE-HGHARISDLGLACDFSKKKPHASVGTHGYMAPEVLQkGTAYDS 370
Cdd:cd14135  105 KAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEkKNTLKLCDFGSASDIGENEITPYLVSRFYRAPEIIL-GLPYDY 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 371 SADWFSLGCMLFKL---------------------LRGHSP---FRQHKTKDKH----------EIDRMTLTVNVELPDT 416
Cdd:cd14135  184 PIDMWSVGCTLYELytgkilfpgktnnhmlklmmdLKGKFPkkmLRKGQFKDQHfdenlnfiyrEVDKVTKKEVRRVMSD 263
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148539879 417 FSP-----------------------ELKSLLEGLLQRDVSKRL 437
Cdd:cd14135  264 IKPtkdlktlligkqrlpdedrkkllQLKDLLDKCLMLDPEKRI 307
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
195-391 3.03e-08

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: 55.50  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCRKAD-----TGKM-YAMKCLDKKRIKMKQGETLAlnERImlsLVSTGDCPFIVCMTYAFHTPDKLC 268
Cdd:cd05044    1 KFLGSGAFGEVFEGTAKDilgdgSGETkVAVKTLRKGATDQEKAEFLK--EAH---LMSNFKHPNILKLLGVCLDNDPQY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHL-------SQHGVFSEKEMRFYATEIILG---LEHMHnrfVVYRDLKPANILLDEHGHAR----IS 334
Cdd:cd05044   76 IILELMEGGDLLSYLraarptaFTPPLLTLKDLLSICVDVAKGcvyLEDMH---FVHRDLAARNCLVSSKDYRErvvkIG 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 335 DLGLACDFSKKKPHASVGtHG-----YMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPF 391
Cdd:cd05044  153 DFGLARDIYKNDYYRKEG-EGllpvrWMAPESLVDGV-FTTQSDVWAFGVLMWEILtLGQQPY 213
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
292-387 3.09e-08

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: 55.88  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 292 KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA----CDFsKKKPHasVGTHGYMAPEVLQkGTA 367
Cdd:cd07850  102 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLArtagTSF-MMTPY--VVTRYYRAPEVIL-GMG 177
                         90       100
                 ....*....|....*....|
gi 148539879 368 YDSSADWFSLGCMLFKLLRG 387
Cdd:cd07850  178 YKENVDIWSVGCIMGEMIRG 197
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
190-436 3.79e-08

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: 55.13  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMyAMKCL---DKKRIKMKQGETLA---LNERIMLSL--VSTGDCPFIVcmtyaf 261
Cdd:cd05148    7 EFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILksdDLLKQQDFQKEVQAlkrLRHKHLISLfaVCSVGEPVYI------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 htpdklcfILDLMNGGDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd05148   80 --------ITELMEKGSLLAFLrsPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 340 --------CDFSKKKPHAsvgthgYMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPFRQHKTKDKheIDRMTLTVN 410
Cdd:cd05148  152 rlikedvyLSSDKKIPYK------WTAPEAASHGT-FSTKSDVWSFGILLYEMFtYGQVPYPGMNNHEV--YDQITAGYR 222
                        250       260
                 ....*....|....*....|....*.
gi 148539879 411 VELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd05148  223 MPCPAKCPQEIYKIMLECWAAEPEDR 248
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
297-421 5.18e-08

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 55.37  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 297 YATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTH----GYMAPEVLQKgTAYDSSA 372
Cdd:cd05103  184 YSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDArlplKWMAPETIFD-RVYTIQS 262
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 373 DWFSLGCMLFKLLR-GHSPFRQHKTkDKHEIDRMTLTVNVELPDTFSPEL 421
Cdd:cd05103  263 DVWSFGVLLWEIFSlGASPYPGVKI-DEEFCRRLKEGTRMRAPDYTTPEM 311
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
289-386 5.63e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 55.48  E-value: 5.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 289 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK---KPHasVGTHGYMAPEVLQkG 365
Cdd:cd07874  116 LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmTPY--VVTRYYRAPEVIL-G 192
                         90       100
                 ....*....|....*....|.
gi 148539879 366 TAYDSSADWFSLGCMLFKLLR 386
Cdd:cd07874  193 MGYKENVDIWSVGCIMGEMVR 213
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
266-386 6.68e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 54.67  E-value: 6.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLsQHGVFSEKEMRFYATEIILGLEHMHNRF--------VVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd14219   77 QLYLITDYHENGSLYDYL-KSTTLDTKAMLKLAYSSVSGLCHLHTEIfstqgkpaIAHRDLKSKNILVKKNGTCCIADLG 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKK------PHASVGTHGYMAPEVLQKGTAYDS-----SADWFSLGCMLFKLLR 386
Cdd:cd14219  156 LAVKFISDTnevdipPNTRVGTKRYMPPEVLDESLNRNHfqsyiMADMYSFGLILWEVAR 215
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
191-391 6.86e-08

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: 54.67  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQGetlalNERIMLSLvstGDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDVRTSEVVAIK---KMSYSGKQS-----NEKWQDII---KEVKFLQRIKHPNSIEYKGCYL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LD----------LMNGGDLhyhLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd06635   96 REhtawlvmeycLGSASDL---LEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 340 cdfSKKKPHAS-VGTHGYMAPEVL--QKGTAYDSSADWFSLGCMLFKLLRGHSPF 391
Cdd:cd06635  173 ---SIASPANSfVGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITCIELAERKPPL 224
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
195-397 7.08e-08

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: 54.52  E-value: 7.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEV----YGCRKADTGKMYAMKCLdkKRIKMKQGETLALNE-RIMLSLVSTGDCPFIVCMTyafHTPDK-LC 268
Cdd:cd05080   10 RDLGEGHFGKVslycYDPTNDGTGEMVAVKAL--KADCGPQHRSGWKQEiDILKTLYHENIVKYKGCCS---EQGGKsLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd05080   85 LIMEYVPLGSLRDYLPKHSI-GLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEY 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148539879 349 ASVGTHG-----YMAPEVLQKGTAYDSSADWfSLGCMLFKLLRGHSPFRQHKTK 397
Cdd:cd05080  164 YRVREDGdspvfWYAPECLKEYKFYYASDVW-SFGVTLYELLTHCDSSQSPPTK 216
RGS_GRK1 cd08748
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 1 ...
47-178 7.17e-08

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 1 (GRK1); The RGS domain is found in G protein-coupled receptor kinases 1 (GRK1, also refered to as Rhodopsin kinase) which play a key role in phosphorylation of rhodopsin (Rho), a G protein-coupled receptor responsible for visual signal transduction in rod cell. GRK1 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. A few inactivation mutations in GRK1 have been found in patients with Oguchi disease, a stationary form of night blindness. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188702  Cd Length: 138  Bit Score: 51.70  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  47 LAERNEITFDKI-FNQKIGFLLFKDFcLNEINEAVPQVKFYEEIKEYEKLDnEEDRLCRSRQIYDAYIMKELLSCSHPFS 125
Cdd:cd08748    9 LKEELDLSFESMcVEQPIGKRLFQQF-LEATEGYAAAVALWKDIEDYDVAE-DGERAKKAQAIRNRYLESSSKEFCAFLD 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 126 KQAVEHVQShlSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWK 178
Cdd:cd08748   87 AKAVARVKE--DGNKVGDDLFKPLLRELLAHLEEAAFAPFLDSMYFLRFLQWK 137
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
301-453 7.48e-08

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: 54.25  E-value: 7.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 301 IILGLEHMHNRF-VVYRDLKPANILLDEHGHARISDLGLACD-------------FSKKKPHASVGTHGYMAPEVLQKGT 366
Cdd:cd14011  123 ISEALSFLHNDVkLVHGNICPESVVINSNGEWKLAGFDFCISseqatdqfpyfreYDPNLPPLAQPNLNYLAPEYILSKT 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 367 AyDSSADWFSLGCMLFKLL-RGHSPFRQHKTKDKHE-----IDRMTLTVNVELPDtfspELKSLLEGLLQRDVSKRLGCH 440
Cdd:cd14011  203 C-DPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKknsnqLRQLSLSLLEKVPE----ELRDHVKTLLNVTPEVRPDAE 277
                        170
                 ....*....|...
gi 148539879 441 gggsqEVKEHSFF 453
Cdd:cd14011  278 -----QLSKIPFF 285
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
292-474 1.12e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 54.28  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 292 KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK---KPHasVGTHGYMAPEVLQkGTAY 368
Cdd:cd07875  126 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmTPY--VVTRYYRAPEVIL-GMGY 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 369 DSSADWFSLGCMLFKLLRGHS--PFRQHKTKDKHEIDRM-------------TLTVNVE-------------LPDTFSP- 419
Cdd:cd07875  203 KENVDIWSVGCIMGEMIKGGVlfPGTDHIDQWNKVIEQLgtpcpefmkklqpTVRTYVEnrpkyagysfeklFPDVLFPa 282
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 420 ----------ELKSLLEGLLQRDVSKRLGChgggsQEVKEHSFFKgvDWQHVYLQKYPPPLIPPR 474
Cdd:cd07875  283 dsehnklkasQARDLLSKMLVIDASKRISV-----DEALQHPYIN--VWYDPSEAEAPPPKIPDK 340
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
454-520 1.19e-07

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 48.90  E-value: 1.19e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879   454 KGVDWQHVYLQKYPPPLIPPRGevnaaDAFDIGSFDEEDTKGiklldcdQELYKNFPLVISERWQQE 520
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIK-----SPTDTSNFDPEFTEE-------TPVLTPVDSPLSGGIQQE 55
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
300-385 1.28e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.11  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 300 EIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-CDFSKKKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLG 378
Cdd:PHA03209 165 QILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAqFPVVAPAFLGLAGTVETNAPEVLAR-DKYNSKADIWSAG 243

                 ....*..
gi 148539879 379 CMLFKLL 385
Cdd:PHA03209 244 IVLFEML 250
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
297-436 1.46e-07

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 53.83  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 297 YATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTH----GYMAPE-VLQKgtAYDSS 371
Cdd:cd05102  177 YSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSArlplKWMAPEsIFDK--VYTTQ 254
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 372 ADWFSLGCMLFKLLR-GHSPFRQHKTkDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd05102  255 SDVWSFGVLLWEIFSlGASPYPGVQI-NEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKER 319
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
200-385 1.69e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 54.08  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 200 GGFGEVYGCRKadTGKMYAMKCLDKKRIKMKQGETLA-----LNERIMLSLVSTGDCPFIVCMTYAFHTpdklCfildlm 274
Cdd:PHA03207 103 GSEGEVFVCTK--HGDEQRKKVIVKAVTGGKTPGREIdilktISHRAIINLIHAYRWKSTVCMVMPKYK----C------ 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 275 nggDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAC--DFSKKKP--HAS 350
Cdd:PHA03207 171 ---DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACklDAHPDTPqcYGW 247
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148539879 351 VGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLL 385
Cdd:PHA03207 248 SGTLETNSPELLALDP-YCAKTDIWSAGLVLFEMS 281
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
277-363 1.75e-07

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: 53.53  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHgVFSEKEMRFYATEIILGLEHMHNRF---------VVYRDLKPANILLDEHGHARISDLGLACdfsKKKP 347
Cdd:cd14055   84 GSLQDYLTRH-ILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADFGLAL---RLDP 159
                         90       100
                 ....*....|....*....|....*
gi 148539879 348 HAS---------VGTHGYMAPEVLQ 363
Cdd:cd14055  160 SLSvdelansgqVGTARYMAPEALE 184
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
190-384 2.77e-07

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 52.66  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTgkmyaMKCLDKKRIKMKQ-GETLALNERIML----SLVSTGDCPFIVCMTYAFHTP 264
Cdd:cd05061    7 KITLLRELGQGSFGMVYEGNARDI-----IKGEAETRVAVKTvNESASLRERIEFlneaSVMKGFTCHHVVRLLGVVSKG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGVFSE----------KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS 334
Cdd:cd05061   82 QPTLVVMELMAHGDLKSYLRSLRPEAEnnpgrppptlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIG 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148539879 335 DLGLACDFSKKKPHASVGTH----GYMAPEVLQKGTaYDSSADWFSLGCMLFKL 384
Cdd:cd05061  162 DFGMTRDIYETDYYRKGGKGllpvRWMAPESLKDGV-FTTSSDMWSFGVVLWEI 214
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
265-437 2.84e-07

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 52.66  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHG----VFSEKEMRFY-----------ATEIILGLEHMHNRFVVYRDLKPANILLDEHG 329
Cdd:cd05092   80 EPLIMVFEYMRHGDLNRFLRSHGpdakILDGGEGQAPgqltlgqmlqiASQIASGMVYLASLHFVHRDLATRNCLVGQGL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 330 HARISDLGLACDFSKKKpHASVGTHG-----YMAPE-VLQKgtAYDSSADWFSLGCMLFKLLR-GHSPFRQhkTKDKHEI 402
Cdd:cd05092  160 VVKIGDFGMSRDIYSTD-YYRVGGRTmlpirWMPPEsILYR--KFTTESDIWSFGVVLWEIFTyGKQPWYQ--LSNTEAI 234
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148539879 403 DRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd05092  235 ECITQGRELERPRTCPPEVYAIMQGCWQREPQQRH 269
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
195-391 3.09e-07

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 52.39  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVY----GCRKADTGKM-YAMKCLDKkrIKMKQGETLALNERIMLSLVSTgdcPFIV-CMTYAFHTPDKLc 268
Cdd:cd05036   12 RALGQGAFGEVYegtvSGMPGDPSPLqVAVKTLPE--LCSEQDEMDFLMEALIMSKFNH---PNIVrCIGVCFQRLPRF- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQH-------GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHAR---ISDLGL 338
Cdd:cd05036   86 ILLELMAGGDLKSFLRENrprpeqpSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRvakIGDFGM 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 339 A-----CDFSKKKPHASVGTHgYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05036  166 ArdiyrADYYRKGGKAMLPVK-WMPPEAFLDGI-FTSKTDVWSFGVLLWEIFSlGYMPY 222
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
196-383 3.43e-07

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: 51.93  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 196 IIGRGGFGEVYGCRKADTGKMYAMKCLDK--KRIKMKqgetlALNERIMLSLVstgDCPFIVCMTYAFHTPDKLCFILDL 273
Cdd:cd05085    3 LLGKGNFGEVYKGTLKDKTPVAVKTCKEDlpQELKIK-----FLSEARILKQY---DHPNIVKLIGVCTQRQPIYIVMEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 274 MNGGD-LHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLacdfSKKKPHASVG 352
Cdd:cd05085   75 VPGGDfLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGM----SRQEDDGVYS 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148539879 353 THG-------YMAPEVLQKGTaYDSSADWFSLGCMLFK 383
Cdd:cd05085  151 SSGlkqipikWTAPEALNYGR-YSSESDVWSFGILLWE 187
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
197-394 3.52e-07

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: 52.52  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTgkMYAMKcldkkriKMKQGETLALN--ERIMLSLVSTGDC---PFIVCMT-YAFHTpDKLCFI 270
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT--EYAVK-------RLKEDSELDWSvvKNSFLTEVEKLSRfrhPNIVDLAgYSAQQ-GNYCLI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQHGVFSEKEMRfYATEIILG----LEHMHNR--FVVYRDLKPANILLDEHGHARISDLGLA--CDF 342
Cdd:cd14159   71 YVYLPNGSLEDRLHCQVSCPCLSWS-QRLHVLLGtaraIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGLArfSRR 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASV--------GTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPFRQH 394
Cdd:cd14159  150 PKQPGMSSTlartqtvrGTLAYLPEEYVKTGT-LSVEIDVYSFGVVLLELLTGRRAMEVD 208
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
266-386 4.07e-07

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 52.35  E-value: 4.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 266 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFyATEIILGLEHMHNRF--------VVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd14220   67 QLYLITDYHENGSLYDFLKCTTLDTRALLKL-AYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGTCCIADLG 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LACDFSKKKPHAS------VGTHGYMAPEVLQKGTAYDS-----SADWFSLGCMLFKLLR 386
Cdd:cd14220  146 LAVKFNSDTNEVDvplntrVGTKRYMAPEVLDESLNKNHfqayiMADIYSFGLIIWEMAR 205
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
304-391 6.00e-07

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: 51.95  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 304 GLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKkpHASVGTHGYMAPEVL--QKGTAYDSSADWFSLGCML 381
Cdd:cd06634  127 GLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPA--NSFVGTPYWMAPEVIlaMDEGQYDGKVDVWSLGITC 204
                         90
                 ....*....|
gi 148539879 382 FKLLRGHSPF 391
Cdd:cd06634  205 IELAERKPPL 214
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
189-391 8.15e-07

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: 51.33  E-value: 8.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 189 NEFSVHRIIGRGGFGEV-----YGCRKADTGKMYAMKCLdKKRIKMKQGETLALNERIMLSLVS-------TGDC----P 252
Cdd:cd05055   35 NNLSFGKTLGAGAFGKVveataYGLSKSDAVMKVAVKML-KPTAHSSEREALMSELKIMSHLGNhenivnlLGACtiggP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 253 FIVCMTYafhtpdklCFILDLMNggdlHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLdEHGH-A 331
Cdd:cd05055  114 ILVITEY--------CCYGDLLN----FLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKiV 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 332 RISDLGLACDFSKKKPHASVGTH----GYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05055  181 KICDFGLARDIMNDSNYVVKGNArlpvKWMAPESIFNCV-YTFESDVWSYGILLWEIFSlGSNPY 244
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
304-437 9.31e-07

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 51.34  E-value: 9.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 304 GLEHMHNRFVVYRDLKPANILL--DEHGHAR--ISDLG--LACDFSK-KKPHASV-----GTHGYMAPEVLQ----KGTA 367
Cdd:cd14018  150 GVDHLVRHGIAHRDLKSDNILLelDFDGCPWlvIADFGccLADDSIGlQLPFSSWyvdrgGNACLMAPEVSTavpgPGVV 229
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 368 YD-SSADWFSLGCMLFKLLRGHSPFrqHKTKDKHEIDRMTLTVNV-ELPDTFSPELKSLLEGLLQRDVSKRL 437
Cdd:cd14018  230 INySKADAWAVGAIAYEIFGLSNPF--YGLGDTMLESRSYQESQLpALPSAVPPDVRQVVKDLLQRDPNKRV 299
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
190-385 1.04e-06

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: 51.02  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRIKMKQGETLALNE------------------------------ 239
Cdd:cd13977    1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPENVELALREfwalssiqrqhpnviqleecvlqrdglaqr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 240 --------RIMLSLVST---GDCPFIVCMTYAfhtpdkLCFILDLMNGGDLH-YHLSQHGvfSEKEMRFYATEIILGLEH 307
Cdd:cd13977   78 mshgssksDLYLLLVETslkGERCFDPRSACY------LWFVMEFCDGGDMNeYLLSRRP--DRQTNTSFMLQLSSALAF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 308 MHNRFVVYRDLKPANILLDEHGHA---RISDLGLA--CDFSKKKPHASV-----------GTHGYMAPEVLQKgtAYDSS 371
Cdd:cd13977  150 LHRNQIVHRDLKPDNILISHKRGEpilKVADFGLSkvCSGSGLNPEEPAnvnkhflssacGSDFYMAPEVWEG--HYTAK 227
                        250
                 ....*....|....
gi 148539879 372 ADWFSLGCMLFKLL 385
Cdd:cd13977  228 ADIFALGIIIWAMV 241
PTZ00284 PTZ00284
protein kinase; Provisional
285-394 1.10e-06

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 51.50  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 285 QHGVFSEKEMRFYATEIILGLEHMHNRF-VVYRDLKPANILLDE---------HGH-------ARISDLGLACDfSKKKP 347
Cdd:PTZ00284 224 KHGPFSHRHLAQIIFQTGVALDYFHTELhLMHTDLKPENILMETsdtvvdpvtNRAlppdpcrVRICDLGGCCD-ERHSR 302
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148539879 348 HASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQH 394
Cdd:PTZ00284 303 TAIVSTRHYRSPEVVL-GLGWMYSTDMWSMGCIIYELYTGKLLYDTH 348
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
197-398 1.21e-06

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 51.16  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 276
Cdd:cd14214   21 LGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 277 GDLHYHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---------DEHGHA----------RISDL 336
Cdd:cd14214  101 NTFEFLKENNFQpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlyNESKSCeeksvkntsiRVADF 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 337 GLACdFSKKKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 398
Cdd:cd14214  181 GSAT-FDHEHHTTIVATRHYRPPEVILE-LGWAQPCDVWSLGCILFEYYRGFTLFQTHENRE 240
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
197-339 1.21e-06

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 50.74  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRK--------------ADTGKMYAMKCLDKKRIKMKQGETLAlneriMLSLVSTGDCPFIVCMTYAFH 262
Cdd:cd05097   13 LGEGQFGEVHLCEAeglaeflgegapefDGQPVLVAVKMLRADVTKTARNDFLK-----EIKIMSRLKNPNIIRLLGVCV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 263 TPDKLCFILDLMNGGDLHYHLSQHGVFSE------------KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH 330
Cdd:cd05097   88 SDDPLCMITEYMENGDLNQFLSQREIESTfthannipsvsiANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYT 167

                 ....*....
gi 148539879 331 ARISDLGLA 339
Cdd:cd05097  168 IKIADFGMS 176
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
197-391 1.33e-06

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: 50.33  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVY-GCRKADT---------GKMYAMKCLDKKRIKMKqgetLALNERIMLSLVSTGDCPfivcmtyafhtpdk 266
Cdd:cd05112   12 IGSGQFGLVHlGYWLNKDkvaiktireGAMSEEDFIEEAEVMMK----LSHPKLVQLYGVCLEQAP-------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 267 LCFILDLMNGGDLHYHL-SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKK 345
Cdd:cd05112   74 ICLVFEFMEHGCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539879 346 KPHASVGTH---GYMAPEVLQKGTaYDSSADWFSLGCMLFKLL-RGHSPF 391
Cdd:cd05112  154 QYTSSTGTKfpvKWSSPEVFSFSR-YSSKSDVWSFGVLMWEVFsEGKIPY 202
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
186-391 1.39e-06

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 50.79  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKrikMKQGETLALNERIM--LSLVSTGDCPFI-----VCMT 258
Cdd:cd05108    4 LKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE---LREATSPKANKEILdeAYVMASVDNPHVcrllgICLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 259 YAFHtpdklcFILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd05108   81 STVQ------LITQLMPFGCLLDYVREHkDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 338 LA--CDFSKKKPHASVGTH--GYMAPE-VLQKgtAYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05108  155 LAklLGAEEKEYHAEGGKVpiKWMALEsILHR--IYTHQSDVWSYGVTVWELMTfGSKPY 212
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
190-398 1.55e-06

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 50.20  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRikmKQGETLALNERIMLSLVSTGD--CPFIVCMTYAFHTPDKL 267
Cdd:cd14036    1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNE---EEKNKAIIQEINFMKKLSGHPniVQFCSAASIGKEESDQG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 268 C--FIL--DLMNGG--DLHYHLSQHGVFSEKEMR--FYATeiILGLEHMHNRF--VVYRDLKPANILLDEHGHARISDLG 337
Cdd:cd14036   78 QaeYLLltELCKGQlvDFVKKVEAPGPFSPDTVLkiFYQT--CRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFG 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539879 338 LAC------DFSKKKPHAS--------VGTHGYMAPEVLQKGTAY--DSSADWFSLGCMLFKLLrghspFRQHKTKD 398
Cdd:cd14036  156 SATteahypDYSWSAQKRSlvedeitrNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCILYLLC-----FRKHPFED 227
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
186-436 2.08e-06

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: 49.59  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVY-GCRKadtGKMYAMKCLDKKrikmKQGETLALNERIMLSLVSTGdcpFIVCMTYAFHTP 264
Cdd:cd05082    3 LNMKELKLLQTIGKGEFGDVMlGDYR---GNKVAVKCIKND----ATAQAFLAEASVMTQLRHSN---LVQLLGVIVEEK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd05082   73 GGLYIVTEYMAKGSLVDYLRSRGrsVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 343 SKKKPHASVGTHgYMAPEVLQKgTAYDSSADWFSLGCMLFKLLR-GHSPFRQHKTKDKheIDRMTLTVNVELPDTFSPEL 421
Cdd:cd05082  153 SSTQDTGKLPVK-WTAPEALRE-KKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDV--VPRVEKGYKMDAPDGCPPAV 228
                        250
                 ....*....|....*
gi 148539879 422 KSLLEGLLQRDVSKR 436
Cdd:cd05082  229 YDVMKNCWHLDAAMR 243
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
197-404 2.12e-06

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: 50.02  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVY-----GCRKADTGKMYAMKCL-DKKRIKMKQGETlalNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI 270
Cdd:cd05091   14 LGEDRFGKVYkghlfGTAPGEQTQAVAIKTLkDKAEGPLREEFR---HEAMLRSRLQH---PNIVCLLGVVTKEQPMSMI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHL---SQHG-------------VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS 334
Cdd:cd05091   88 FSYCSHGDLHEFLvmrSPHSdvgstdddktvksTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKIS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539879 335 DLGL-----ACDFSKKKPHASVGTHgYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPFRQHKTKDKHEIDR 404
Cdd:cd05091  168 DLGLfrevyAADYYKLMGNSLLPIR-WMSPEAIMYGK-FSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMIR 241
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
185-339 2.46e-06

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 49.99  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 185 HLTMNEfsvhrIIGRGGFGEVYGCRKAD----TGKMYAMKCLDKK----RIKM------KQGETLALNE-RIMLSLVStg 249
Cdd:cd05095    6 LLTFKE-----KLGEGQFGEVHLCEAEGmekfMDKDFALEVSENQpvlvAVKMlradanKNARNDFLKEiKIMSRLKD-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 250 dcPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHG------------VFSEKEMRFYATEIILGLEHMHNRFVVYRD 317
Cdd:cd05095   79 --PNIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQpegqlalpsnalTVSYSDLRFMAAQIASGMKYLSSLNFVHRD 156
                        170       180
                 ....*....|....*....|..
gi 148539879 318 LKPANILLDEHGHARISDLGLA 339
Cdd:cd05095  157 LATRNCLVGKNYTIKIADFGMS 178
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
195-385 2.80e-06

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 49.54  E-value: 2.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVYGCR---KAD-TGKMYAMKCLdKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLcfI 270
Cdd:cd05079   10 RDLGEGHFGKVELCRydpEGDnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKL--I 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHA 349
Cdd:cd05079   87 MEFLPSGSLKEYLPRNkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYY 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148539879 350 SVGTH-----GYMAPEVLQKGTAYDSSADWfSLGCMLFKLL 385
Cdd:cd05079  167 TVKDDldspvFWYAPECLIQSKFYIASDVW-SFGVTLYELL 206
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
265-441 2.96e-06

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: 49.65  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 DKLCFILDLMNGGDLHYHLSQHGV-------------FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHA 331
Cdd:cd05093   80 DPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 332 RISDLGLACDFSKKKpHASVGTHG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLLR-GHSPFRQhkTKDKHEIDRM 405
Cdd:cd05093  160 KIGDFGMSRDVYSTD-YYRVGGHTmlpirWMPPESIMY-RKFTTESDVWSLGVVLWEIFTyGKQPWYQ--LSNNEVIECI 235
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148539879 406 TLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGCHG 441
Cdd:cd05093  236 TQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKE 271
RGS_GRK4 cd08750
Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 4 ...
61-181 4.04e-06

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 4 (GRK4); The RGS domain is an essential part of the GRK4 (G protein-coupled receptor kinase4) proteins, which are membrane-associated serine/threonine protein kinases that phosphorylate G protein-coupled receptors (GPCRs) upon agonist stimulation. This phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events. GRK4 is a member of the GRK kinase family which includes three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. GRK4 plays a key role in regulating dopaminergic-mediated natriuresis and is associated with essential hypertension and/or salt-sensitive hypertension. GRK4 exists in four splice variants involved in hyperphosphorylation, desensitization, and internalization of two dopamine receptors (D1R and D3R). GRK4 also increases the expression of a key receptor of the renin-angiotensin system, the AT1R (angiotensin type 1 receptor). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188704  Cd Length: 132  Bit Score: 46.81  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879  61 QKIGFLLFKDFClneinEAVPQVK----FYEEIKEYEKLDNEEDRLCRSRqIYDAYIMKELLSCSHPFSKQAVEHVQSHL 136
Cdd:cd08750    9 QPIGRLLFRQFC-----DTRPTLKrcieFLDAVAEYEVAPDEKRSDCGLS-ILDTYFNNGSAAHLPEIPQDVVTECRLKL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 148539879 137 sKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVE 181
Cdd:cd08750   83 -EENPSKELFEECTRVVHEYLSGEPFEAYQESMYFSRFLQWKWLE 126
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
252-456 4.37e-06

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 49.17  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 252 PFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHgvFSEKEMRFYATEIILG----LEHMHNRFVVYRDLKPANILLDE 327
Cdd:cd08227   59 PNIVPYRATFIADNELWVVTSFMAYGSAKDLICTH--FMDGMSELAIAYILQGvlkaLDYIHHMGYVHRSVKASHILISV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 328 HGHARISdlGLACDFSKKK-----------PHASVGTHGYMAPEVLQKG-TAYDSSADWFSLGCMLFKLLRGHSPFRQHK 395
Cdd:cd08227  137 DGKVYLS--GLRSNLSMINhgqrlrvvhdfPKYSVKVLPWLSPEVLQQNlQGYDAKSDIYSVGITACELANGHVPFKDMP 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 396 TK---------------DKHEI--DRMTLTVNVELPD--------------------------TFSPELKSLLEGLLQRD 432
Cdd:cd08227  215 ATqmlleklngtvpcllDTTTIpaEELTMKPSRSGANsglgesttvstprpsngessshpynrTFSPHFHHFVEQCLQRN 294
                        250       260
                 ....*....|....*....|....
gi 148539879 433 VSKRlgchgGGSQEVKEHSFFKGV 456
Cdd:cd08227  295 PDAR-----PSASTLLNHSFFKQI 313
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
278-436 4.78e-06

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: 48.68  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 278 DLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARIS--DLGLACDFSKKKPHASVGTHG 355
Cdd:cd14112   85 DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKlvDFGRAQKVSKLGKVPVDGDTD 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 356 YMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQhKTKDKHEIDRMTLTVNVE---LPDTFSPELKSLLEGLLQRD 432
Cdd:cd14112  165 WASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTS-EYDDEEETKENVIFVKCRpnlIFVEATQEALRFATWALKKS 243

                 ....
gi 148539879 433 VSKR 436
Cdd:cd14112  244 PTRR 247
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
197-395 6.02e-06

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 48.40  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVygcRKAdtgkMYAMKcldKKRIK-----MKQGETLALNERIM--LSLVSTGDCPFIVCMTyAFHTPDKLCF 269
Cdd:cd05115   12 LGSGNFGCV---KKG----VYKMR---KKQIDvaikvLKQGNEKAVRDEMMreAQIMHQLDNPYIVRMI-GVCEAEALML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLS-QHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPH 348
Cdd:cd05115   81 VMEMASGGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 349 ASVGTHG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLLR-GHSPFRQHK 395
Cdd:cd05115  161 YKARSAGkwplkWYAPECINF-RKFSSRSDVWSYGVTMWEAFSyGQKPYKKMK 212
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
192-398 6.17e-06

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: 48.32  E-value: 6.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 192 SVHRIIGRGGFGEVYGCRKADTGKM---YAMKCLdKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLC 268
Cdd:cd05066    7 KIEKVIGAGEFGEVCSGRLKLPGKReipVAIKTL-KAGYTEKQRRDFLSEASIMGQF----DHPNIIHLEGVVTRSKPVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 269 FILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLAcDFSKKKP 347
Cdd:cd05066   82 IVTEYMENGSLDAFLRKHdGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLS-RVLEDDP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 348 HASVGTHG------YMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPFRQHKTKD 398
Cdd:cd05066  161 EAAYTTRGgkipirWTAPEAIAYRK-FTSASDVWSYGIVMWEVMSyGERPYWEMSNQD 217
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
195-436 7.49e-06

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: 48.26  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEV-----YGCRKADTGKMYAMKCL------DKKRIKMKQGETLA-----LNERIMLSLVSTGDCPFIVCMT 258
Cdd:cd05054   13 KPLGRGAFGKViqasaFGIDKSATCRTVAVKMLkegataSEHKALMTELKILIhighhLNVVNLLGACTKPGGPLMVIVE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 259 Y-------AFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRF-----YATEIILGLEHMHNRFVVYRDLKPANILLD 326
Cdd:cd05054   93 FckfgnlsNYLRSKREEFVPYRDKGARDVEEEEDDDELYKEPLTLedlicYSFQVARGMEFLASRKCIHRDLAARNILLS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 327 EHGHARISDLGLACDFSKKKPHASVGTH----GYMAPE-VLQKgtAYDSSADWFSLGCMLFKLLR-GHSPFRQHKTkDKH 400
Cdd:cd05054  173 ENNVVKICDFGLARDIYKDPDYVRKGDArlplKWMAPEsIFDK--VYTTQSDVWSFGVLLWEIFSlGASPYPGVQM-DEE 249
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148539879 401 EIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKR 436
Cdd:cd05054  250 FCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKER 285
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
270-385 9.21e-06

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 48.13  E-value: 9.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNRF---------VVYRDLKPANILLDEHGHARISDLGLAC 340
Cdd:cd14054   72 VLEYAPKGSLCSYLRENTL-DWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLAM 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539879 341 D-FSKKKPH-----------ASVGTHGYMAPEVLQKGT------AYDSSADWFSLGCMLFKLL 385
Cdd:cd14054  151 VlRGSSLVRgrpgaaenasiSEVGTLRYMAPEVLEGAVnlrdceSALKQVDVYALGLVLWEIA 213
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
292-385 9.96e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 48.54  E-value: 9.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 292 KEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKK---PHASVGTHGYMAPEVLqKGTAY 368
Cdd:PHA03210 267 KQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEReafDYGWVGTVATNSPEIL-AGDGY 345
                         90
                 ....*....|....*..
gi 148539879 369 DSSADWFSLGCMLFKLL 385
Cdd:PHA03210 346 CEITDIWSCGLILLDML 362
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
195-391 1.26e-05

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: 47.34  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 195 RIIGRGGFGEVY----------GCRKADTGKMYAMKCLDKKRIkMKqgeTLALNERIMLSLVSTGDCPFIVCMTYafhtp 264
Cdd:cd05072   13 KKLGAGQFGEVWmgyynnstkvAVKTLKPGTMSVQAFLEEANL-MK---TLQHDKLVRLYAVVTKEEPIYIITEY----- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 265 dklcfildLMNGGDLHYHLSQHG--VFSEKEMRFYAtEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDF 342
Cdd:cd05072   84 --------MAKGSLLDFLKSDEGgkVLLPKLIDFSA-QIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148539879 343 SKKKPHASVGTH---GYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05072  155 EDNEYTAREGAKfpiKWTAPEAINFGS-FTIKSDVWSFGILLYEIVTyGKIPY 206
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
192-391 1.28e-05

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: 47.41  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 192 SVHRIIGRGGFGEVY-----GCRKADTG------KMYAMKCLDKKRI----KMKQGETLALNERIM-LSLVSTGDCPFIV 255
Cdd:cd05053   15 TLGKPLGEGAFGQVVkaeavGLDNKPNEvvtvavKMLKDDATEKDLSdlvsEMEMMKMIGKHKNIInLLGACTQDGPLYV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 256 CMTYAFH------------TPDKLCFILDLMNGGDLhyhlsqhgvfSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI 323
Cdd:cd05053   95 VVEYASKgnlreflrarrpPGEEASPDDPRVPEEQL----------TQKDLVSFAYQVARGMEYLASKKCIHRDLAARNV 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 324 LLDEHGHARISDLGLA-----CDFSKKKphasvgTHG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05053  165 LVTEDNVMKIADFGLArdihhIDYYRKT------TNGrlpvkWMAPEALFD-RVYTHQSDVWSFGVLLWEIFTlGGSPY 236
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
289-391 1.62e-05

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: 47.31  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 289 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-----CDFSKKKPHASVGTHgYMAPEVLQ 363
Cdd:cd05098  132 LSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLArdihhIDYYKKTTNGRLPVK-WMAPEALF 210
                         90       100
                 ....*....|....*....|....*....
gi 148539879 364 KgTAYDSSADWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05098  211 D-RIYTHQSDVWSFGVLLWEIFTlGGSPY 238
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
191-398 1.70e-05

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 47.32  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFI 270
Cdd:cd14215   14 YEIVSTLGEGTFGRVVQCIDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPENKNLCVQMFDWFDYHGHMCIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 271 LDLMNGGDLHYhLSQHGVF--SEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---------------DEHG---- 329
Cdd:cd14215   94 FELLGLSTFDF-LKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrDERSvkst 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 330 HARISDLGLACdFSKKKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 398
Cdd:cd14215  173 AIRVVDFGSAT-FDHEHHSTIVSTRHYRAPEVILE-LGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRE 239
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
300-470 1.71e-05

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 47.71  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 300 EIILGLEHMHNRF-VVYRDLKPANILLD-EHGHAR--------------------------------------------- 332
Cdd:cd14218  127 QVLQGLDYLHTKCkIIHTDIKPENILMCvDEGYVRrlaaeatiwqqagapppsgssvsfgasdflvnplepqnadkirvk 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 333 ISDLGLACdFSKKKPHASVGTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK----TKDKHEIDRMtlt 408
Cdd:cd14218  207 IADLGNAC-WVHKHFTEDIQTRQYRALEVL-IGAEYGTPADIWSTACMAFELATGDYLFEPHSgedyTRDEDHIAHI--- 281
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148539879 409 vnVELPDTFSPELKslLEGLLQRDVSKRLGchgggsqEVKEHSFFKGVDWQHVYLQKYPPPL 470
Cdd:cd14218  282 --VELLGDIPPHFA--LSGRYSREYFNRRG-------ELRHIKNLKHWGLYEVLVEKYEWPL 332
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
298-391 1.76e-05

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: 47.27  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 298 ATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA-----CDFSKKKPHASVGTHgYMAPEVLQKgTAYDSSA 372
Cdd:cd05099  140 AYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLArgvhdIDYYKKTSNGRLPVK-WMAPEALFD-RVYTHQS 217
                         90       100
                 ....*....|....*....|
gi 148539879 373 DWFSLGCMLFKLLR-GHSPF 391
Cdd:cd05099  218 DVWSFGILMWEIFTlGGSPY 237
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
190-384 2.28e-05

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 46.56  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVY-GCRKAdtgkmyAMKCLDKKRIKMKQ-GETLALNERIML----SLVSTGDCPFIVCMTYAFHT 263
Cdd:cd05062    7 KITMSRELGQGSFGMVYeGIAKG------VVKDEPETRVAIKTvNEAASMRERIEFlneaSVMKEFNCHHVVRLLGVVSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 264 PDKLCFILDLMNGGDLHYHL----------SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARI 333
Cdd:cd05062   81 GQPTLVIMELMTRGDLKSYLrslrpemennPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKI 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 334 SDLGLACDFSKKKPHASVGTH----GYMAPEVLQKGTaYDSSADWFSLGCMLFKL 384
Cdd:cd05062  161 GDFGMTRDIYETDYYRKGGKGllpvRWMSPESLKDGV-FTTYSDVWSFGVVLWEI 214
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
197-385 2.33e-05

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 46.85  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADTGKMYAMKCldkkRIKMKQGETLALNERIM---------------LSLVSTGDCPFIVCMTYAF 261
Cdd:cd05096   13 LGEGQFGEVHLCEVVNPQDLPTLQF----PFNVRKGRPLLVAVKILrpdanknarndflkeVKILSRLKDPNIIRLLGVC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 HTPDKLCFILDLMNGGDLHYHLSQHG-------------------VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPAN 322
Cdd:cd05096   89 VDEDPLCMITEYMENGDLNQFLSSHHlddkeengndavppahclpAISYSSLLHVALQIASGMKYLSSLNFVHRDLATRN 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539879 323 ILLDEHGHARISDLGL-----ACDFSKKKPHASVGTHgYMAPEVLQKGTaYDSSADWFSLGCMLFKLL 385
Cdd:cd05096  169 CLVGENLTIKIADFGMsrnlyAGDYYRIQGRAVLPIR-WMAWECILMGK-FTTASDVWAFGVTLWEIL 234
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
191-391 3.04e-05

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: 46.37  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 191 FSVHRIIGRGGFGEVY-GCRKADTGKM--YAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFI-----VCMTY-AF 261
Cdd:cd05035    1 LKLGKILGEGEFGSVMeAQLKQDDGSQlkVAVKTMKVDIHTYSEIEEFLSEAACMKDF----DHPNVmrligVCFTAsDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 262 HTPDKLCFILDLMNGGDLHYHL--SQHGVFSEK----EMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISD 335
Cdd:cd05035   77 NKPPSPMVILPFMKHGDLHSYLlySRLGGLPEKlplqTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVAD 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 336 LGLacdfSKK--------KPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLL-RGHSPF 391
Cdd:cd05035  157 FGL----SRKiysgdyyrQGRISKMPVKWIALESLAD-NVYTSKSDVWSFGVTMWEIAtRGQTPY 216
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
197-387 3.11e-05

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 46.42  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 197 IGRGGFGEVYGCRKADtgKMYAMKCLDK-KRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMN 275
Cdd:cd14160    1 IGEGEIFEVYRVRIGN--RSYAVKLFKQeKKMQWKKHWKRFLSELEVLLLFQH---PNILELAAYFTETEKFCLVYPYMQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 276 GGDLHYHLSQHGVfsEKEMRFYA-TEIILG----LEHMHNR---FVVYRDLKPANILLDEHGHARISDLGLAcdfsKKKP 347
Cdd:cd14160   76 NGTLFDRLQCHGV--TKPLSWHErINILIGiakaIHYLHNSqpcTVICGNISSANILLDDQMQPKLTDFALA----HFRP 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148539879 348 HA---------SVGTH---GYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRG 387
Cdd:cd14160  150 HLedqsctinmTTALHkhlWYMPEEYIRQGK-LSVKTDVYSFGIVIMEVLTG 200
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
186-398 3.28e-05

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 46.17  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 186 LTMNEFSVHRIIGRGGFGEVYGCRKADTGKM----YAMKCLdKKRIKMKQGETLALNERIMLSLVSTGDCPFI-VCMTYA 260
Cdd:cd05109    4 LKETELKKVKVLGSGAFGTVYKGIWIPDGENvkipVAIKVL-RENTSPKANKEILDEAYVMAGVGSPYVCRLLgICLTST 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 261 FHtpdklcFILDLMNGGDLHYHLSQH-GVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLA 339
Cdd:cd05109   83 VQ------LVTQLMPYGCLLDYVRENkDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148539879 340 --CDFSKKKPHASVGTH--GYMAPE-VLQKGTAYDSsaDWFSLGCMLFKLLR-GHSPFRQHKTKD 398
Cdd:cd05109  157 rlLDIDETEYHADGGKVpiKWMALEsILHRRFTHQS--DVWSYGVTVWELMTfGAKPYDGIPARE 219
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
190-392 3.30e-05

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 46.15  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 190 EFSVHRIIGRGGFGEVYGCRKAdtGKMyAMKCLDkkrIKMKQGETLALNERIMLSLVSTGDCPFIVCMTyAFHTPDKLCF 269
Cdd:cd14153    1 QLEIGELIGKGRFGQVYHGRWH--GEV-AIRLID---IERDNEEQLKAFKREVMAYRQTRHENVVLFMG-ACMSPPHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539879 270 ILDLMNGGDLHYHLSQHG-VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDeHGHARISDLG-------LACD 341
Cdd:cd14153   74 ITSLCKGRTLYSVVRDAKvVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlftisgvLQAG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148539879 342 FSKKKPHASVGTHGYMAPEVLQKGT--------AYDSSADWFSLGCMLFKLLRGHSPFR 392
Cdd:cd14153  153 RREDKLRIQSGWLCHLAPEIIRQLSpeteedklPFSKHSDVFAFGTIWYELHAREWPFK 211
 
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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