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Conserved domains on  [gi|15242554|ref|NP_198819|]
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Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

D6PK family serine/threonine-protein kinase( domain architecture ID 10144965)

D6PK family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it regulates the auxin transport activity of PIN auxin efflux facilitators by direct phosphorylation

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0005524|GO:0006468|GO:0004674
PubMed:  19614568
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
113-464 1.34e-179

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: 506.00  E-value: 1.34e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05574   2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPTLIq 272
Cdd:cd05574  82 YCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPPV- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRKakteKAGSDSLPMLIAEPTaARSMSFVGTHEYLA 352
Cdd:cd05574 161 -----------------------------------RKSLRKGSRRS----SVKSIEKETFVAEPS-ARSNSFVGTEEYIA 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE-GSISFAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd05574 201 PEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPEsPPVSSEAKDLIRKLLVKDPSKRLGSK 280
                       330       340       350
                ....*....|....*....|....*....|...
gi 15242554 432 KGATEIKQHPFFNNVNWALIRSTTPPEIPKPID 464
Cdd:cd05574 281 RGASEIKRHPFFRGVNWALIRNMTPPIIPRPDD 313
Keratin_B2_2 pfam13885
Keratin, high sulfur B2 protein;
267-309 1.85e-03

Keratin, high sulfur B2 protein;


:

Pssm-ID: 464017 [Multi-domain]  Cd Length: 45  Bit Score: 36.21  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15242554   267 SPTLIQSTS-QPSCHIASYCiQPPCIDPSCKLPVACiQPSCFKP 309
Cdd:pfam13885   3 QPSCCQPSCcQPSCCQPSCC-QPSCCQPSCCRPSCC-RSSCCQP 44
 
Name Accession Description Interval E-value
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
113-464 1.34e-179

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: 506.00  E-value: 1.34e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05574   2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPTLIq 272
Cdd:cd05574  82 YCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPPV- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRKakteKAGSDSLPMLIAEPTaARSMSFVGTHEYLA 352
Cdd:cd05574 161 -----------------------------------RKSLRKGSRRS----SVKSIEKETFVAEPS-ARSNSFVGTEEYIA 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE-GSISFAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd05574 201 PEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPEsPPVSSEAKDLIRKLLVKDPSKRLGSK 280
                       330       340       350
                ....*....|....*....|....*....|...
gi 15242554 432 KGATEIKQHPFFNNVNWALIRSTTPPEIPKPID 464
Cdd:cd05574 281 RGASEIKRHPFFRGVNWALIRNMTPPIIPRPDD 313
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
114-443 9.12e-89

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 272.10  E-value: 9.12e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLigRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    194 CSGGDLH-ILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:smart00220  79 CEGGDLFdLLKKR---GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLA----------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    273 stsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPrkaktekagsdslpmliaeptaaRSMSFVGTHEYLA 352
Cdd:smart00220 145 -------------------------------------RQLDPGE-----------------------KLTTFVGTPEYMA 164
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEGSISFAAKDLIRGLLTKDPKKRLg 429
Cdd:smart00220 165 PEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPkppFPPPEWDISPEAKDLIRKLLVKDPEKRL- 243
                          330
                   ....*....|....
gi 15242554    430 fkkGATEIKQHPFF 443
Cdd:smart00220 244 ---TAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
111-460 2.19e-59

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 198.89  E-value: 2.19e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  191 MEFCSGGDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:PTZ00263  97 LEFVVGGELftHL---RKAGR-FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEkagsdslpmliaeptaaRSMSFVGTH 348
Cdd:PTZ00263 166 -------------------------------------------------KKVPD-----------------RTFTLCGTP 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRL 428
Cdd:PTZ00263 180 EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNW-FDGRARDLVKGLLQTDHTKRL 258
                        330       340       350
                 ....*....|....*....|....*....|....
gi 15242554  429 G-FKKGATEIKQHPFFNNVNW-ALIRSTTPPEIP 460
Cdd:PTZ00263 259 GtLKGGVADVKNHPYFHGANWdKLYARYYPAPIP 292
Pkinase pfam00069
Protein kinase domain;
114-443 1.09e-52

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 177.44  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   194 CSGGDLH-ILRQKqpgKHFSELAARFYASEVLLALEYLHMMgvvyrdlkpenvmvredghimlsdfdlslqsfvsptliq 272
Cdd:pfam00069  80 VEGGSLFdLLSEK---GAFSEREAKFIMKQILEGLESGSSL--------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYLA 352
Cdd:pfam00069 118 ---------------------------------------------------------------------TTFVGTPWYMA 128
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG--SISFAAKDLIRGLLTKDPKKRLgf 430
Cdd:pfam00069 129 PEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsNLSEEAKDLLKKLLKKDPSKRL-- 206
                         330
                  ....*....|...
gi 15242554   431 kkGATEIKQHPFF 443
Cdd:pfam00069 207 --TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
111-427 9.99e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 177.51  E-value: 9.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:COG0515   6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvspt 269
Cdd:COG0515  86 MEYVEGESLAdLLRRRGP---LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGI--------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKtekagsdslpmLIAEPTAARSMSFVGTHE 349
Cdd:COG0515 154 -------------------------------------------------AR-----------ALGGATLTQTGTVVGTPG 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKK 426
Cdd:COG0515 174 YMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSelrPDLPPALDAIVLRALAKDPEE 253

                .
gi 15242554 427 R 427
Cdd:COG0515 254 R 254
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
191-386 2.74e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 65.59  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  191 MEFCSGGDL-HILRQKQPgkhfseL----AARfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsf 265
Cdd:NF033483  86 MEYVDGRTLkDYIREHGP------LspeeAVE-IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFG------ 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  266 vsptliqstsqpschIAsyciqppcidpscklpvaciqpscfkprflnnkprKAktekagsdslpmlIAEPTAARSMSFV 345
Cdd:NF033483 153 ---------------IA-----------------------------------RA-------------LSSTTMTQTNSVL 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15242554  346 GTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG 386
Cdd:NF033483 170 GTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG 210
Keratin_B2_2 pfam13885
Keratin, high sulfur B2 protein;
267-309 1.85e-03

Keratin, high sulfur B2 protein;


Pssm-ID: 464017 [Multi-domain]  Cd Length: 45  Bit Score: 36.21  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15242554   267 SPTLIQSTS-QPSCHIASYCiQPPCIDPSCKLPVACiQPSCFKP 309
Cdd:pfam13885   3 QPSCCQPSCcQPSCCQPSCC-QPSCCQPSCCRPSCC-RSSCCQP 44
 
Name Accession Description Interval E-value
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
113-464 1.34e-179

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: 506.00  E-value: 1.34e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05574   2 HFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPTLIq 272
Cdd:cd05574  82 YCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPPPV- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRKakteKAGSDSLPMLIAEPTaARSMSFVGTHEYLA 352
Cdd:cd05574 161 -----------------------------------RKSLRKGSRRS----SVKSIEKETFVAEPS-ARSNSFVGTEEYIA 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE-GSISFAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd05574 201 PEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPEsPPVSSEAKDLIRKLLVKDPSKRLGSK 280
                       330       340       350
                ....*....|....*....|....*....|...
gi 15242554 432 KGATEIKQHPFFNNVNWALIRSTTPPEIPKPID 464
Cdd:cd05574 281 RGASEIKRHPFFRGVNWALIRNMTPPIIPRPDD 313
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
120-443 5.00e-99

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: 298.28  E-value: 5.00e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 HILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpsc 279
Cdd:cd05123  81 FSHLSKE--GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLA------------------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 280 hiasyciqppcidpscklpvaciqpscfkprflnnkprkakteKAGSDslpmliaepTAARSMSFVGTHEYLAPEIIRGD 359
Cdd:cd05123 141 -------------------------------------------KELSS---------DGDRTYTFCGTPEYLAPEVLLGK 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 360 GHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLF-NVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLGFkKGATEIK 438
Cdd:cd05123 169 GYGKAVDWWSLGVLLYEMLTGKPPFYAE-NRKEIYeKILKSPLKFPEY-VSPEAKSLISGLLQKDPTKRLGS-GGAEEIK 245

                ....*
gi 15242554 439 QHPFF 443
Cdd:cd05123 246 AHPFF 250
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
114-443 9.12e-89

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 272.10  E-value: 9.12e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLigRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    194 CSGGDLH-ILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:smart00220  79 CEGGDLFdLLKKR---GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLA----------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    273 stsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPrkaktekagsdslpmliaeptaaRSMSFVGTHEYLA 352
Cdd:smart00220 145 -------------------------------------RQLDPGE-----------------------KLTTFVGTPEYMA 164
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEGSISFAAKDLIRGLLTKDPKKRLg 429
Cdd:smart00220 165 PEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPkppFPPPEWDISPEAKDLIRKLLVKDPEKRL- 243
                          330
                   ....*....|....
gi 15242554    430 fkkGATEIKQHPFF 443
Cdd:smart00220 244 ---TAEEALQHPFF 254
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
114-461 4.28e-83

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: 259.05  E-value: 4.28e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL-HILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliq 272
Cdd:cd05580  83 VPGGELfSLLRRSG---RFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFG------------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscFKPRFLNnkprkaktekagsdslpmliaeptaaRSMSFVGTHEYLA 352
Cdd:cd05580 147 ----------------------------------FAKRVKD--------------------------RTYTLCGTPEYLA 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLG-FK 431
Cdd:cd05580 167 PEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSF-FDPDAKDLIKRLLVVDLTKRLGnLK 245
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 432 KGATEIKQHPFFNNVNW-ALI-RSTTPPEIPK 461
Cdd:cd05580 246 NGVEDIKNHPWFAGIDWdALLqRKIPAPYVPK 277
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
123-448 6.99e-82

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: 255.22  E-value: 6.99e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 123 GDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL-HI 201
Cdd:cd05579   4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLySL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 202 LRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPTliqstsqpschi 281
Cdd:cd05579  84 LENV---GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQ------------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 282 asyciqppcidpscklpvaciqpscfkprflNNKPRKAKTEKAGSDslpmliaeptaaRSMSFVGTHEYLAPEIIRGDGH 361
Cdd:cd05579 149 -------------------------------IKLSIQKKSNGAPEK------------EDRRIVGTPDYLAPEILLGQGH 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 362 GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG-SISFAAKDLIRGLLTKDPKKRLGFkKGATEIKQH 440
Cdd:cd05579 186 GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpEVSDEAKDLISKLLTPDPEKRLGA-KGIEEIKNH 264

                ....*...
gi 15242554 441 PFFNNVNW 448
Cdd:cd05579 265 PFFKGIDW 272
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
118-466 1.25e-81

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: 255.99  E-value: 1.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGL-LDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALaNRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqst 274
Cdd:cd05570  81 GDLmfHIQRARR----FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGM-------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpsCKLPVaciqpscfkprfLNNKprKAKTekagsdslpmliaeptaarsmsFVGTHEYLAPE 354
Cdd:cd05570 143 --------------------CKEGI------------WGGN--TTST----------------------FCGTPDYIAPE 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLF-NVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGF-KK 432
Cdd:cd05570 167 ILREQDYGFSVDWWALGVLLYEMLAGQSPFEGD-DEDELFeAILNDEVLYPR-WLSREAVSILKGLLTKDPARRLGCgPK 244
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15242554 433 GATEIKQHPFFNNVNWALI--RSTTPPEIPK---PIDLS 466
Cdd:cd05570 245 GEADIKAHPFFRNIDWDKLekKEVEPPFKPKvksPRDTS 283
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
114-466 1.86e-75

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: 241.42  E-value: 1.86e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05573   3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptlI 271
Cdd:cd05573  83 MPGGDLmnLLIKYDV----FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTK-------M 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 QSTSQPSchiaSYCIQPpcidpscklpvacIQPSCFKPRFLNNKPRKAKTekagsdslpmliaeptaARSMSFVGTHEYL 351
Cdd:cd05573 152 NKSGDRE----SYLNDS-------------VNTLFQDNVLARRRPHKQRR-----------------VRAYSAVGTPDYI 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFP-EGSISFAAKDLIRGLLTkDPKKRL 428
Cdd:cd05573 198 APEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMNwkESLVFPdDPDVSPEAIDLIRRLLC-DPEDRL 276
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242554 429 GfkkGATEIKQHPFFNNVNWALIRSTTPPEIPK---PIDLS 466
Cdd:cd05573 277 G---SAEEIKAHPFFKGIDWENLRESPPPFVPElssPTDTS 314
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
114-443 8.94e-74

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: 234.42  E-value: 8.94e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEkfSCL--LM 191
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDE--SKLyfVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDL-HILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptl 270
Cdd:cd05581  81 EYAPNGDLlEYIRKY---GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFG----------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpVACIQPScfkprflNNKPRKAKTEKAGSDslpmliaEPTAARSMSFVGTHEY 350
Cdd:cd05581 147 ----------------------------TAKVLGP-------DSSPESTKGDADSQI-------AYNQARAASFVGTAEY 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLG- 429
Cdd:cd05581 185 VSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPEN-FPPDAKDLIQKLLVLDPSKRLGv 263
                       330
                ....*....|....*
gi 15242554 430 -FKKGATEIKQHPFF 443
Cdd:cd05581 264 nENGGYDELKAHPFF 278
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
114-471 4.28e-72

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: 232.12  E-value: 4.28e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYL---AELREMGCFFAMKVMDKGMLIGRKKLVR-AQTEREILGLL-DHPFLPTLYSHFETEKFSC 188
Cdd:cd05614   2 FELLKVLGTGAYGKVFLvrkVSGHDANKLYAMKVLRKAALVQKAKTVEhTRTERNVLEHVrQSPFLVTLHYAFQTDAKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHI-LRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVS 267
Cdd:cd05614  82 LILDYVSGGELFThLYQRD---HFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS-KEFLT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakTEKAgsdslpmliaeptaaRSMSFVGT 347
Cdd:cd05614 158 -----------------------------------------------------EEKE---------------RTYSFCGT 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 HEYLAPEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLK----FPEgSISFAAKDLIRGLLTK 422
Cdd:cd05614 170 IEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKcdppFPS-FIGPVARDLLQKLLCK 248
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15242554 423 DPKKRLGF-KKGATEIKQHPFFNNVNWALIRSTtppEIPKPIDLSILNET 471
Cdd:cd05614 249 DPKKRLGAgPQGAQEIKEHPFFKGLDWEALALR---KVNPPFRPSIRSEL 295
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
120-446 9.16e-70

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: 223.81  E-value: 9.16e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELR---EMGCFFAMKVMDKGMLIGRKK-LVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd05583   2 LGTGAYGKVFLVRKVgghDAGKLYAMKVLKKATIVQKAKtAEHTMTERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDL--HiLRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliq 272
Cdd:cd05583  82 NGGELftH-LYQRE---HFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKE--------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprFLNNKprkaktekagsdslpmliaeptAARSMSFVGTHEYLA 352
Cdd:cd05583 149 --------------------------------------FLPGE----------------------NDRAYSFCGTIEYMA 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRG--DGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLK----FPEgSISFAAKDLIRGLLTKDPKK 426
Cdd:cd05583 169 PEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKshppIPK-TFSAEAKDFILKLLEKDPKK 247
                       330       340
                ....*....|....*....|.
gi 15242554 427 RLGFKK-GATEIKQHPFFNNV 446
Cdd:cd05583 248 RLGAGPrGAHEIKEHPFFKGL 268
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
113-442 2.87e-69

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: 221.96  E-value: 2.87e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIgrKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQ--KSGLEHQLRREIeiQSHLRHPNILRLYGYFEDKKRIYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptl 270
Cdd:cd14007  79 LEYAPNGELYKELKKQ--KRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGW---------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpSCHIasyciqppcidpscklpvaciqpscfkprflNNKPRkaktekagsdslpmliaeptaarsMSFVGTHEY 350
Cdd:cd14007 147 -------SVHA-------------------------------PSNRR------------------------KTFCGTLDY 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd14007 165 LPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPS-SVSPEAKDLISKLLQKDPSKRLSL 243
                       330
                ....*....|..
gi 15242554 431 KkgatEIKQHPF 442
Cdd:cd14007 244 E----QVLNHPW 251
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
118-499 3.03e-69

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: 224.12  E-value: 3.03e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIL-GLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsq 276
Cdd:cd05575  81 GELFFHLQRE--RHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGL---------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpsCKlpvaciqpscfkprflNNKPRKAKTEkagsdslpmliaeptaarsmSFVGTHEYLAPEII 356
Cdd:cd05575 143 ------------------CK----------------EGIEPSDTTS--------------------TFCGTPEYLAPEVL 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKKGATE 436
Cdd:cd05575 169 RKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRT-NVSPSARDLLEGLLQKDRTKRLGSGNDFLE 247
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 437 IKQHPFFNNVNWALI--RSTTPPEIP--------KPIDLSILNETLKSSVQQQGKHSKQSDSSSGPYLDFEFF 499
Cdd:cd05575 248 IKNHSFFRPINWDDLeaKKIPPPFNPnvsgpldlRNIDPEFTREPVPASVGKSADSVAVSASVQEADNAFDGF 320
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
118-471 1.15e-68

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: 222.62  E-value: 1.15e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqsts 275
Cdd:cd05571  81 ELffHLSRERV----FSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGL--------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpsCKlpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMS-FVGTHEYLAPE 354
Cdd:cd05571 142 -------------------CK-------------------------------------EEISYGATTKtFCGTPEYLAPE 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFN-VVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLG-FKK 432
Cdd:cd05571 166 VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NRDHEVLFElILMEEVRFPS-TLSPEAKSLLAGLLKKDPKKRLGgGPR 243
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15242554 433 GATEIKQHPFFNNVNW-ALIRSttppEIPKPIDLSILNET 471
Cdd:cd05571 244 DAKEIMEHPFFASINWdDLYQK----KIPPPFKPQVTSET 279
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
114-448 2.83e-66

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: 214.96  E-value: 2.83e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05609   2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRqkqpgKHFSELA---ARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPTl 270
Cdd:cd05609  82 VEGGDCATLL-----KNIGPLPvdmARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLT- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqsTSQPSCHIASYCiqppcidpscklpvaciqpscfkPRFLNNKprkaktekagsdslpmliaeptaarsmsFVGTHEY 350
Cdd:cd05609 156 ---TNLYEGHIEKDT-----------------------REFLDKQ----------------------------VCGTPEY 181
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS--ISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd05609 182 IAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDdaLPDDAQDLITRLLQQNPLERL 261
                       330       340
                ....*....|....*....|
gi 15242554 429 GfKKGATEIKQHPFFNNVNW 448
Cdd:cd05609 262 G-TGGAEEVKQHPFFQDLDW 280
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
120-448 1.69e-65

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: 212.47  E-value: 1.69e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 -HILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqSFvsptliqstsqps 278
Cdd:cd05572  81 wTILRDR---GLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDF-----GF------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 279 chiasyciqppcidpscklpvaciqpscfkprflnnkprkAKteKAGSdslpmliaeptAARSMSFVGTHEYLAPEIIRG 358
Cdd:cd05572 140 ----------------------------------------AK--KLGS-----------GRKTWTFCGTPEYVAPEIILN 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 359 DGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR--ETLFNVVGQ--PLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKK-G 433
Cdd:cd05572 167 KGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGidKIEFPK-YIDKNAKNLIKQLLRRNPEERLGYLKgG 245
                       330
                ....*....|....*
gi 15242554 434 ATEIKQHPFFNNVNW 448
Cdd:cd05572 246 IRDIKKHKWFEGFDW 260
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
118-461 2.95e-65

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: 213.79  E-value: 2.95e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGL-LDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALaSQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqst 274
Cdd:cd05592  81 GDLmfHI---QQSGR-FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGM-------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpsCKLPVaciqpscfkprflnNKPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLAPE 354
Cdd:cd05592 143 --------------------CKENI--------------YGENKAST----------------------FCGTPDYIAPE 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKK-G 433
Cdd:cd05592 167 ILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPR-WLTKEAASCLSLLLERNPEKRLGVPEcP 245
                       330       340       350
                ....*....|....*....|....*....|
gi 15242554 434 ATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05592 246 AGDIRDHPFFKTIDWDKLerREIDPPFKPK 275
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
114-498 2.39e-62

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: 206.31  E-value: 2.39e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKL--VRAqtEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVahVRA--ERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptli 271
Cdd:cd05599  81 EFLPGGDMMTLLMKK--DTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL----------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpsCKlpvaciqpscfkprflnnkprkaktekaGSDSLPMliaeptaarSMSFVGTHEYL 351
Cdd:cd05599 148 -----------------------CT----------------------------GLKKSHL---------AYSTVGTPDYI 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFP-EGSISFAAKDLIRGLLTkDPKKRL 428
Cdd:cd05599 168 APEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNwrETLVFPpEVPISPEAKDLIERLLC-DAEHRL 246
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 429 GfKKGATEIKQHPFFNNVNWALIRSTTPPEIPK---PIDLSILNETLKSSVQQQGKHSKQSDSSSGPYLDFEF 498
Cdd:cd05599 247 G-ANGVEEIKSHPFFKGVDWDHIRERPAPILPEvksILDTSNFDEFEEVDLQIPSSPEAGKDSKELKSKDWVF 318
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
113-462 3.44e-62

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: 204.85  E-value: 3.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAEL---REMGCFFAMKVMDKGMLIGRKKLVR-AQTEREIL-GLLDHPFLPTLYSHFETEKFS 187
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKATIVQKAKTAEhTRTERQVLeHIRQSPFLVTLHYAFQTDTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsf 265
Cdd:cd05613  81 HLILDYINGGELftHLSQRER----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKE-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vsptliqstsqpschiasYCIQppcidpscklpvaciqpscfkprflnnkprkaKTEkagsdslpmliaeptaaRSMSFV 345
Cdd:cd05613 155 ------------------FLLD--------------------------------ENE-----------------RAYSFC 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRG--DGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLK----FPEgSISFAAKDLIRGL 419
Cdd:cd05613 168 GTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKseppYPQ-EMSALAKDIIQRL 246
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15242554 420 LTKDPKKRLGF-KKGATEIKQHPFFNNVNWALIRSTTPPEIPKP 462
Cdd:cd05613 247 LMKDPKKRLGCgPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
114-461 3.57e-62

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: 204.98  E-value: 3.57e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL-HILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliq 272
Cdd:cd05612  83 VPGGELfSYLRNS---GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGF------------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYLA 352
Cdd:cd05612 148 -------------------------------------------------------------AKKLRDRTWTLCGTPEYLA 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLG-FK 431
Cdd:cd05612 167 PEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPR-HLDLYAKDLIKKLLVVDRTRRLGnMK 245
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 432 KGATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05612 246 NGADDVKNHRWFKSVDWDDVpqRKLKPPIVPK 277
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
118-461 4.54e-62

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: 205.63  E-value: 4.54e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqsts 275
Cdd:cd05595  81 ELffHLSRERV----FTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGL--------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpsCKLPVaciqpscfkprflnnkprkaktekagSDSLPMliaeptaarsMSFVGTHEYLAPEI 355
Cdd:cd05595 142 -------------------CKEGI--------------------------TDGATM----------KTFCGTPEYLAPEV 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFN-VVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRL-GFKKG 433
Cdd:cd05595 167 LEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHERLFElILMEEIRFPR-TLSPEAKSLLAGLLKKDPKQRLgGGPSD 244
                       330       340       350
                ....*....|....*....|....*....|
gi 15242554 434 ATEIKQHPFFNNVNW--ALIRSTTPPEIPK 461
Cdd:cd05595 245 AKEVMEHRFFLSINWqdVVQKKLLPPFKPQ 274
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
114-461 8.86e-62

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: 206.62  E-value: 8.86e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05629   3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqS 273
Cdd:cd05629  83 LPGGDLMTMLIKY--DTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGL------------S 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQPSCHIASYCIQPpcidpscklpvaciqpscFKPRFLNNKPRKAKTEKAGSDSLPM----LIAEPTAARSM---SFVG 346
Cdd:cd05629 149 TGFHKQHDSAYYQKL------------------LQGKSNKNRIDNRNSVAVDSINLTMsskdQIATWKKNRRLmaySTVG 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFPEG-SISFAAKDLIRGLLTkD 423
Cdd:cd05629 211 TPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIINwrETLYFPDDiHLSVEAEDLIRRLIT-N 289
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15242554 424 PKKRLGfKKGATEIKQHPFFNNVNWALIRSTTPPEIPK 461
Cdd:cd05629 290 AENRLG-RGGAHEIKSHPFFRGVDWDTIRQIRAPFIPQ 326
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
118-460 9.07e-62

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: 204.56  E-value: 9.07e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAEL---REMGCFFAMKVMDKGMLIGRKKlVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd05582   1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDR-VRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFvsptliqst 274
Cdd:cd05582  80 RGGDLFTRLSKE--VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESI--------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKagsdslpmliaeptaaRSMSFVGTHEYLAPE 354
Cdd:cd05582 149 ---------------------------------------------DHEK----------------KAYSFCGTVEYMAPE 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFK-KG 433
Cdd:cd05582 168 VVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQ-FLSPEAQSLLRALFKRNPANRLGAGpDG 246
                       330       340
                ....*....|....*....|....*....
gi 15242554 434 ATEIKQHPFFNNVNWA--LIRSTTPPEIP 460
Cdd:cd05582 247 VEEIKRHPFFATIDWNklYRKEIKPPFKP 275
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
113-466 1.23e-60

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: 202.16  E-value: 1.23e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05598   2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKqpgKH-FSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptli 271
Cdd:cd05598  82 YIPGGDLMSLLIK---KGiFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL----------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpsCFKPRFLNNkprkAKTEKAgsdslpmliaeptaarsMSFVGTHEYL 351
Cdd:cd05598 148 ----------------------------------CTGFRWTHD----SKYYLA-----------------HSLVGTPNYI 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP--LKFP-EGSISFAAKDLIRGLLTkDPKKRL 428
Cdd:cd05598 173 APEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRttLKIPhEANLSPEAKDLILRLCC-DAEDRL 251
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242554 429 GfKKGATEIKQHPFFNNVNWALIRSTTPPEIPK---PIDLS 466
Cdd:cd05598 252 G-RNGADEIKAHPFFAGIDWEKLRKQKAPYIPTirhPTDTS 291
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
114-470 6.64e-60

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: 199.83  E-value: 6.64e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL---DHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVnsaRHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL--HIlrqkqpgkH---FSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsf 265
Cdd:cd05589  81 MEYAAGGDLmmHI--------HedvFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGL----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vsptliqstsqpschiasyciqppcidpsCKlpvaciqpscfkprflnnkprkaktEKAGSdslpmliaeptAARSMSFV 345
Cdd:cd05589 148 -----------------------------CK-------------------------EGMGF-----------GDRTSTFC 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPeGSISFAAKDLIRGLLTKDPK 425
Cdd:cd05589 163 GTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYP-RFLSTEAISIMRRLLRKNPE 241
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 426 KRLGF-KKGATEIKQHPFFNNVNWA--LIRSTTPPEIPK---PIDLSILNE 470
Cdd:cd05589 242 RRLGAsERDAEDVKKQPFFRNIDWEalLARKIKPPFVPTiksPEDVSNFDE 292
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
114-464 8.15e-60

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: 200.49  E-value: 8.15e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05610   6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGD----LHILrqkqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspt 269
Cdd:cd05610  86 LIGGDvkslLHIY------GYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLS-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liQSTSQPSCHIASYCIQPPCIDPSCKLPVACIQPSCFKPRFLNNKPRKAKTEKAGSDSLPMLIAEPtaarsmsFVGTHE 349
Cdd:cd05610 152 --KVTLNRELNMMDILTTPSMAKPKNDYSRTPGQVLSLISSLGFNTPTPYRTPKSVRRGAARVEGER-------ILGTPD 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG--SISFAAKDLIRGLLTKDPKKR 427
Cdd:cd05610 223 YLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGeeELSVNAQNAIEILLTMDPTKR 302
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 428 LGFKkgatEIKQHPFFNNVNWALIRSTTPPEIPKPID 464
Cdd:cd05610 303 AGLK----ELKQHPLFHGVDWENLQNQTMPFIPQPDD 335
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
117-460 1.25e-59

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: 199.17  E-value: 1.25e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAEL---REMGCFFAMKVMDKGMLIGRKK-LVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKttgSDKGKIFAMKVLKKASIVRNQKdTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptl 270
Cdd:cd05584  81 YLSGGELfmHLEREGI----FMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGL---------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpsCKlpvaciqpscfkprflnnkprkaktEKAGSDSLpmliaeptaarSMSFVGTHEY 350
Cdd:cd05584 147 ------------------------CK-------------------------ESIHDGTV-----------THTFCGTIEY 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd05584 167 MAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPP-YLTNEARDLLKKLLKRNVSSRLGS 245
                       330       340       350
                ....*....|....*....|....*....|...
gi 15242554 431 KKG-ATEIKQHPFFNNVNW--ALIRSTTPPEIP 460
Cdd:cd05584 246 GPGdAEEIKAHPFFRHINWddLLAKKVEPPFKP 278
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
117-461 1.87e-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: 198.77  E-value: 1.87e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHP-FLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqs 273
Cdd:cd05587  81 GGDLmyHI---QQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGM------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpsCKLPVAciqpscfkprflnnkprKAKTEKagsdslpmliaeptaarsmSFVGTHEYLAP 353
Cdd:cd05587 144 ---------------------CKEGIF-----------------GGKTTR-------------------TFCGTPDYIAP 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGF-KK 432
Cdd:cd05587 167 EIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK-SLSKEAVSICKGLLTKHPAKRLGCgPT 245
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242554 433 GATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05587 246 GERDIKEHPFFRRIDWEKLerREIQPPFKPK 276
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
111-460 2.19e-59

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 198.89  E-value: 2.19e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  191 MEFCSGGDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:PTZ00263  97 LEFVVGGELftHL---RKAGR-FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA------- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEkagsdslpmliaeptaaRSMSFVGTH 348
Cdd:PTZ00263 166 -------------------------------------------------KKVPD-----------------RTFTLCGTP 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRL 428
Cdd:PTZ00263 180 EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNW-FDGRARDLVKGLLQTDHTKRL 258
                        330       340       350
                 ....*....|....*....|....*....|....
gi 15242554  429 G-FKKGATEIKQHPFFNNVNW-ALIRSTTPPEIP 460
Cdd:PTZ00263 259 GtLKGGVADVKNHPYFHGANWdKLYARYYPAPIP 292
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
118-498 2.91e-59

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: 198.27  E-value: 2.91e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIL-GLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsq 276
Cdd:cd05603  81 GELFFHLQRE--RCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGL---------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpsCKLPVaciqpscfkprflnnkprkaktekagsdslpmliaEPTAARSmSFVGTHEYLAPEII 356
Cdd:cd05603 143 ------------------CKEGM-----------------------------------EPEETTS-TFCGTPEYLAPEVL 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPeGSISFAAKDLIRGLLTKDPKKRLGFKKGATE 436
Cdd:cd05603 169 RKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLP-GGKTVAACDLLQGLLHKDQRRRLGAKADFLE 247
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 437 IKQHPFFNNVNWALI--RSTTPPEIPK---PIDL-----SILNETLKSSVQQQGKHSKQSDSSSGPYLDFEF 498
Cdd:cd05603 248 IKNHVFFSPINWDDLyhKRITPPYNPNvagPADLrhfdpEFTQEAVPHSVGRTPDLTASSSSSSSAFLGFSY 319
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
114-461 3.55e-59

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: 198.30  E-value: 3.55e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05601   3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd05601  83 HPGGDLLSLLSRYDDI-FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG-------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidPSCKLPvaciqpscfkprflNNKprkaktekagsdslpmliaeptAARSMSFVGTHEYLAP 353
Cdd:cd05601 148 -------------------SAAKLS--------------SDK----------------------TVTSKMPVGTPDYIAP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EII------RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFPEG-SISFAAKDLIRGLLTkDP 424
Cdd:cd05601 173 EVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNfkKFLKFPEDpKVSESAVDLIKGLLT-DA 251
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 425 KKRLGFKKgateIKQHPFFNNVNWALIRSTTPPEIPK 461
Cdd:cd05601 252 KERLGYEG----LCCHPFFSGIDWNNLRQTVPPFVPT 284
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
113-442 5.73e-59

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: 195.39  E-value: 5.73e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMlIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKK-LKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvs 267
Cdd:cd05117  80 LCTGGELfdRIVKKG----SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLA------ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPrKAKTekagsdslpmliaeptaarsmsFVGT 347
Cdd:cd05117 150 ------------------------------------------KIFEEGE-KLKT----------------------VCGT 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 HEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDP 424
Cdd:cd05117 165 PYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSpewKNVSEEAKDLIKRLLVVDP 244
                       330
                ....*....|....*...
gi 15242554 425 KKRLgfkkGATEIKQHPF 442
Cdd:cd05117 245 KKRL----TAAEALNHPW 258
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
117-448 8.36e-59

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: 195.01  E-value: 8.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQgESPYVAKLYYSFQSKDYLYLVMEYLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDLHILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqsts 275
Cdd:cd05611  81 GGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS-------------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRKaktekagsdslpmliaeptaarsmsFVGTHEYLAPEI 355
Cdd:cd05611 145 --------------------------------RNGLEKRHNKK-------------------------FVGTPDYLAPET 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKRLGfKK 432
Cdd:cd05611 168 ILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEevkEFCSPEAVDLINRLLCMDPAKRLG-AN 246
                       330
                ....*....|....*.
gi 15242554 433 GATEIKQHPFFNNVNW 448
Cdd:cd05611 247 GYQEIKSHPFFKSINW 262
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
113-443 2.43e-58

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: 193.63  E-value: 2.43e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05578   1 HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptl 270
Cdd:cd05578  81 LLLGGDLryHLQQKV----KFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFN----------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpVACIqpscFKPRFLNNkprkaktekagsdslpmliaeptaarSMSfvGTHEY 350
Cdd:cd05578 146 ----------------------------IATK----LTDGTLAT--------------------------STS--GTKPY 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR---ETLFNVVGQPLKFPEGSISfAAKDLIRGLLTKDPKKR 427
Cdd:cd05578 166 MAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTsieEIRAKFETASVLYPAGWSE-EAIDLINKLLERDPQKR 244
                       330
                ....*....|....*.
gi 15242554 428 LGFKKgatEIKQHPFF 443
Cdd:cd05578 245 LGDLS---DLKNHPYF 257
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
120-460 2.52e-57

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: 191.59  E-value: 2.52e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 --HILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsqp 277
Cdd:cd05577  81 kyHIYNVGTRG--FSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGL----------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 SCHIasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSdslpmliaeptaarsmsfVGTHEYLAPEIIR 357
Cdd:cd05577 142 AVEF------------------------------------KGGKKIKGR------------------VGTHGYMAPEVLQ 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 358 GD-GHGSSVDWWTFGIFLYELLTGKTPFKGNG----NRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKK 432
Cdd:cd05577 168 KEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKekvdKEELKRRTLEMAVEYPD-SFSPEARSLCEGLLQKDPERRLGCRG 246
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242554 433 G-ATEIKQHPFFNNVNWALIRS--TTPPEIP 460
Cdd:cd05577 247 GsADEVKEHPFFRSLNWQRLEAgmLEPPFVP 277
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
120-479 7.88e-57

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: 191.63  E-value: 7.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 HILRQKQpGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsqpsc 279
Cdd:cd05585  82 FHHLQRE-GR-FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGL------------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 280 hiasyciqppcidpsCKLpvaciqpscfkprflnNKPRKAKTEkagsdslpmliaeptaarsmSFVGTHEYLAPEIIRGD 359
Cdd:cd05585 141 ---------------CKL----------------NMKDDDKTN--------------------TFCGTPEYLAPELLLGH 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 360 GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLGFkKGATEIKQ 439
Cdd:cd05585 170 GYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDG-FDRDAKDLLIGLLNRDPTKRLGY-NGAQEIKN 247
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 440 HPFFNNVNWA--LIRSTTPPEIP------------------KPIDLSILNETLKSSVQQQ 479
Cdd:cd05585 248 HPFFDQIDWKrlLMKKIQPPFKPavenaidtsnfdeeftreKPIDSVVDDSHLSESVQQQ 307
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
114-466 8.84e-57

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: 8.84e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05597   3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd05597  83 YCGGDLLTLLSKF-EDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpSCFKprflnnkprkaktekagsdslpmlIAEPTAARSMSFVGTHEYLAP 353
Cdd:cd05597 148 -------------------------------SCLK------------------------LREDGTVQSSVAVGTPDYISP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIR--GDGHGS---SVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP--LKFP--EGSISFAAKDLIRGLLTkDP 424
Cdd:cd05597 173 EILQamEDGKGRygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKehFSFPddEDDVSEEAKDLIRRLIC-SR 251
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15242554 425 KKRLGfKKGATEIKQHPFFNNVNWALIRSTTPPEIPK---PIDLS 466
Cdd:cd05597 252 ERRLG-QNGIDDFKKHPFFEGIDWDNIRDSTPPYIPEvtsPTDTS 295
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
109-461 1.07e-56

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: 193.32  E-value: 1.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 109 LGLGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd05600   8 LKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLqSFVSP 268
Cdd:cd05600  88 LAMEYVPGGDFRTLLNNS--GILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLAS-GTLSP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 TLIQSTSQpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRKAKTEKAGSDSLPMLIAEpTAARSMSFVGTH 348
Cdd:cd05600 165 KKIESMKI-------------------------------RLEEVKNTAFLELTAKERRNIYRAMRKE-DQNYANSVVGSP 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQPLKFP-------EGSISFAAKDLIRGL 419
Cdd:cd05600 213 DYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYhwKKTLQRPvytdpdlEFNLSDEAWDLITKL 292
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15242554 420 LTkDPKKRLGFKKgatEIKQHPFFNNVNWALIR-STTPPEIPK 461
Cdd:cd05600 293 IT-DPQDRLQSPE---QIKNHPFFKNIDWDRLReGSKPPFIPE 331
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
117-466 1.21e-56

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: 191.33  E-value: 1.21e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIL-GLLDHPFLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqsts 275
Cdd:cd05604  81 GGELFFHLQRE--RSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGL--------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpsCKLPVaciqpscfkprflnnkprkaktekAGSDSlpmliaeptaarSMSFVGTHEYLAPEI 355
Cdd:cd05604 144 -------------------CKEGI------------------------SNSDT------------TTTFCGTPEYLAPEV 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLGFKKGAT 435
Cdd:cd05604 169 IRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPG-ISLTAWSILEELLEKDRQLRLGAKEDFL 247
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15242554 436 EIKQHPFFNNVNWA-LIRSTTP----PEIPKPIDLS 466
Cdd:cd05604 248 EIKNHPFFESINWTdLVQKKIPppfnPNVNGPDDIS 283
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
114-466 1.82e-56

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: 189.92  E-value: 1.82e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14209   3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL-HILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd14209  83 VPGGEMfSHLRRI---GRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFA----------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTekagsdslpmliaeptaaRSMSFVGTHEYLA 352
Cdd:cd14209 149 --------------------------------------------KRVKG------------------RTWTLCGTPEYLA 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLG-FK 431
Cdd:cd14209 167 PEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSH-FSSDLKDLLRNLLQVDLTKRFGnLK 245
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15242554 432 KGATEIKQHPFFNNVNWALI--RSTTPPEIPK---PIDLS 466
Cdd:cd14209 246 NGVNDIKNHKWFATTDWIAIyqRKVEAPFIPKlkgPGDTS 285
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
114-479 2.29e-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: 188.21  E-value: 2.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05619   7 FVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLFFVME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL--HIlrqkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPtl 270
Cdd:cd05619  87 YLNGGDLmfHI----QSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGD-- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaARSMSFVGTHEY 350
Cdd:cd05619 161 --------------------------------------------------------------------AKTSTFCGTPDY 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd05619 173 IAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQ-DEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPERRLGV 251
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 431 KKgatEIKQHPFFNNVNWALI--RSTTPPEIPK---PIDLS-----ILNETLKSSVQQQ 479
Cdd:cd05619 252 RG---DIRQHPFFREINWEALeeREIEPPFKPKvksPFDCSnfdkeFLNEKPRLSFADR 307
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
113-442 4.21e-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: 185.03  E-value: 4.21e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIG--RKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEeiEEKIKR---EIEIMKLLNHPNIIKLYEVIETENKIYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspt 269
Cdd:cd14003  78 MEYASGGELfDYIVNNGR---LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLS-------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnNKPRKAKtekagsdslpmliaeptaaRSMSFVGTHE 349
Cdd:cd14003 147 --------------------------------------------NEFRGGS-------------------LLKTFCGTPA 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd14003 164 YAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS-HLSPDARDLIRRMLVVDPSKRI 242
                       330
                ....*....|....
gi 15242554 429 gfkkGATEIKQHPF 442
Cdd:cd14003 243 ----TIEEILNHPW 252
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
111-461 1.07e-54

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: 187.21  E-value: 1.07e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05593  14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsp 268
Cdd:cd05593  94 MEYVNGGELffHLSRERV----FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL-------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpsCKLPVAciqpscfkprflnnkprkaktekagsdslpmliaepTAARSMSFVGTH 348
Cdd:cd05593 162 --------------------------CKEGIT------------------------------------DAATMKTFCGTP 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFN-VVGQPLKFPEgSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd05593 180 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFElILMEDIKFPR-TLSADAKSLLSGLLIKDPNKR 257
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 428 L-GFKKGATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05593 258 LgGGPDDAKEIMRHSFFTGVNWQDVydKKLVPPFKPQ 294
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
113-462 1.56e-54

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: 184.48  E-value: 1.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05605   1 TFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL--HILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptl 270
Cdd:cd05605  81 IMNGGDLkfHIYNMGNPG--FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmlIAEPTAARSMsfVGTHEY 350
Cdd:cd05605 152 --------------------------------------------------------------IPEGETIRGR--VGTVGY 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG--------------NRETLFNvvgqplKFPEgsisfAAKDLI 416
Cdd:cd05605 168 MAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKekvkreevdrrvkeDQEEYSE------KFSE-----EAKSIC 236
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15242554 417 RGLLTKDPKKRLGFKK-GATEIKQHPFFNNVNWALIRS--TTPPEIPKP 462
Cdd:cd05605 237 SQLLQKDPKTRLGCRGeGAEDVKSHPFFKSINFKRLEAglLEPPFVPDP 285
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
118-480 2.12e-54

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: 185.15  E-value: 2.12e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL--HIlrqkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqst 274
Cdd:cd05620  81 GDLmfHI----QDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGM-------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpsCKlpvaciqpscfkprflnnkprkaktEKAGSDSlpmliaeptaaRSMSFVGTHEYLAPE 354
Cdd:cd05620 143 --------------------CK-------------------------ENVFGDN-----------RASTFCGTPDYIAPE 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNREtLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRLGFkkgA 434
Cdd:cd05620 167 ILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDE-LFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLGV---V 242
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 435 TEIKQHPFFNNVNWALI--RSTTPPEIPK---PIDLS-----ILNETLKSSVQQQG 480
Cdd:cd05620 243 GNIRGHPFFKTINWTALekRELDPPFKPKvksPSDYSnfdreFLSEKPRLSYSDKN 298
Pkinase pfam00069
Protein kinase domain;
114-443 1.09e-52

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 177.44  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   194 CSGGDLH-ILRQKqpgKHFSELAARFYASEVLLALEYLHMMgvvyrdlkpenvmvredghimlsdfdlslqsfvsptliq 272
Cdd:pfam00069  80 VEGGSLFdLLSEK---GAFSEREAKFIMKQILEGLESGSSL--------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYLA 352
Cdd:pfam00069 118 ---------------------------------------------------------------------TTFVGTPWYMA 128
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG--SISFAAKDLIRGLLTKDPKKRLgf 430
Cdd:pfam00069 129 PEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsNLSEEAKDLLKKLLKKDPSKRL-- 206
                         330
                  ....*....|...
gi 15242554   431 kkGATEIKQHPFF 443
Cdd:pfam00069 207 --TATQALQHPWF 217
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
118-461 1.27e-52

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: 181.08  E-value: 1.27e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL--HILRQKQ-PGKHfselaARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqs 273
Cdd:cd05588  81 GDLmfHMQRQRRlPEEH-----ARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGM------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpsCKLPVaciqpscfkprflnnkpRKAKTekagsdslpmliaeptaarSMSFVGTHEYLAP 353
Cdd:cd05588 143 ---------------------CKEGL-----------------RPGDT-------------------TSTFCGTPNYIAP 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRET--------LFNVV-GQPLKFPEgSISFAAKDLIRGLLTKDP 424
Cdd:cd05588 166 EILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDNpdqntedyLFQVIlEKPIRIPR-SLSVKAASVLKGFLNKNP 244
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242554 425 KKRLGFKK--GATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05588 245 AERLGCHPqtGFADIQSHPFFRTIDWEQLeqKQVTPPYKPR 285
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
120-461 1.48e-52

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: 180.49  E-value: 1.48e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLMEFCSGGD 198
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 199 L--HIlrqkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsq 276
Cdd:cd05590  83 LmfHI----QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGM---------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpsCKLPVaciqpscfkprflnnkpRKAKTekagsdslpmliaeptaarSMSFVGTHEYLAPEII 356
Cdd:cd05590 143 ------------------CKEGI-----------------FNGKT-------------------TSTFCGTPDYIAPEIL 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFN-VVGQPLKFPeGSISFAAKDLIRGLLTKDPKKRLGF--KKG 433
Cdd:cd05590 169 QEMLYGPSVDWWAMGVLLYEMLCGHAPFEAE-NEDDLFEaILNDEVVYP-TWLSQDAVDILKAFMTKNPTMRLGSltLGG 246
                       330       340       350
                ....*....|....*....|....*....|
gi 15242554 434 ATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05590 247 EEAILRHPFFKELDWEKLnrRQIEPPFRPR 276
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
96-464 4.71e-52

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: 180.22  E-value: 4.71e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  96 DAIQNVKCSKNedLGLGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLD-HPFL 174
Cdd:cd05617   1 DGMDGIKISQG--LGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASsNPFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 175 PTLYSHFETEKFSCLLMEFCSGGDL--HILRQKQ-PGKHfselaARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG 251
Cdd:cd05617  79 VGLHSCFQTTSRLFLVIEYVNGGDLmfHMQRQRKlPEEH-----ARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 252 HIMLSDFDLSLQSfVSPTLIQSTsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpm 331
Cdd:cd05617 154 HIKLTDYGMCKEG-LGPGDTTST--------------------------------------------------------- 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 332 liaeptaarsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFK------GNGNRETLFNVV-GQPLKFP 404
Cdd:cd05617 176 ------------FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDiitdnpDMNTEDYLFQVIlEKPIRIP 243
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242554 405 EgSISFAAKDLIRGLLTKDPKKRLG--FKKGATEIKQHPFFNNVNWALI--RSTTPPEIPKPID 464
Cdd:cd05617 244 R-FLSVKASHVLKGFLNKDPKERLGcqPQTGFSDIKSHTFFRSIDWDLLekKQVTPPFKPQITD 306
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
114-465 6.52e-52

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: 179.44  E-value: 6.52e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIL-GLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05602   9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVLD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliq 272
Cdd:cd05602  89 YINGGELFYHLQRE--RCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGL------------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpsCKLPVaciqpscfkprflnnkprkaktekagsdslpmliaEPTAARSmSFVGTHEYLA 352
Cdd:cd05602 155 ----------------------CKENI-----------------------------------EPNGTTS-TFCGTPEYLA 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFpEGSISFAAKDLIRGLLTKDPKKRLGFKK 432
Cdd:cd05602 177 PEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQL-KPNITNSARHLLEGLLQKDRTKRLGAKD 255
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15242554 433 GATEIKQHPFFNNVNW--ALIRSTTPPEIPK---PIDL 465
Cdd:cd05602 256 DFTEIKNHIFFSPINWddLINKKITPPFNPNvsgPNDL 293
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
114-461 6.72e-52

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: 179.84  E-value: 6.72e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05594  27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHM-MGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptl 270
Cdd:cd05594 107 ANGGELffHLSRERV----FSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGL---------- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpsCKLPVaciqpscfkprflnnkprkakteKAGsdslpmliaeptaARSMSFVGTHEY 350
Cdd:cd05594 173 ------------------------CKEGI-----------------------KDG-------------ATMKTFCGTPEY 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFN-VVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRL- 428
Cdd:cd05594 193 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDHEKLFElILMEEIRFPR-TLSPEAKSLLSGLLKKDPKQRLg 270
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15242554 429 GFKKGATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05594 271 GGPDDAKEIMQHKFFAGIVWQDVyeKKLVPPFKPQ 305
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
118-461 4.03e-51

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: 176.53  E-value: 4.03e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGL-LDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALaAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsq 276
Cdd:cd05591  81 GDL--MFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGM---------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpsCKLPVaciqpscfkprfLNNKprkaktekagsdslpmliaeptaaRSMSFVGTHEYLAPEII 356
Cdd:cd05591 143 ------------------CKEGI------------LNGK------------------------TTTTFCGTPDYIAPEIL 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLF-NVVGQPLKFPEGsISFAAKDLIRGLLTKDPKKRLG---FKK 432
Cdd:cd05591 169 QELEYGPSVDWWALGVLMYEMMAGQPPFEAD-NEDDLFeSILHDDVLYPVW-LSKEAVSILKAFMTKNPAKRLGcvaSQG 246
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242554 433 GATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05591 247 GEDAIRQHPFFREIDWEALeqRKVKPPFKPK 277
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
114-460 6.89e-51

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: 175.07  E-value: 6.89e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKlgcGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05608   6 FRVLGK---GGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HI--LRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvspt 269
Cdd:cd05608  83 MNGGDLryHIynVDEENPG--FQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVE------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprfLNNKPRKAKtekagsdslpmliaeptaarsmSFVGTHE 349
Cdd:cd05608 155 ------------------------------------------LKDGQTKTK----------------------GYAGTPG 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG----NRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPK 425
Cdd:cd05608 171 FMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGekveNKELKQRILNDSVTYSE-KFSPASKSICEALLAKDPE 249
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15242554 426 KRLGFKKGA-TEIKQHPFFNNVNWALIRS--TTPPEIP 460
Cdd:cd05608 250 KRLGFRDGNcDGLRTHPFFRDINWRKLEAgiLPPPFVP 287
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
114-461 9.39e-51

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: 175.96  E-value: 9.39e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHP-FLPTLYSHFETEKFSCLLME 192
Cdd:cd05616   2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLhILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliq 272
Cdd:cd05616  82 YVNGGDL-MYHIQQVGR-FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGM------------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpsCKLPVAciqpscfkprflnnkprkaktekagsdslpmliaepTAARSMSFVGTHEYLA 352
Cdd:cd05616 148 ----------------------CKENIW------------------------------------DGVTTKTFCGTPDYIA 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGF-K 431
Cdd:cd05616 170 PEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPK-SMSKEAVAICKGLMTKHPGKRLGCgP 248
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 432 KGATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05616 249 EGERDIKEHAFFRYIDWEKLerKEIQPPYKPK 280
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
120-460 1.09e-50

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: 175.84  E-value: 1.09e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIL---GLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQpGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsq 276
Cdd:cd05586  81 GELFWHLQKE-GR-FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS--------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscfKPRFLNNKPrkaktekagsdslpmliaeptaarSMSFVGTHEYLAPEII 356
Cdd:cd05586 144 -------------------------------KADLTDNKT------------------------TNTFCGTTEYLAPEVL 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRLGFKKGAT 435
Cdd:cd05586 169 LDEkGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVLSDEGRSFVKGLLNRNPKHRLGAHDDAV 248
                       330       340
                ....*....|....*....|....*..
gi 15242554 436 EIKQHPFFNNVNWALI--RSTTPPEIP 460
Cdd:cd05586 249 ELKEHPFFADIDWDLLskKKITPPFKP 275
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
114-460 1.16e-50

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: 176.41  E-value: 1.16e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05596  28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDY 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd05596 108 MPGGDLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFG-------------- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvACIqpscfkprflnnkprkakteKAGSDSLpmliaeptaARSMSFVGTHEYLAP 353
Cdd:cd05596 171 --------------------------TCM--------------------KMDKDGL---------VRSDTAVGTPDYISP 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIR---GDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ--PLKFP-EGSISFAAKDLIRGLLTkDPKK 426
Cdd:cd05596 196 EVLKsqgGDGVyGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHknSLQFPdDVEISKDAKSLICAFLT-DREV 274
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15242554 427 RLGfKKGATEIKQHPFFNNVNWAL--IRSTTPPEIP 460
Cdd:cd05596 275 RLG-RNGIEEIKAHPFFKNDQWTWdnIRETVPPVVP 309
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
111-427 9.99e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 177.51  E-value: 9.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:COG0515   6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvspt 269
Cdd:COG0515  86 MEYVEGESLAdLLRRRGP---LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGI--------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKtekagsdslpmLIAEPTAARSMSFVGTHE 349
Cdd:COG0515 154 -------------------------------------------------AR-----------ALGGATLTQTGTVVGTPG 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKK 426
Cdd:COG0515 174 YMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSelrPDLPPALDAIVLRALAKDPEE 253

                .
gi 15242554 427 R 427
Cdd:COG0515 254 R 254
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
114-462 4.94e-49

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: 170.92  E-value: 4.94e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05632   4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptli 271
Cdd:cd05632  84 MNGGDLkfHIYNMGNPG--FEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmlIAEPTAARSMsfVGTHEYL 351
Cdd:cd05632 154 -------------------------------------------------------------IPEGESIRGR--VGTVGYM 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG---NRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd05632 171 APEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKekvKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDPKQRL 250
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 429 GFKK-GATEIKQHPFFNNVNWALIRS--TTPPEIPKP 462
Cdd:cd05632 251 GCQEeGAGEVKRHPFFRNMNFKRLEAgmLDPPFVPDP 287
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
120-460 6.98e-49

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: 169.54  E-value: 6.98e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGmligRKKLVRAQT----EREILGLL----DHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKK----RIKMKQGETlalnERIMLSLVstggDCPFIVCMTYAFQTPDKLCFIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHI-LRQkqpgkH--FSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd05606  78 DLMNGGDLHYhLSQ-----HgvFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppCiDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfVGTH 348
Cdd:cd05606 146 ---------------------C-DFSKKKPHAS-------------------------------------------VGTH 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEII-RGDGHGSSVDWWTFGIFLYELLTGKTPF---KGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDP 424
Cdd:cd05606 161 GYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPD-SFSPELKSLLEGLLQRDV 239
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15242554 425 KKRLGFK-KGATEIKQHPFFNNVNWALI--RSTTPPEIP 460
Cdd:cd05606 240 SKRLGCLgRGATEVKEHPFFKGVDWQQVylQKYPPPLIP 278
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
104-461 8.43e-49

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: 171.33  E-value: 8.43e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 104 SKNED-LGLGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHP-FLPTLYSHF 181
Cdd:cd05615   1 SNNLDrVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPpFLTQLHSCF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ETEKFSCLLMEFCSGGDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd05615  81 QTVDRLYFVMEYVNGGDLmyHI---QQVGK-FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 LSLQSFVSptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptAA 339
Cdd:cd05615 157 MCKEHMVE----------------------------------------------------------------------GV 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 340 RSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGL 419
Cdd:cd05615 167 TTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK-SLSKEAVSICKGL 245
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15242554 420 LTKDPKKRLGF-KKGATEIKQHPFFNNVNWALI--RSTTPPEIPK 461
Cdd:cd05615 246 MTKHPAKRLGCgPEGERDIREHAFFRRIDWDKLenREIQPPFKPK 290
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
111-490 1.93e-48

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: 171.01  E-value: 1.93e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05627   1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptl 270
Cdd:cd05627  81 MEFLPGGDMMTLLMKK--DTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGL---------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqSTSQPSCHIASYcIQPPCIDPscklpvaciqPSCFKPRFLNNKpRKAKTEKAGSDSLpmliaeptaarSMSFVGTHEY 350
Cdd:cd05627 149 --CTGLKKAHRTEF-YRNLTHNP----------PSDFSFQNMNSK-RKAETWKKNRRQL-----------AYSTVGTPDY 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKF-PEGSISFAAKDLIRGLLTkDPKKR 427
Cdd:cd05627 204 IAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNwkETLVFpPEVPISEKAKDLILRFCT-DAENR 282
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 428 LGfKKGATEIKQHPFFNNVNWALIR---STTPPEIPKPIDLSILNETLKSSVQQQGKHSKQSDSSS 490
Cdd:cd05627 283 IG-SNGVEEIKSHPFFEGVDWEHIRerpAAIPIEIKSIDDTSNFDDFPESDILQPAPNTTEPDYKS 347
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
120-443 2.86e-48

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: 167.34  E-value: 2.86e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTE---------RE--ILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNDRGKiknalddvrREiaIMKKLDHPNIVRLYEVIDDPESDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLM--EFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfv 266
Cdd:cd14008  81 LYLvlEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsqpschiasyciqppcidpscklpvaciqpscfkprFLNNKPRKAKTEkagsdslpmliaeptaarsmsfvG 346
Cdd:cd14008 158 --------------------------------------------FEDGNDTLQKTA-----------------------G 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THEYLAPEIIRGDG---HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFP-EGSISFAAKDLIRGLLTK 422
Cdd:cd14008 171 TPAFLAPELCDGDSktySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPiPPELSPELKDLLRRMLEK 250
                       330       340
                ....*....|....*....|.
gi 15242554 423 DPKKRLGFKkgatEIKQHPFF 443
Cdd:cd14008 251 DPEKRITLK----EIKEHPWV 267
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
114-462 1.00e-46

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: 164.01  E-value: 1.00e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05631   2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSfvsptli 271
Cdd:cd05631  82 MNGGDLkfHIYNMGNPG--FDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaePTAARSMSFVGTHEYL 351
Cdd:cd05631 153 ----------------------------------------------------------------PEGETVRGRVGTVGYM 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPF---KGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd05631 169 APEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFrkrKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPKERL 248
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 429 GFK-KGATEIKQHPFFNNVNWALIRSTT--PPEIPKP 462
Cdd:cd05631 249 GCRgNGAAGVKQHPIFKNINFKRLEANMlePPFCPDP 285
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
113-427 1.61e-46

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: 162.63  E-value: 1.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMD-KGMliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlSNM--SEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDL--HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspt 269
Cdd:cd08215  79 EYADGGDLaqKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGIS-------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHE 349
Cdd:cd08215 151 ----------------------------------------KVLESTTDLAKT----------------------VVGTPY 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFN--VVGQPLKFPEG-SISFaaKDLIRGLLTKDPKK 426
Cdd:cd08215 169 YLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEAN-NLPALVYkiVKGQYPPIPSQySSEL--RDLVNSMLQKDPEK 245

                .
gi 15242554 427 R 427
Cdd:cd08215 246 R 246
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
114-462 1.72e-46

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: 163.27  E-value: 1.72e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05630   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLqsfvsptli 271
Cdd:cd05630  82 MNGGDLkfHIYHMGQAG--FPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAV--------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpscHIasyciqppcidpscklpvaciqpscfkPRFLNNKPRkaktekagsdslpmliaeptaarsmsfVGTHEYL 351
Cdd:cd05630 151 --------HV---------------------------PEGQTIKGR---------------------------VGTVGYM 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPF---KGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd05630 169 APEVVKNERYTFSPDWWALGCLLYEMIAGQSPFqqrKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDPAERL 248
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 429 GFK-KGATEIKQHPFFNNVNWALIRS--TTPPEIPKP 462
Cdd:cd05630 249 GCRgGGAREVKEHPLFKKLNFKRLGAgmLEPPFKPDP 285
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
113-427 3.21e-46

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: 161.60  E-value: 3.21e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptli 271
Cdd:cd14014  81 YVEGGSLAdLLRERGP---LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGI----------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKtekagsdslpmLIAEPTAARSMSFVGTHEYL 351
Cdd:cd14014 147 -----------------------------------------------AR-----------ALGDSGLTQTGSVLGTPAYM 168
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDL---IRGLLTKDPKKR 427
Cdd:cd14014 169 APEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALdaiILRALAKDPEER 247
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
114-443 5.52e-46

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: 161.15  E-value: 5.52e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMliGRKKLVRA-QTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd06606   2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSG--DSEEELEAlEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKqpGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptlIQ 272
Cdd:cd06606  80 YVPGGSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKR-------LA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 STSQPSChiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarSMSFVGTHEYLA 352
Cdd:cd06606 151 EIATGEG-------------------------------------------------------------TKSLRGTPYWMA 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG---QPLKFPEGsISFAAKDLIRGLLTKDPKKRLg 429
Cdd:cd06606 170 PEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKIGssgEPPPIPEH-LSEEAKDFLRKCLQRDPKKRP- 247
                       330
                ....*....|....
gi 15242554 430 fkkGATEIKQHPFF 443
Cdd:cd06606 248 ---TADELLQHPFL 258
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
109-460 1.02e-45

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: 163.66  E-value: 1.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 109 LGLGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIL-GLLDHPFLPTLYSHFETEKFS 187
Cdd:cd05618  17 LGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFeQASNHPFLVGLHSCFQTESRL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFvs 267
Cdd:cd05618  97 FFVIEYVNGGDLMFHMQRQ--RKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGL-- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsQPSCHIASYCiqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGT 347
Cdd:cd05618 173 --------RPGDTTSTFC------------------------------------------------------------GT 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 HEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRET--------LFNVV-GQPLKFPEgSISFAAKDLIRG 418
Cdd:cd05618 185 PNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNpdqntedyLFQVIlEKQIRIPR-SLSVKAASVLKS 263
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 419 LLTKDPKKRLGF--KKGATEIKQHPFFNNVNWALI--RSTTPPEIP 460
Cdd:cd05618 264 FLNKDPKERLGChpQTGFADIQGHPFFRNVDWDLMeqKQVVPPFKP 309
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
112-443 4.92e-45

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: 158.57  E-value: 4.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIgrKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd14081   1 GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLS--KESVLMKVEREIaiMKLIEHPNVLKLYDVYENKKYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsp 268
Cdd:cd14081  79 VLEYVSGGELfDYLVKKGR---LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGM-------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiASYCIQPPCIDPSCklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTH 348
Cdd:cd14081 148 -------------ASLQPEGSLLETSC--------------------------------------------------GSP 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14081 165 HYACPEVIKGEKyDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPH-FISPDAQDLLRRMLEVNPEKR 243
                       330
                ....*....|....*.
gi 15242554 428 LGFKkgatEIKQHPFF 443
Cdd:cd14081 244 ITIE----EIKKHPWF 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
120-441 1.59e-44

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: 155.89  E-value: 1.59e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLE--ELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 HILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpsc 279
Cdd:cd00180  79 KDLLKENKGP-LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLA------------------ 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 280 hiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsMSFVGTHEYLAPEIIRGD 359
Cdd:cd00180 140 ------------------------------KDLDSDDSLLKT--------------------TGGTTPPYYAPPELLGGR 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 360 GHGSSVDWWTFGIFLYELltgktpfkgngnretlfnvvgqplkfPEgsisfaAKDLIRGLLTKDPKKRLGFKkgatEIKQ 439
Cdd:cd00180 170 YYGPKVDIWSLGVILYEL--------------------------EE------LKDLIRRMLQYDPKKRPSAK----ELLE 213

                ..
gi 15242554 440 HP 441
Cdd:cd00180 214 HL 215
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
114-466 2.49e-44

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: 160.18  E-value: 2.49e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05626   3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqSFVSPTLIQS 273
Cdd:cd05626  83 IPGGDMMSLLIRM--EVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLC--TGFRWTHNSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQPSCHIASYCIQPPCI--DPScklpvaciqpSCFKPRFLNNKPRKAKTEKagsdslpmliaepTAARSMSFVGTHEYL 351
Cdd:cd05626 159 YYQKGSHIRQDSMEPSDLwdDVS----------NCRCGDRLKTLEQRATKQH-------------QRCLAHSLVGTPNYI 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFP-EGSISFAAKDLIrGLLTKDPKKRL 428
Cdd:cd05626 216 APEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINweNTLHIPpQVKLSPEAVDLI-TKLCCSAEERL 294
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242554 429 GfKKGATEIKQHPFFNNVNWAL-IRSTTPPEIPK---PIDLS 466
Cdd:cd05626 295 G-RNGADDIKAHPFFSEVDFSSdIRTQPAPYVPKishPMDTS 335
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
114-461 2.97e-43

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: 157.47  E-value: 2.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05621  54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptlIQS 273
Cdd:cd05621 134 MPGGDLVNLMSNY---DVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMK-------MDE 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQPSCHIAsyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfVGTHEYLAP 353
Cdd:cd05621 204 TGMVHCDTA--------------------------------------------------------------VGTPDYISP 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIR---GDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ--PLKFPEG-SISFAAKDLIRGLLTkDPKK 426
Cdd:cd05621 222 EVLKsqgGDGYyGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHknSLNFPDDvEISKHAKNLICAFLT-DREV 300
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242554 427 RLGfKKGATEIKQHPFFNN--VNWALIRSTTPPEIPK 461
Cdd:cd05621 301 RLG-RNGVEEIKQHPFFRNdqWNWDNIRETAAPVVPE 336
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
114-466 9.12e-43

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: 156.71  E-value: 9.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05624  74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDY 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd05624 154 YVGGDLLTLLSKFEDK-LPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG-------------- 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpSCFKprflnnkprkaktekagsdslpmlIAEPTAARSMSFVGTHEYLAP 353
Cdd:cd05624 219 -------------------------------SCLK------------------------MNDDGTVQSSVAVGTPDYISP 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRG--DG---HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFPE--GSISFAAKDLIRGLLTKDp 424
Cdd:cd05624 244 EILQAmeDGmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNheERFQFPShvTDVSEEAKDLIQRLICSR- 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15242554 425 KKRLGfKKGATEIKQHPFFNNVNWALIRSTTPPEIP---KPIDLS 466
Cdd:cd05624 323 ERRLG-QNGIEDFKKHAFFEGLNWENIRNLEAPYIPdvsSPSDTS 366
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
114-460 1.92e-42

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: 155.93  E-value: 1.92e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05622  75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd05622 155 MPGGDLVNLMSNY---DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-------------- 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpSCFKprflNNKPRKAKTEKAgsdslpmliaeptaarsmsfVGTHEYLAP 353
Cdd:cd05622 218 -------------------------------TCMK----MNKEGMVRCDTA--------------------VGTPDYISP 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIR---GDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ--PLKFPEGS-ISFAAKDLIRGLLTkDPKK 426
Cdd:cd05622 243 EVLKsqgGDGYyGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHknSLTFPDDNdISKEAKNLICAFLT-DREV 321
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15242554 427 RLGfKKGATEIKQHPFFNNVNWAL--IRSTTPPEIP 460
Cdd:cd05622 322 RLG-RNGVEEIKRHLFFKNDQWAWetLRDTVAPVVP 356
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
113-443 3.08e-42

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: 151.17  E-value: 3.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14099   2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd14099  82 LCSNGSLmELLKRRKA---LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLA---------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSdslpmliaeptaaRSMSFVGTHEYL 351
Cdd:cd14099 149 -----------------------------------------------ARLEYDGE-------------RKKTLCGTPNYI 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG-SISFAAKDLIRGLLTKDPKKRLg 429
Cdd:cd14099 169 APEVLEKKkGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlSISDEAKDLIRSMLQPDPTKRP- 247
                       330
                ....*....|....
gi 15242554 430 fkkGATEIKQHPFF 443
Cdd:cd14099 248 ---SLDEILSHPFF 258
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
113-441 3.23e-42

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: 150.94  E-value: 3.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMI--ENEVAILRRVKHPNIVQLIEEYDTDTELYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG----HIMLSDFDLslqsfv 266
Cdd:cd14095  79 LVKGGDLfdAI---TSSTK-FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGL------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsqpschiASYCIQPpcidpsckLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvG 346
Cdd:cd14095 149 ---------------ATEVKEP--------LFTVC--------------------------------------------G 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG-NGNRETLFNVV--GQpLKFPEGS---ISFAAKDLIRGLL 420
Cdd:cd14095 162 TPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpDRDQEELFDLIlaGE-FEFLSPYwdnISDSAKDLISRML 240
                       330       340
                ....*....|....*....|.
gi 15242554 421 TKDPKKRLgfkkGATEIKQHP 441
Cdd:cd14095 241 VVDPEKRY----SAGQVLDHP 257
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
96-496 3.61e-42

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 153.21  E-value: 3.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   96 DAIQNVKCSKNEDLGLGHFRLLKKLGCGDIGSVYLAELREmGCF--FAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPF 173
Cdd:PTZ00426  14 DSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKN-EDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  174 LPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHI 253
Cdd:PTZ00426  93 CVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRN--KRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  254 MLSDFDLslqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmli 333
Cdd:PTZ00426 171 KMTDFGF------------------------------------------------------------------------- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  334 AEPTAARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgnretlfnvvgQPL----KFPEGSIS 409
Cdd:PTZ00426 178 AKVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYAN-----------EPLliyqKILEGIIY 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  410 FA------AKDLIRGLLTKDPKKRLG-FKKGATEIKQHPFFNNVNWALIRSTTpPEIP-KPIDLSILNETLKSSVQQQGK 481
Cdd:PTZ00426 247 FPkfldnnCKHLMKKLLSHDLTKRYGnLKKGAQNVKEHPWFGNIDWVSLLHKN-VEVPyKPKYKNVFDSSNFERVQEDLT 325
                        410
                 ....*....|....*
gi 15242554  482 HSKQSDSSSGPYLDF 496
Cdd:PTZ00426 326 IADKITNENDPFFDW 340
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
113-443 6.18e-42

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: 150.05  E-value: 6.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKIN---LESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL-HILRQKqpGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd05122  78 FCSGGSLkDLLKNT--NKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLS---------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvACIQPSCFKprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYL 351
Cdd:cd05122 146 ----------------------------AQLSDGKTR---------------------------------NTFVGTPYWM 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLF-NVVGQPLKFPEG---SISFaaKDLIRGLLTKDPKKR 427
Cdd:cd05122 165 APEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFlIATNGPPGLRNPkkwSKEF--KDFLKKCLQKDPEKR 242
                       330
                ....*....|....*.
gi 15242554 428 LgfkkGATEIKQHPFF 443
Cdd:cd05122 243 P----TAEQLLKHPFI 254
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
114-478 1.75e-41

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: 152.50  E-value: 1.75e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05628   3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqS 273
Cdd:cd05628  83 LPGGDMMTLLMKK--DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGL------------C 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQPSCHIASYCIQppcIDPSCklpvaciqPSCFKPRFLNNKpRKAKTEKAGSDSLpmliaeptaarSMSFVGTHEYLAP 353
Cdd:cd05628 149 TGLKKAHRTEFYRN---LNHSL--------PSDFTFQNMNSK-RKAETWKRNRRQL-----------AFSTVGTPDYIAP 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKF-PEGSISFAAKDLIRGLLTkDPKKRLGf 430
Cdd:cd05628 206 EVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNwkETLIFpPEVPISEKAKDLILRFCC-EWEHRIG- 283
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 431 KKGATEIKQHPFFNNVNWALIR---STTPPEIPKPIDLSILNETLKSSVQQ 478
Cdd:cd05628 284 APGVEEIKTNPFFEGVDWEHIRerpAAIPIEIKSIDDTSNFDEFPDSDILK 334
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
114-466 7.80e-41

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: 150.97  E-value: 7.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspTLIQS 273
Cdd:cd05625  83 IPGGDMMSLLIRM--GVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC-------TGFRW 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQPSCHIASYCIQPPCIDPSCKL--PVACIQPSCFKPRflnnKPRKAKTEKagsdslpmliaeptAARSMSFVGTHEYL 351
Cdd:cd05625 154 THDSKYYQSGDHLRQDSMDFSNEWgdPENCRCGDRLKPL----ERRAARQHQ--------------RCLAHSLVGTPNYI 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF---PEGSISFAAKDLIRGlLTKDPKKRL 428
Cdd:cd05625 216 APEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLhipPQAKLSPEASDLIIK-LCRGPEDRL 294
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242554 429 GfKKGATEIKQHPFFNNVNWAL-IRSTTPPEIPK---PIDLS 466
Cdd:cd05625 295 G-KNGADEIKAHPFFKTIDFSSdLRQQSAPYIPKithPTDTS 335
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
114-466 8.96e-41

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: 151.32  E-value: 8.96e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05623  74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDY 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd05623 154 YVGGDLLTLLSKFEDR-LPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFG-------------- 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpSCFKprflnnkprkaktekagsdslpmLIAEPTAARSMSfVGTHEYLAP 353
Cdd:cd05623 219 -------------------------------SCLK-----------------------LMEDGTVQSSVA-VGTPDYISP 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRG--DG---HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG--QPLKFPE--GSISFAAKDLIRGLLTKDp 424
Cdd:cd05623 244 EILQAmeDGkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNhkERFQFPTqvTDVSENAKDLIRRLICSR- 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15242554 425 KKRLGfKKGATEIKQHPFFNNVNWALIRSTTPPEIPK---PIDLS 466
Cdd:cd05623 323 EHRLG-QNGIEDFKNHPFFVGIDWDNIRNCEAPYIPEvssPTDTS 366
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
114-461 4.15e-39

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: 143.51  E-value: 4.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVylaELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05607   7 FRVLGKGGFGEVCAV---QVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQPGKHFSELAarFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSfvsptli 271
Cdd:cd05607  84 MNGGDLkyHIYNVGERGIEMERVI--FYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnKPRKAKTEKAgsdslpmliaeptaarsmsfvGTHEYL 351
Cdd:cd05607 155 -------------------------------------------KEGKPITQRA---------------------GTNGYM 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR----ETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd05607 171 APEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKvskeELKRRTLEDEVKFEHQNFTEEAKDICRLFLAKKPENR 250
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15242554 428 LGFKKGATEIKQHPFFNNVNWALIRS--TTPPEIPK 461
Cdd:cd05607 251 LGSRTNDDDPRKHEFFKSINFPRLEAglIDPPFVPD 286
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
109-460 2.91e-38

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: 142.89  E-value: 2.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 109 LGLGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL---DHPFLPTLYSHFETEK 185
Cdd:cd05633   2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMTYAFHTPD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLMEFCSGGDLHiLRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsf 265
Cdd:cd05633  82 KLCFILDLMNGGDLH-YHLSQHGV-FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGL----- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vsptliqstsqpschiasyciqppcidpscklpvACiqpscfkpRFLNNKPRKAktekagsdslpmliaeptaarsmsfV 345
Cdd:cd05633 155 ----------------------------------AC--------DFSKKKPHAS-------------------------V 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEII-RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG-------NRETLFNVVGQPLKF-PEgsisfaAKDLI 416
Cdd:cd05633 168 GTHGYMAPEVLqKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdkheiDRMTLTVNVELPDSFsPE------LKSLL 241
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15242554 417 RGLLTKDPKKRLGFKKGAT-EIKQHPFFNNVNW--ALIRSTTPPEIP 460
Cdd:cd05633 242 EGLLQRDVSKRLGCHGRGAqEVKEHSFFKGIDWqqVYLQKYPPPLIP 288
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
114-460 2.88e-37

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: 139.41  E-value: 2.88e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL---DHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14223   2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVstgDCPFIVCMSYAFHTPDKLSFI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHiLRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptl 270
Cdd:cd14223  82 LDLMNGGDLH-YHLSQHGV-FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGL---------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvACiqpscfkpRFLNNKPRKAktekagsdslpmliaeptaarsmsfVGTHEY 350
Cdd:cd14223 150 -----------------------------AC--------DFSKKKPHAS-------------------------VGTHGY 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEII-RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG-------NRETLFNVVGQPLKF-PEgsisfaAKDLIRGLLT 421
Cdd:cd14223 168 MAPEVLqKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKtkdkheiDRMTLTMAVELPDSFsPE------LRSLLEGLLQ 241
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242554 422 KDPKKRLG-FKKGATEIKQHPFFNNVNWALI--RSTTPPEIP 460
Cdd:cd14223 242 RDVNRRLGcMGRGAQEVKEEPFFRGLDWQMVflQKYPPPLIP 283
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
113-445 8.10e-37

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: 136.57  E-value: 8.10e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMD-KGMLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd06623   2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHvDGDEEFRKQLLR---ELKTLRSCESPYVVKCYGAFYKEGEISIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLH-MMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfVSPTL 270
Cdd:cd06623  79 EYMDGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFG------ISKVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaEPTAARSMSFVGTHEY 350
Cdd:cd06623 151 ----------------------------------------------------------------ENTLDQCNTFVGTVTY 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR---ETLFNVVGQPLKF-PEGSISFAAKDLIRGLLTKDPKK 426
Cdd:cd06623 167 MSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPsffELMQAICDGPPPSlPAEEFSPEFRDFISACLQKDPKK 246
                       330
                ....*....|....*....
gi 15242554 427 RLgfkkGATEIKQHPFFNN 445
Cdd:cd06623 247 RP----SAAELLQHPFIKK 261
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
113-442 1.12e-35

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: 133.75  E-value: 1.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRA-QTEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLfQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG--HIMLSDFDLslqsfvspt 269
Cdd:cd14098  81 EYVEGGDLMDFIMAWGA--IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGL--------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSdslpMLIaeptaarsmSFVGTHE 349
Cdd:cd14098 150 -------------------------------------------------AKVIHTGT----FLV---------TFCGTMA 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRG------DGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFNVVGQ------PLKfpEGSISFAAKDLIR 417
Cdd:cd14098 168 YLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTGALPFDGS-SQLPVEKRIRKgrytqpPLV--DFNISEEAIDFIL 244
                       330       340
                ....*....|....*....|....*
gi 15242554 418 GLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14098 245 RLLDVDPEKRM----TAAQALDHPW 265
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
120-441 2.17e-35

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: 132.39  E-value: 2.17e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMligrKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD----KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 -HILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV--REDGHIMLSDFDLSLQsfvsptliqstsq 276
Cdd:cd14006  77 lDRLAERG---SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLadRPSPQIKIIDFGLARK------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcIDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEII 356
Cdd:cd14006 141 --------------LNPGEELKEIF--------------------------------------------GTPEFVAPEIV 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKRLgfkkG 433
Cdd:cd14006 163 NGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEeyfSSVSQEAKDFIRKLLVKEPRKRP----T 238

                ....*...
gi 15242554 434 ATEIKQHP 441
Cdd:cd14006 239 AQEALQHP 246
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
120-442 3.78e-34

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: 128.88  E-value: 3.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLigRKKLVRA-QTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGD 198
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKL--NKKLQENlESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 199 LHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENvmvredghIMLSDfdlslqsfvsptliqstsqps 278
Cdd:cd14009  79 LSQYIRKR--GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQN--------LLLST--------------------- 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 279 chiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagSDSLPML-IAEPTAARSMS-------FVGTHEY 350
Cdd:cd14009 128 -----------------------------------------------SGDDPVLkIADFGFARSLQpasmaetLCGSPLY 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV--VGQPLKFP-EGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14009 161 MAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIerSDAVIPFPiAAQLSPDCKDLLRRLLRRDPAER 240
                       330
                ....*....|....*
gi 15242554 428 LGFKkgatEIKQHPF 442
Cdd:cd14009 241 ISFE----EFFAHPF 251
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
116-442 2.31e-33

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: 126.98  E-value: 2.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMGCFFAMKVMDKgmlIGR--KKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14002   5 VLELIGEGSFGKVYKGRRKYTGQVVALKFIPK---RGKseKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGgDLH-ILrqkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliq 272
Cdd:cd14002  82 AQG-ELFqIL---EDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGF------------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaARSMSF-------- 344
Cdd:cd14002 146 ------------------------------------------------------------------ARAMSCntlvltsi 159
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFN-VVGQPLKFPEgSISFAAKDLIRGLLTKD 423
Cdd:cd14002 160 KGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTN-SIYQLVQmIVKDPVKWPS-NMSPEFKSFLQGLLNKD 237
                       330
                ....*....|....*....
gi 15242554 424 PKKRLGFkkgaTEIKQHPF 442
Cdd:cd14002 238 PSKRLSW----PDLLEHPF 252
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
120-441 3.02e-33

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: 126.57  E-value: 3.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKgmlIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKC---RKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 hILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VREDGH-IMLSDFDLSLQsfvsptliqstsqp 277
Cdd:cd14103  78 -FERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARK-------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 schiasyciqppcIDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIR 357
Cdd:cd14103 143 -------------YDPDKKLKVLF--------------------------------------------GTPEFVAPEVVN 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 358 GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS---ISFAAKDLIRGLLTKDPKKRLgfkkGA 434
Cdd:cd14103 166 YEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAfddISDEAKDFISKLLVKDPRKRM----SA 241

                ....*..
gi 15242554 435 TEIKQHP 441
Cdd:cd14103 242 AQCLQHP 248
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
111-442 6.47e-33

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: 125.84  E-value: 6.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLigRKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd14116   4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQL--EKAGVEHQLRREveIQSHLRHPNILRLYGYFHDATRVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHilRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSfvsp 268
Cdd:cd14116  82 LILEYAPLGTVY--RELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHA---- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaePTAARSmSFVGTH 348
Cdd:cd14116 156 -------------------------------------------------------------------PSSRRT-TLCGTL 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd14116 168 DYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPD-FVTEGARDLISRLLKHNPSQRP 246
                       330
                ....*....|....
gi 15242554 429 GFKkgatEIKQHPF 442
Cdd:cd14116 247 MLR----EVLEHPW 256
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
113-427 1.34e-32

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: 124.79  E-value: 1.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14083   4 KYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSL--ENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLhILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvspt 269
Cdd:cd14083  82 LVTGGEL-FDRIVEKGS-YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLS-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKAGSDSlpmliaepTAArsmsfvGTHE 349
Cdd:cd14083 152 --------------------------------------------------KMEDSGVMS--------TAC------GTPG 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFNvvgQPLK----FPE---GSISFAAKDLIRGLLTK 422
Cdd:cd14083 168 YVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFY-DENDSKLFA---QILKaeyeFDSpywDDISDSAKDFIRHLMEK 243

                ....*
gi 15242554 423 DPKKR 427
Cdd:cd14083 244 DPNKR 248
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
118-441 1.82e-32

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: 125.20  E-value: 1.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGML--IGRK---KLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14084  12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFtiGSRReinKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVR---EDGHIMLSDFDLSlqsfvspt 269
Cdd:cd14084  92 LMEGGEL--FDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSsqeEECLIKITDFGLS-------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLnnkprkaktekaGSDSLpMliaeptaaRSMsfVGTHE 349
Cdd:cd14084 162 ----------------------------------------KIL------------GETSL-M--------KTL--CGTPT 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDG---HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQPLKFPEG--SISFAAKDLIRGLLTK 422
Cdd:cd14084 179 YLAPEVLRSFGtegYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQIlsGKYTFIPKAwkNVSEEAKDLVKKMLVV 258
                       330
                ....*....|....*....
gi 15242554 423 DPKKRLgfkkGATEIKQHP 441
Cdd:cd14084 259 DPSRRP----SIEEALEHP 273
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
114-443 4.65e-32

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: 123.45  E-value: 4.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMG--CFFAMKVMDkgmligRKK---------LVRaqtEREILGLLDHPFLPTLYSHFE 182
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGlkEKVACKIID------KKKapkdflekfLPR---ELEILRKLRHPNIIQVYSIFE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 183 TEKFSCLLMEFCSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdl 260
Cdd:cd14080  73 RGSKVFIFMEYAEHGDLleYIQKRGA----LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDF-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 261 slqSFvsptliqstsqpschiASYCiqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSLPMLiaeptaar 340
Cdd:cd14080 147 ---GF----------------ARLC---------------------------------------PDDDGDVL-------- 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 341 SMSFVGTHEYLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG--SISFAAKDLIR 417
Cdd:cd14080 161 SKTFCGSAAYAAPEILQGIPyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSvkKLSPECKDLID 240
                       330       340
                ....*....|....*....|....*.
gi 15242554 418 GLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd14080 241 QLLEPDPTKRA----TIEEILNHPWL 262
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
114-443 5.35e-32

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: 123.18  E-value: 5.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKgmligrkklVRAQTE-------REI--LGLLDHPFLPTLYSHFETE 184
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSK---------KKAPEDylqkflpREIevIKGLKHPNLICFYEAIETT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqs 264
Cdd:cd14162  73 SRVYIIMELAENGDLLDYIRKN--GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGF---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcidpscklpvaciqpSCFKPRFLNNKPRKAKTekagsdslpmliaeptaarsmsF 344
Cdd:cd14162 147 ----------------------------------------ARGVMKTKDGKPKLSET----------------------Y 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRG---DGHGSsvDWWTFGIFLYELLTGKTPFkGNGNRETLFNVVGQPLKFPEG-SISFAAKDLIRGLL 420
Cdd:cd14162 165 CGSYAYASPEILRGipyDPFLS--DIWSMGVVLYTMVYGRLPF-DDSNLKVLLKQVQRRVVFPKNpTVSEECKDLILRML 241
                       330       340
                ....*....|....*....|...
gi 15242554 421 TKdPKKRLGFKkgatEIKQHPFF 443
Cdd:cd14162 242 SP-VKKRITIE----EIKRDPWF 259
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
114-442 6.53e-32

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: 123.17  E-value: 6.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligRKKLV-RAQTEREilglLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14010   2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSK---RPEVLnEVRLTHE----LKHPNVLKFYEWYETSNHLWLVVE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLH-ILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS-LQSFVSPTL 270
Cdd:cd14010  75 YCTGGDLEtLLRQD---GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArREGEILKEL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 IQSTSQPSchiasyciqppcidpscklpvaciqpscfkprflNNKPRKAKtekagsdslpmliaeptaarsMSFVGTHEY 350
Cdd:cd14010 152 FGQFSDEG----------------------------------NVNKVSKK---------------------QAKRGTPYY 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFP----EGSISFAAKDLIRGLLTKDPKK 426
Cdd:cd14010 177 MAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPppkvSSKPSPDFKSLLKGLLEKDPAK 256
                       330
                ....*....|....*.
gi 15242554 427 RLGFkkgaTEIKQHPF 442
Cdd:cd14010 257 RLSW----DELVKHPF 268
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
118-442 9.19e-32

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: 122.80  E-value: 9.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVM---DkgmliGRKKLVRA-QTEREILGLLDHPFLPTLYS---HFETekfSCLL 190
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKEIrfqD-----NDPKTIKEiADEMKVLEGLDHPNLVRYYGvevHREE---VYIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL-HILRQkqpGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvSPT 269
Cdd:cd06626  78 MEYCQEGTLeELLRH---GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-------SAV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 LIQSTSQPSCHiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaARSMSFVGTHE 349
Cdd:cd06626 148 KLKNNTTTMAP----------------------------------------------------------GEVNSLVGTPA 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGD---GHGSSVDWWTFGIFLYELLTGKTPF-KGNGNRETLFNVV-GQPLKFPEGS-ISFAAKDLIRGLLTKD 423
Cdd:cd06626 170 YMAPEVITGNkgeGHGRAADIWSLGCVVLEMATGKRPWsELDNEWAIMYHVGmGHKPPIPDSLqLSPEGKDFLSRCLESD 249
                       330
                ....*....|....*....
gi 15242554 424 PKKRLgfkkGATEIKQHPF 442
Cdd:cd06626 250 PKKRP----TASELLDHPF 264
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
114-457 2.86e-31

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: 121.51  E-value: 2.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLigRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14117   8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQI--EKEGVEHQLRREIeiQSHLRHPNILRLYNYFHDRKRIYLIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHilRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvSPTLi 271
Cdd:cd14117  86 EYAPRGELY--KELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH---APSL- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaaRSMSFVGTHEYL 351
Cdd:cd14117 160 --------------------------------------------------------------------RRRTMCGTLDYL 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd14117 172 PPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPP-FLSDGSRDLISKLLRYHPSERLPLK 250
                       330       340
                ....*....|....*....|....*.
gi 15242554 432 kgatEIKQHPFFNnvnwALIRSTTPP 457
Cdd:cd14117 251 ----GVMEHPWVK----ANSRRVLPP 268
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
114-443 3.59e-31

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: 121.28  E-value: 3.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREIL--GLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMK---RAPGDCPENIKKEVCiqKMLSHKNVVRFYGHRREGEFQYLFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd14069  80 EYASGGEL--FDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLA---------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpSCFKprfLNNKPRKaktekagsdslpmliaeptaarSMSFVGTHEYL 351
Cdd:cd14069 148 ---------------------------------TVFR---YKGKERL----------------------LNKMCGTLPYV 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPF---KGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14069 170 APELLAKKKyRAEPVDVWSCGIVLFAMLAGELPWdqpSDSCQEYSDWKENKKTYLTPWKKIDTAALSLLRKILTENPNKR 249
                       330
                ....*....|....*.
gi 15242554 428 LGFKkgatEIKQHPFF 443
Cdd:cd14069 250 ITIE----DIKKHPWY 261
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
113-443 4.89e-31

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: 120.41  E-value: 4.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMD-KGMLIGRKKLVRAqtEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISlEKIPKSDLKSVMG--EIDLLKKLNHPNIVKYIGSVKTKDSLYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILrQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptlI 271
Cdd:cd06627  79 EYVENGSLASI-IKKFGK-FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATK-------L 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 QSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaaRSMSFVGTHEYL 351
Cdd:cd06627 150 NEVEK---------------------------------------------------------------DENSVVGTPYWM 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP-LKFPEGsISFAAKDLIRGLLTKDPKKRlgf 430
Cdd:cd06627 167 APEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDhPPLPEN-ISPELRDFLLQCFQKDPTLR--- 242
                       330
                ....*....|...
gi 15242554 431 kKGATEIKQHPFF 443
Cdd:cd06627 243 -PSAKELLKHPWL 254
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
111-441 4.90e-31

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: 120.57  E-value: 4.90e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLigRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14078   2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAL--GDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsp 268
Cdd:cd14078  80 LEYCPGGELfdYIVAKDR----LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGL-------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpsCFKPrflnnkprkakteKAGSDSlpmliaeptaaRSMSFVGTH 348
Cdd:cd14078 148 -------------------------------------CAKP-------------KGGMDH-----------HLETCCGSP 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFNVVgQPLKFPEGS-ISFAAKDLIRGLLTKDPKK 426
Cdd:cd14078 167 AYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDD-NVMALYRKI-QSGKYEEPEwLSPSSKLLLDQMLQVDPKK 244
                       330
                ....*....|....*
gi 15242554 427 RLGFKkgatEIKQHP 441
Cdd:cd14078 245 RITVK----ELLNHP 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
113-442 7.58e-31

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: 120.05  E-value: 7.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14185   1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMI--ESEILIIKSLSHPNIVKLFEVYETEKEIYLILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLH--ILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDghimlsdfdlslqsfvsptl 270
Cdd:cd14185  79 YVRGGDLFdaIIESVK----FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHN-------------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkPRKAKTEKAGSDSLPMLIAEPTaarsMSFVGTHEY 350
Cdd:cd14185 135 ---------------------------------------------PDKSTTLKLADFGLAKYVTGPI----FTVCGTPTY 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG-NGNRETLFNVV--GQPLKFPE--GSISFAAKDLIRGLLTKDPK 425
Cdd:cd14185 166 VAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIqlGHYEFLPPywDNISEAAKDLISRLLVVDPE 245
                       330
                ....*....|....*..
gi 15242554 426 KRLgfkkGATEIKQHPF 442
Cdd:cd14185 246 KRY----TAKQVLQHPW 258
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
114-442 2.94e-30

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: 118.42  E-value: 2.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14186   3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLH--ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptli 271
Cdd:cd14186  83 CHNGEMSryLKNRKKP---FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQ-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpsCKLPvaciqpscfkprflnnkprkaktekagsdslpmliaeptAARSMSFVGTHEYL 351
Cdd:cd14186 152 -----------------------LKMP---------------------------------------HEKHFTMCGTPNYI 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFk 431
Cdd:cd14186 170 SPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPA-FLSREAQDLIHQLLRKNPADRLSL- 247
                       330
                ....*....|.
gi 15242554 432 kgaTEIKQHPF 442
Cdd:cd14186 248 ---SSVLDHPF 255
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
120-432 3.41e-30

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: 118.02  E-value: 3.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELR--EMgcffAMKVMDKGMLIGRKKlvRA-QTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd13999   1 IGSGSFGEVYKGKWRgtDV----AIKKLKVEDDNDELL--KEfRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLH-ILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqsts 275
Cdd:cd13999  75 GSLYdLLHKKK--IPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLS-------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaciqpscfkpRFLNNkprkaktekagsdslpmliaepTAARSMSFVGTHEYLAPEI 355
Cdd:cd13999 139 ----------------------------------RIKNS----------------------TTEKMTGVVGTPRWMAPEV 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPL--KFPEG-SISFaaKDLIRGLLTKDPKKRLGFKK 432
Cdd:cd13999 163 LRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLrpPIPPDcPPEL--SKLIKRCWNEDPEKRPSFSE 240
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
114-441 4.38e-30

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: 117.87  E-value: 4.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLH--ILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSPTLI 271
Cdd:cd14073  83 ASGGELYdyISERRR----LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS-NLYSKDKLL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 QstsqpschiaSYCiqppcidpscklpvaciqpscfkprflnnkprkaktekaGSdslPMliaeptaarsmsfvgtheYL 351
Cdd:cd14073 158 Q----------TFC---------------------------------------GS---PL------------------YA 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKG-NGNRETLFNVVGQPLKFPEGSISFAakdLIRGLLTKDPKKRlg 429
Cdd:cd14073 168 SPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGsDFKRLVKQISSGDYREPTQPSDASG---LIRWMLTVNPKRR-- 242
                       330
                ....*....|....
gi 15242554 430 fkkgAT--EIKQHP 441
Cdd:cd14073 243 ----ATieDIANHW 252
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
118-443 5.18e-30

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: 118.22  E-value: 5.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligRKKLVRAQTEREILGL---LDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd14106  14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRR---RGQDCRNEILHEIAVLelcKDCPRVVNLHEVYETRSELILILELA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHilRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd14106  91 AGGELQ--TLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGIS---------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKprkaktekagsdslpmliaepTAARSMsfVGTHEYL 351
Cdd:cd14106 159 --------------------------------------RVIGEG---------------------EEIREI--LGTPDYV 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd14106 178 APEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEelfKDVSPLAIDFIKRLLVKDPEKRL 257
                       330
                ....*....|....*
gi 15242554 429 gfkkGATEIKQHPFF 443
Cdd:cd14106 258 ----TAKECLEHPWL 268
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
120-442 2.15e-29

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: 115.96  E-value: 2.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIalLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DLHILRQKQpGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSfvsptliqstsqp 277
Cdd:cd06632  88 SIHKLLQRY-GA-FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHV------------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 schiasyciqppcidpscklpvaciqpscfkprflnNKPRKAKtekagsdslpmliaeptaarsmSFVGTHEYLAPEIIR 357
Cdd:cd06632 153 ------------------------------------EAFSFAK----------------------SFKGSPYWMAPEVIM 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 358 --GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPlKFPE--GSISFAAKDLIRGLLTKDPKKRlgfkKG 433
Cdd:cd06632 175 qkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSG-ELPPipDHLSPDAKDFIRLCLQRDPEDR----PT 249

                ....*....
gi 15242554 434 ATEIKQHPF 442
Cdd:cd06632 250 ASQLLEHPF 258
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
114-473 2.51e-29

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: 116.58  E-value: 2.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKgmligRKKLVRaqTEREIL---GllDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDK-----SKRDPS--EEIEILlryG--QHPNIITLRDVYDDGNSVYLV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH----IMLSDFDLSLQS 264
Cdd:cd14091  73 TELLRGGELldRILRQK----FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 FVSPTLIQStsqpschiasyciqpPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsf 344
Cdd:cd14091 149 RAENGLLMT---------------PCY----------------------------------------------------- 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 vgTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRET----LFNVVGQPLKFPEG---SISFAAKDLIR 417
Cdd:cd14091 161 --TANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFA-SGPNDTpeviLARIGSGKIDLSGGnwdHVSDSAKDLVR 237
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 418 GLLTKDPKKRLgfkkGATEIKQHPffnnvnWALIRSTTPPE-IPKPIDLSILNETLK 473
Cdd:cd14091 238 KMLHVDPSQRP----TAAQVLQHP------WIRNRDSLPQRqLTDPQDAALVKGAVA 284
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
113-443 7.13e-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: 114.76  E-value: 7.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmligrkkLVRAQTE-----REI--LGLLDHPFLPTLYSHFETEK 185
Cdd:cd06610   2 DYELIEVIGSGATAVVYAAYCLPKKEKVAIKRID---------LEKCQTSmdelrKEIqaMSQCNHPNVVSYYTSFVVGD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLMEFCSGGD-LHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqs 264
Cdd:cd06610  73 ELWLVMPLLSGGSlLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcidpscklpvACIqpscFKPRFLNNKPRKaktekagsdslpmliaeptaarsmSF 344
Cdd:cd06610 150 -----------------------------------ASL----ATGGDRTRKVRK------------------------TF 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV-GQPLKFPEG------SISFaaKDLI 416
Cdd:cd06610 167 VGTPCWMAPEVMEQVrGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLqNDPPSLETGadykkySKSF--RKMI 244
                       330       340
                ....*....|....*....|....*..
gi 15242554 417 RGLLTKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd06610 245 SLCLQKDPSKR----PTAEELLKHKFF 267
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
138-443 1.28e-28

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: 113.89  E-value: 1.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 138 CFFAMKVMDKgmligrKKLVR-----AQTEREI--LGLLDHPFLPTLYSHF---ETEKFScLLMEFCSGGDLHILRqKQP 207
Cdd:cd14119  19 CRRAVKILKK------RKLRRipngeANVKREIqiLRRLNHRNVIKLVDVLyneEKQKLY-MVMEYCVGGLQEMLD-SAP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 208 GKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS--LQSFVSPTLIqSTSQpschiasyc 285
Cdd:cd14119  91 DKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAeaLDLFAEDDTC-TTSQ--------- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 286 iqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIRGDG--HGS 363
Cdd:cd14119 161 ------------------------------------------------------------GSPAFQPPEIANGQDsfSGF 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 364 SVDWWTFGIFLYELLTGKTPFKGnGNRETLFNVVGQ-PLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14119 181 KVDIWSAGVTLYNMTTGKYPFEG-DNIYKLFENIGKgEYTIPD-DVDPDLQDLLRGMLEKDPEKRFTIE----QIRQHPW 254

                .
gi 15242554 443 F 443
Cdd:cd14119 255 F 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
107-442 1.33e-28

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: 114.05  E-value: 1.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKklgcgdigsvyLAELREMGCFFAMKVMDKGMLigrKKLVRAQTEREI--LGLLDHPFLPTLYSHFETE 184
Cdd:cd14074   9 ETLGRGHFAVVK-----------LARHVFTGEKVAVKVIDKTKL---DDVSKAHLFQEVrcMKLVQHPNVVRLYEVIDTQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDLH--ILRQkqpGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHIMLSDFDLS 261
Cdd:cd14074  75 TKLYLILELGDGGDMYdyIMKH---ENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 lQSFVsptliqstsqpschiasyciqppcidPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaars 341
Cdd:cd14074 152 -NKFQ--------------------------PGEKLETSC---------------------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 msfvGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLL 420
Cdd:cd14074 165 ----GSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPA-HVSPECKDLIRRML 239
                       330       340
                ....*....|....*....|..
gi 15242554 421 TKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14074 240 IRDPKKRASLE----EIENHPW 257
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
120-443 1.36e-28

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: 114.37  E-value: 1.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDK---GMLIGRKKLVRAQTEREILGLL---DHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14093  11 LGRGVSSTVRRCIEKETGQEFAVKIIDItgeKSSENEAEELREATRREIEILRqvsGHPNIIELHDVFESPTFIFLVFEL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliq 272
Cdd:cd14093  91 CRKGELfDYLTEVVT---LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR--------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcIDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLA 352
Cdd:cd14093 159 ------------------LDEGEKLRELC--------------------------------------------GTPGYLA 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIR------GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF--PE-GSISFAAKDLIRGLLTKD 423
Cdd:cd14093 177 PEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFgsPEwDDISDTAKDLISKLLVVD 256
                       330       340
                ....*....|....*....|
gi 15242554 424 PKKRLgfkkGATEIKQHPFF 443
Cdd:cd14093 257 PKKRL----TAEEALEHPFF 272
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-443 1.90e-28

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: 113.10  E-value: 1.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRkklvRAQTEREILGLL----DHPFLPTLYSHFETEKFS-- 187
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPK----AALREIKLLKHLndveGHPNIVKLLDVFEHRGGNhl 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCsGGDLHILRQKQPgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRED-GHIMLSDFDLSlqsfv 266
Cdd:cd05118  77 CLVFELM-GMNLYELIKDYP-RGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLA----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptlIQSTSQPSCHiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsFVG 346
Cdd:cd05118 150 ----RSFTSPPYTP---------------------------------------------------------------YVA 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV---GQPLkfpegsisfaAKDLIRGLLTK 422
Cdd:cd05118 163 TRWYRAPEVLLGAKPyGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVrllGTPE----------ALDLLSKMLKY 232
                       330       340
                ....*....|....*....|.
gi 15242554 423 DPKKRLgfkkGATEIKQHPFF 443
Cdd:cd05118 233 DPAKRI----TASQALAHPYF 249
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
114-442 2.30e-28

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: 113.27  E-value: 2.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmLIGRKKLVRaQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKE-QVAREGMVE-QIKREIaiMKLLRHPNIVELHEVMATKTKIFFVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSL--QSFVSPT 269
Cdd:cd14663  80 ELVTGGEL--FSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAlsEQFRQDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 LIQSTsqpsChiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHE 349
Cdd:cd14663 158 LLHTT----C------------------------------------------------------------------GTPN 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFNVVGQ-----PLKFPEGsisfaAKDLIRGLLTKD 423
Cdd:cd14663 168 YVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFD-DENLMALYRKIMKgefeyPRWFSPG-----AKSLIKRILDPN 241
                       330
                ....*....|....*....
gi 15242554 424 PKKRLGFkkgaTEIKQHPF 442
Cdd:cd14663 242 PSTRITV----EQIMASPW 256
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
120-441 2.36e-28

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: 113.61  E-value: 2.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLI-----------------GRKK---LVRAQTEREILGLLDHPFLPTLYS 179
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLkqagffrrppprrkpgaLGKPldpLDRVYREIAILKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 180 HFE--TEKFSCLLMEFCSGGDlhILRQkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSD 257
Cdd:cd14118  82 VLDdpNEDNLYMVFELVDKGA--VMEV-PTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakTEKAGSDSLpmliAEPT 337
Cdd:cd14118 159 FGVS-----------------------------------------------------------NEFEGDDAL----LSST 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 AarsmsfvGTHEYLAPEIIRGDG---HGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFN-VVGQPLKFPEG-SISFAA 412
Cdd:cd14118 176 A-------GTPAFMAPEALSESRkkfSGKALDIWAMGVTLYCFVFGRCPFEDD-HILGLHEkIKTDPVVFPDDpVVSEQL 247
                       330       340
                ....*....|....*....|....*....
gi 15242554 413 KDLIRGLLTKDPKKRLGFkkgaTEIKQHP 441
Cdd:cd14118 248 KDLILRMLDKNPSERITL----PEIKEHP 272
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
114-463 2.47e-28

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: 113.49  E-value: 2.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmligrkkLVRAQTE-----REILglldhpFLPTLYSHFETEKFSC 188
Cdd:cd06609   3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVID---------LEEAEDEiediqQEIQ------FLSQCDSPYITKYYGS 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LL--------MEFCSGGD-LHILRqkqPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd06609  68 FLkgsklwiiMEYCGGGSvLDLLK---PGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 LSLQsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprfLNNKPRKAKTekagsdslpmliaeptaa 339
Cdd:cd06609 144 VSGQ------------------------------------------------LTSTMSKRNT------------------ 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 340 rsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ-PLKFPEGSISFAAKDLIRG 418
Cdd:cd06609 158 ----FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNnPPSLEGNKFSKPFKDFVEL 233
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15242554 419 LLTKDPKKRLgfkkGATEIKQHPFfnnvnwalIRSTTPPEIPKPI 463
Cdd:cd06609 234 CLNKDPKERP----SAKELLKHKF--------IKKAKKTSYLTLL 266
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
111-443 3.91e-28

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: 112.36  E-value: 3.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14079   1 IGNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL--HILRQkqpGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd14079  81 MEYVSGGELfdYIVQK---GR-LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpscHIASyciqppciDPscklpvACIQPSCfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTH 348
Cdd:cd14079 150 -----------NIMR--------DG------EFLKTSC---------------------------------------GSP 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKgNGNRETLF-NVVGQPLKFPeGSISFAAKDLIRGLLTKDPKK 426
Cdd:cd14079 166 NYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFD-DEHIPNLFkKIKSGIYTIP-SHLSPGARDLIKRMLVVDPLK 243
                       330
                ....*....|....*..
gi 15242554 427 RLGFKkgatEIKQHPFF 443
Cdd:cd14079 244 RITIP----EIRQHPWF 256
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-442 9.00e-28

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: 112.53  E-value: 9.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLA-ELREMGCFFAMKVMDKGML--IGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVRKADLssDNLKGSSRANILKEvqIMKRLSHPNIVKLLDFQESDEYYY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENV--------------------M 246
Cdd:cd14096  83 IVLELADGGEIfhQIVRLT----YFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLlfepipfipsivklrkadddE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 247 VRED-------------GHIMLSDFDLSLQSFVSPTliqstsqpschiasyciQPPCidpscklpvaciqpscfkprfln 313
Cdd:cd14096 159 TKVDegefipgvggggiGIVKLADFGLSKQVWDSNT-----------------KTPC----------------------- 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 314 nkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETL 393
Cdd:cd14096 199 --------------------------------GTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFY-DESIETL 245
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15242554 394 FNVVGQP----LKFPEGSISFAAKDLIRGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14096 246 TEKISRGdytfLSPWWDEISKSAKDLISHLLTVDPAKRYDID----EFLAHPW 294
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
113-442 2.46e-27

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: 110.65  E-value: 2.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIG-RKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd14105   6 FYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsRRGVSREDIEREvsILRQVLHPNIITLHDVFENKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG----HIMLSDFDLSLQs 264
Cdd:cd14105  86 ILELVAGGELfDFLAEKES---LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAHK- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcIDPSCKlpvaciqpscFKPRFlnnkprkaktekagsdslpmliaeptaarsmsf 344
Cdd:cd14105 162 --------------------------IEDGNE----------FKNIF--------------------------------- 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 vGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLT 421
Cdd:cd14105 173 -GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDeyfSNTSELAKDFIRQLLV 251
                       330       340
                ....*....|....*....|.
gi 15242554 422 KDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14105 252 KDPRKRMTIQ----ESLRHPW 268
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
114-456 6.83e-27

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: 109.70  E-value: 6.83e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLvraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSL---ENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvsp 268
Cdd:cd14166  82 VSGGELfdRILERGV----YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLS------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKAGSDSlpmliaepTAArsmsfvGTH 348
Cdd:cd14166 151 ---------------------------------------------------KMEQNGIMS--------TAC------GTP 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFNvvgqplKFPEG----------SISFAAKDLIRG 418
Cdd:cd14166 166 GYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY-EETESRLFE------KIKEGyyefespfwdDISESAKDFIRH 238
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15242554 419 LLTKDPKKRLGFKKGAteikQHPFFNNvNWALIRSTTP 456
Cdd:cd14166 239 LLEKNPSKRYTCEKAL----SHPWIIG-NTALHRDIYP 271
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
114-442 9.98e-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: 109.21  E-value: 9.98e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMV--ENEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVR---EDGHIMLSDFDLSLqsfvsp 268
Cdd:cd14169  83 VTGGELfdRIIERG----SYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK------ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcIDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTH 348
Cdd:cd14169 153 ----------------------IEAQGMLSTAC--------------------------------------------GTP 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPK 425
Cdd:cd14169 167 GYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywDDISESAKDFIRHLLERDPE 246
                       330
                ....*....|....*..
gi 15242554 426 KRLGFKKGAteikQHPF 442
Cdd:cd14169 247 KRFTCEQAL----QHPW 259
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
114-427 1.13e-26

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: 108.27  E-value: 1.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMD-KGMliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDiSRM--SRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd08529  80 YAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVA----------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLA 352
Cdd:cd08529 149 -------------------------------------KILSDTTNFAQT----------------------IVGTPYYLS 169
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV-GqplKFPEGSISFAAK--DLIRGLLTKDPKKR 427
Cdd:cd08529 170 PELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVrG---KYPPISASYSQDlsQLIDSCLTKDYRQR 244
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
120-442 1.24e-26

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: 108.58  E-value: 1.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSI--ENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 hILRQKQPGkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM---VREDGHIMLSDFDLSlqsfvsptliqstsq 276
Cdd:cd14167  89 -FDRIVEKG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLS--------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKAGSdslpmliAEPTAArsmsfvGTHEYLAPEII 356
Cdd:cd14167 152 -------------------------------------------KIEGSGS-------VMSTAC------GTPGYVAPEVL 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKRLGFKKG 433
Cdd:cd14167 176 AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywDDISDSAKDFIQHLMEKDPEKRFTCEQA 255

                ....*....
gi 15242554 434 AteikQHPF 442
Cdd:cd14167 256 L----QHPW 260
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
107-442 1.39e-26

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: 108.57  E-value: 1.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKLGCGDIGSVYLAElremgcfFAMKVMDKGmliGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFETE 184
Cdd:cd14194  11 EELGSGQFAVVKKCREKSTGLQYAAK-------FIKKRRTKS---SRRGVSREDIEREvsILKEIQHPNVITLHEVYENK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG----HIMLSDFD 259
Cdd:cd14194  81 TDVILILELVAGGELfDFLAEKES---LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 LSLQsfvsptliqstsqpschiasyciqppcIDpscklpvaciqpscFKPRFLNnkprkaktekagsdslpmliaeptaa 339
Cdd:cd14194 158 LAHK---------------------------ID--------------FGNEFKN-------------------------- 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 340 rsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLI 416
Cdd:cd14194 171 ----IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeyfSNTSALAKDFI 246
                       330       340
                ....*....|....*....|....*.
gi 15242554 417 RGLLTKDPKKRLGFKKGAteikQHPF 442
Cdd:cd14194 247 RRLLVKDPKKRMTIQDSL----QHPW 268
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
113-428 1.41e-26

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: 108.55  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIG-RKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd14195   6 HYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSsRRGVSREEIEREvnILREIQHPNIITLHDIFENKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVredghimlsdfdlslqsfvsp 268
Cdd:cd14195  86 ILELVSGGELfDFLAEKES---LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIML--------------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tLIQSTSQPSCHIASYCIqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSDSlpmliaeptaarsMSFVGTH 348
Cdd:cd14195 142 -LDKNVPNPRIKLIDFGI--------------------------------AHKIEAGNEF-------------KNIFGTP 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPK 425
Cdd:cd14195 176 EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEeyfSNTSELAKDFIRRLLVKDPK 255

                ...
gi 15242554 426 KRL 428
Cdd:cd14195 256 KRM 258
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
105-427 2.36e-26

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: 108.30  E-value: 2.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 105 KNEDLglghfRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdkgmLIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFE 182
Cdd:cd06620   3 KNQDL-----ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVI----HIDAKSSVRKQILRElqILHECHSPYIVSFYGAFL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 183 TEKFS-CLLMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLH-MMGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd06620  74 NENNNiIICMEYMDCGSLdKILKKKGP---FPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 lslqsfVSPTLIQStsqpschIAsyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaa 339
Cdd:cd06620 151 ------VSGELINS-------IA--------------------------------------------------------- 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 340 rsMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN-----------GNRETLFNVVGQPL-KFPEGS 407
Cdd:cd06620 161 --DTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSnddddgyngpmGILDLLQRIVNEPPpRLPKDR 238
                       330       340
                ....*....|....*....|.
gi 15242554 408 I-SFAAKDLIRGLLTKDPKKR 427
Cdd:cd06620 239 IfPKDLRDFVDRCLLKDPRER 259
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
105-428 2.39e-26

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: 108.97  E-value: 2.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 105 KNEDLGLGHFRLLKKlgCGDigsvylaelREMGCFFAMKVMDKGMligrkklvRAQTEREILGLL---DHPFLPTLYSHF 181
Cdd:cd14179  11 KDKPLGEGSFSICRK--CLH---------KKTNQEYAVKIVSKRM--------EANTQREIAALKlceGHPNIVKLHEVY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ETEKFSCLLMEFCSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDF 258
Cdd:cd14179  72 HDQLHTFLVMELLKGGEL--LERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLqsfvsptliqstsqpschiasycIQPPCIDPscklpvacIQPSCFkprflnnkprkaktekagsdslpmliaepta 338
Cdd:cd14179 150 GFAR-----------------------LKPPDNQP--------LKTPCF------------------------------- 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 arsmsfvgTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISF-------- 410
Cdd:cd14179 168 --------TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMKKIKQGDFSFegeawknv 239
                       330       340
                ....*....|....*....|
gi 15242554 411 --AAKDLIRGLLTKDPKKRL 428
Cdd:cd14179 240 sqEAKDLIQGLLTVDPNKRI 259
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
114-442 3.09e-26

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: 107.51  E-value: 3.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdKGMLIGRKK---LVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVL-KEISVGELQpdeTVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL--HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVReDGHIMLSDFDLSlqsfvsp 268
Cdd:cd08222  81 TEYCEGGDLddKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK-NNVIKVGDFGIS------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTH 348
Cdd:cd08222 153 -----------------------------------------RILMGTSDLATT----------------------FTGTP 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV-GQPLKFPEgSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd08222 170 YYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVeGETPSLPD-KYSKELNAIYSRMLNKDPALR 248
                       330
                ....*....|....*
gi 15242554 428 lgfkKGATEIKQHPF 442
Cdd:cd08222 249 ----PSAAEILKIPF 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
107-442 4.69e-26

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: 106.96  E-value: 4.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKlgCGDigsvylaelREMGCFFAMKVMDKGML-IGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFET 183
Cdd:cd14196  11 EELGSGQFAIVKK--CRE---------KSTGLEYAAKFIKKRQSrASRRGVSREEIEREvsILRQVLHPNIITLHDVYEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 184 EKFSCLLMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG----HIMLSDF 258
Cdd:cd14196  80 RTDVVLILELVSGGELfDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSlqsfvsptliqstsqpscHIASYCIQppcidpscklpvaciqpscFKPRFlnnkprkaktekagsdslpmliaepta 338
Cdd:cd14196 157 GLA------------------HEIEDGVE-------------------FKNIF--------------------------- 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 arsmsfvGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDL 415
Cdd:cd14196 173 -------GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEeffSHTSELAKDF 245
                       330       340
                ....*....|....*....|....*..
gi 15242554 416 IRGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14196 246 IRKLLVKETRKRLTIQ----EALRHPW 268
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
114-444 1.01e-25

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: 105.89  E-value: 1.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVM----DKGMligRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd06605   3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIrleiDEAL---QKQILR---ELDVLHKCNSPYIVGFYGAFYSEGDISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDLHILRQKQPGKHFSELAARFYAseVLLALEYLH-MMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsp 268
Cdd:cd06605  77 CMEYMDGGSLDKILKEVGRIPERILGKIAVA--VVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQ----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tLIQStsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTekagsdslpmliaeptaarsmsFVGTH 348
Cdd:cd06605 150 -LVDS--------------------------------------------LAKT----------------------FVGTR 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR------ETLFNVV-GQPLKFPEGSISFAAKDLIRGLLT 421
Cdd:cd06605 163 SYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVdEPPPLLPSGKFSPDFQDFVSQCLQ 242
                       330       340
                ....*....|....*....|...
gi 15242554 422 KDPKKRLGFKkgatEIKQHPFFN 444
Cdd:cd06605 243 KDPTERPSYK----ELMEHPFIK 261
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
113-444 1.21e-25

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: 105.37  E-value: 1.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmlIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd06614   1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMR----LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL-HILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptli 271
Cdd:cd06614  77 YMDGGSLtDIITQNP--VRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADF------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiaSYCiqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSM--SFVGTHE 349
Cdd:cd06614 142 -----------GFA------------------------------------------------AQLTKEKSKrnSVVGTPY 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ---PLKFPEgSISFAAKDLIRGLLTKDPKK 426
Cdd:cd06614 163 WMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPE-KWSPEFKDFLNKCLVKDPEK 241
                       330
                ....*....|....*...
gi 15242554 427 RlgfkKGATEIKQHPFFN 444
Cdd:cd06614 242 R----PSAEELLQHPFLK 255
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
118-443 2.65e-25

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: 104.52  E-value: 2.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMdkgmlIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLL-MEFCSG 196
Cdd:cd14109  10 EDEKRAAQGAPFHVTERSTGRNFLAQLR-----YGDPFLMR---EVDIHNSLDHPNIVQMHDAYDDEKLAVTViDNLAST 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL---HILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDgHIMLSDFDLSlqsfvsptliqs 273
Cdd:cd14109  82 IELvrdNLLPGKD---YYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQS------------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNkprkaktekagsDSLPMLIaeptaarsmsfVGTHEYLAP 353
Cdd:cd14109 146 ------------------------------------RRLLR------------GKLTTLI-----------YGSPEFVSP 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF---PEGSISFAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd14109 167 EIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFdssPLGNISDDARDFIKKLLVYIPESRLTV 246
                       330
                ....*....|...
gi 15242554 431 KkgatEIKQHPFF 443
Cdd:cd14109 247 D----EALNHPWF 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
118-443 2.79e-25

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: 104.40  E-value: 2.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLiGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd14071   6 RTIGKGNFAVVKLARHRITKTEVAIKIIDKSQL-DEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqSTS 275
Cdd:cd14071  85 EIfdYLAQHG----RMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS-----------NFF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 QPSCHIASYCIQPPcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgtheYLAPEI 355
Cdd:cd14071 150 KPGELLKTWCGSPP------------------------------------------------------------YAAPEV 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKKga 434
Cdd:cd14071 170 FEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPF-FMSTDCEHLIRRMLVLDPSKRLTIEQ-- 246

                ....*....
gi 15242554 435 teIKQHPFF 443
Cdd:cd14071 247 --IKKHKWM 253
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
120-442 5.01e-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: 5.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRaqtEREILGLLD-HPFLPTLYSHFETEKFSCLLMEFCSGGD 198
Cdd:cd14090  10 LGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFR---EVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRGGP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 199 L--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIM---LSDFDLslqsfvsptliqs 273
Cdd:cd14090  87 LlsHIEKRV----HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpvkICDFDL------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiASyciqppcidpscklpvaciqpscfKPRFLNNKPRKAKTekagsdslPMLiaeptaarsMSFVGTHEYLAP 353
Cdd:cd14090 150 --------GS------------------------GIKLSSTSMTPVTT--------PEL---------LTPVGSAEYMAP 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIR---GDGH--GSSVDWWTFGIFLYELLTGKTPFKGNGNR--------------ETLFNVV-GQPLKFPE---GSISF 410
Cdd:cd14090 181 EVVDafvGEALsyDKRCDLWSLGVILYIMLCGYPPFYGRCGEdcgwdrgeacqdcqELLFHSIqEGEYEFPEkewSHISA 260
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 411 AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14090 261 EAKDLISHLLVRDASQRY----TAEQVLQHPW 288
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
114-443 5.25e-25

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: 104.49  E-value: 5.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVM-----DKGmligrkklVRAQTEREI--LGLLDHPFLPTLYSHFETEKF 186
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIrldneEEG--------IPSTALREIslLKELKHPNIVKLLDVIHTENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGgDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFV 266
Cdd:cd07829  73 LYLVFEYCDQ-DLKKYLDKRPGP-LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLA-RAFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 SPtliqstsqpschIASYciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvg 346
Cdd:cd07829 150 IP------------LRTY-------------------------------------------------------------- 155
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THE-----YLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP--------LKFPEGSIS 409
Cdd:cd07829 156 THEvvtlwYRAPEILLGSKHySTAVDIWSVGCIFAELITGKPLFPGDSEIDQLfkiFQILGTPteeswpgvTKLPDYKPT 235
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 410 F-----------------AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07829 236 FpkwpkndlekvlprldpEGIDLLSKMLQYNPAKRI----SAKEALKHPYF 282
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
113-442 5.52e-25

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: 103.78  E-value: 5.52e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMlIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14097   2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREK-AGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL-HILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG-------HIMLSDFDLSLQS 264
Cdd:cd14097  81 LCEDGELkELLLRK---GFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 FvsptliqstsqpschiasyciqppcidpscKLPVACIQPSCfkprflnnkprkaktekagsdslpmliaeptaarsmsf 344
Cdd:cd14097 158 Y------------------------------GLGEDMLQETC-------------------------------------- 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 vGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGnGNRETLFNVVGQ-PLKFPE---GSISFAAKDLIRGLL 420
Cdd:cd14097 170 -GTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVA-KSEEKLFEEIRKgDLTFTQsvwQSVSDAAKNVLQQLL 247
                       330       340
                ....*....|....*....|..
gi 15242554 421 TKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14097 248 KVDPAHRM----TASELLDNPW 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
114-441 9.82e-25

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: 102.85  E-value: 9.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLvRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKERE-DSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd08530  81 APFGDLSklISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS---------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklPVAciqpscfkprflnnKPRKAKTEkagsdslpmliaeptaarsmsfVGTHEYL 351
Cdd:cd08530 151 --------------------------KVL--------------KKNLAKTQ----------------------IGTPLYA 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQplKFPEGSISFAA--KDLIRGLLTKDPKKRLg 429
Cdd:cd08530 169 APEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRG--KFPPIPPVYSQdlQQIIRSLLQVNPKKRP- 245
                       330
                ....*....|..
gi 15242554 430 fkkGATEIKQHP 441
Cdd:cd08530 246 ---SCDKLLQSP 254
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
114-427 1.47e-24

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: 102.60  E-value: 1.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGML--IGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLnpSSLQKLFR---EVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHIL-----RQKqpgkhfsELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfv 266
Cdd:cd14072  79 EYASGGEVFDYlvahgRMK-------EKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqSTSQPSCHIASYCIQPPcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvg 346
Cdd:cd14072 147 ------NEFTPGNKLDTFCGSPP--------------------------------------------------------- 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 theYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPK 425
Cdd:cd14072 164 ---YAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPF-YMSTDCENLLKKFLVLNPS 239

                ..
gi 15242554 426 KR 427
Cdd:cd14072 240 KR 241
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
120-443 1.54e-24

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: 102.69  E-value: 1.54e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQ---NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 hILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VREDGH-IMLSDFDLSLQsfvsptliqstsqp 277
Cdd:cd14190  89 -FERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcVNRTGHqVKIIDFGLARR-------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 schiasyciqppcidpscklpvaciqpscFKPRflnnkprkaktEKAgsdslpmliaeptaarSMSFvGTHEYLAPEIIR 357
Cdd:cd14190 154 -----------------------------YNPR-----------EKL----------------KVNF-GTPEFLSPEVVN 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 358 GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG---SISFAAKDLIRGLLTKDPKKRLgfkkGA 434
Cdd:cd14190 177 YDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEEtfeHVSDEAKDFVSNLIIKERSARM----SA 252

                ....*....
gi 15242554 435 TEIKQHPFF 443
Cdd:cd14190 253 TQCLKHPWL 261
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
114-443 1.87e-24

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 103.00  E-value: 1.87e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdkgmligRKKLVRAQ---TEREILGLL---DHPFLPTLYSHFETEKFS 187
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-------KKKFYSWEecmNLREVKSLRklnEHPNIVKLKEVFRENDEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLqsfvs 267
Cdd:cd07830  74 YFVFEYMEG-NLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAR----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsqpscHIASyciQPPCIDpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsFVGT 347
Cdd:cd07830 148 ------------EIRS---RPPYTD---------------------------------------------------YVST 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 HEYLAPEII-RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLF---NVVGQP----------------LKFPEG- 406
Cdd:cd07830 162 RWYRAPEILlRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYkicSVLGTPtkqdwpegyklasklgFRFPQFa 241
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 407 ---------SISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07830 242 ptslhqlipNASPEAIDLIKDMLRWDPKKRP----TASQALQHPYF 283
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
119-442 2.04e-24

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


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 101.98  E-value: 2.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLA----ELREMgcfFAMKVMDKgmligrKKLVRAQ-----TEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd14121   2 KLGSGTYATVYKAyrksGAREV---VAVKCVSK------SSLNKAStenllTEIELLKKLKHPHIVELKDFQWDEEHIYL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDLHI-LRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV--REDGHIMLSDFDLSlqsfv 266
Cdd:cd14121  73 IMEYCSGGDLSRfIRSR---RTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFA----- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsQpscHIasyciqppcidpscklpvaciqpscfkprflnnKPRKAKTEKAGSdslPMliaeptaarsmsfvg 346
Cdd:cd14121 145 ---------Q---HL---------------------------------KPNDEAHSLRGS---PL--------------- 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 theYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ-PLKFPEG-SISFAAKDLIRGLLTKDP 424
Cdd:cd14121 162 ---YMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSkPIEIPTRpELSADCRDLLLRLLQRDP 238
                       330
                ....*....|....*...
gi 15242554 425 KKRLGFKkgatEIKQHPF 442
Cdd:cd14121 239 DRRISFE----EFFAHPF 252
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
111-443 2.73e-24

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: 101.89  E-value: 2.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIgRKKLVRaqTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14114   1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHES-DKETVR--KEIQIMNQLHHPKLINLHDAFEDDNEMVLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM--VREDGHIMLSDFDLSLQsfvsp 268
Cdd:cd14114  78 LEFLSGGEL-FERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMctTKRSNEVKLIDFGLATH----- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcIDPscklpvaciqpscfkprflnNKPRKAKTekagsdslpmliaeptaarsmsfvGTH 348
Cdd:cd14114 152 ----------------------LDP--------------------KESVKVTT------------------------GTA 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS---ISFAAKDLIRGLLTKDPK 425
Cdd:cd14114 166 EFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAfsgISEEAKDFIRKLLLADPN 245
                       330
                ....*....|....*...
gi 15242554 426 KRLgfkkGATEIKQHPFF 443
Cdd:cd14114 246 KRM----TIHQALEHPWL 259
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
140-444 3.66e-24

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: 102.76  E-value: 3.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 140 FAMKVMDKgmligrkklvRAQTEREI--LGLLD-HPFLPTLYSHFETEKFSCLLMEFCSGGDLhiLRQKQPGKHFSELAA 216
Cdd:cd14092  34 FAVKIVSR----------RLDTSREVqlLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGEL--LERIRKKKRFTESEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 217 RFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppCIDP 293
Cdd:cd14092 102 SRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFA----------------------------RLKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 294 SCKLpvacIQPSCFkprflnnkprkaktekagsdSLPmliaeptaarsmsfvgtheYLAPEIIRGD----GHGSSVDWWT 369
Cdd:cd14092 154 ENQP----LKTPCF--------------------TLP-------------------YAAPEVLKQAlstqGYDESCDLWS 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 370 FGIFLYELLTGKTPFKGNGNRETLFNVVGqplKFPEGSISF----------AAKDLIRGLLTKDPKKRLgfkkGATEIKQ 439
Cdd:cd14092 191 LGVILYTMLSGQVPFQSPSRNESAAEIMK---RIKSGDFSFdgeewknvssEAKSLIQGLLTVDPSKRL----TMSELRN 263

                ....*
gi 15242554 440 HPFFN 444
Cdd:cd14092 264 HPWLQ 268
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
134-443 5.62e-24

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: 101.59  E-value: 5.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 134 REMGCFFAMKVMD---KGMLIGRKKLVRAQTEREILGL---LDHPFLPTLYSHFETEKFSCLLMEFCSGGDL-HILRQKQ 206
Cdd:cd14181  32 RHTGQEFAVKIIEvtaERLSPEQLEEVRSSTLKEIHILrqvSGHPSIITLIDSYESSTFIFLVFDLMRRGELfDYLTEKV 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 207 PgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsqpSCHiasyci 286
Cdd:cd14181 112 T---LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGF-----------------SCH------ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 287 qppcIDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIR------GDG 360
Cdd:cd14181 166 ----LEPGEKLRELC--------------------------------------------GTPGYLAPEILKcsmdetHPG 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 361 HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF--PE-GSISFAAKDLIRGLLTKDPKKRLgfkkGATEI 437
Cdd:cd14181 198 YGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssPEwDDRSSTVKDLISRLLVVDPEIRL----TAEQA 273

                ....*.
gi 15242554 438 KQHPFF 443
Cdd:cd14181 274 LQHPFF 279
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
114-445 6.09e-24

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: 101.73  E-value: 6.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGR--KKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14086   3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARdhQKLER---EARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLhilrqkqpgkhFSELAARFYASE---------VLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFD 259
Cdd:cd14086  80 DLVTGGEL-----------FEDIVAREFYSEadashciqqILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 LSLQSfvsptliqSTSQPSCHiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaa 339
Cdd:cd14086 149 LAIEV--------QGDQQAWF----------------------------------------------------------- 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 340 rsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFkGNGNRETLFNVV--GQpLKFPE---GSISFAAKD 414
Cdd:cd14086 162 ---GFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPF-WDEDQHRLYAQIkaGA-YDYPSpewDTVTPEAKD 236
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242554 415 LIRGLLTKDPKKRLgfkkGATEIKQHPFFNN 445
Cdd:cd14086 237 LINQMLTVNPAKRI----TAAEALKHPWICQ 263
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
112-442 9.17e-24

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: 100.60  E-value: 9.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKL------------VRAQTEREILGLLDHPFLPTLYS 179
Cdd:cd14077   1 GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKErekrlekeisrdIRTIREAALSSLLNHPHICRLRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 180 HFETEKFSCLLMEFCSGGDL--HILrqkQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSD 257
Cdd:cd14077  81 FLRTPNHYYMLFEYVDGGQLldYII---SHGK-LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSlqSFVSPTLIQSTSQPSCHIASyciqppcidpscklpvaciqpscfkPRFLNNKPrkaktekagsdslpmliaept 337
Cdd:cd14077 157 FGLS--NLYDPRRLLRTFCGSLYFAA-------------------------PELLQAQP--------------------- 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsfvgtheYLAPEiirgdghgssVDWWTFGIFLYELLTGKTPFKgNGNRETLFNVVGQ-PLKFPEgSISFAAKDLI 416
Cdd:cd14077 189 ------------YTGPE----------VDVWSFGVVLYVLVCGKVPFD-DENMPALHAKIKKgKVEYPS-YLSSECKSLI 244
                       330       340
                ....*....|....*....|....*.
gi 15242554 417 RGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14077 245 SRMLVVDPKKRATLE----QVLNHPW 266
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
120-432 1.19e-23

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: 100.18  E-value: 1.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDK-LRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDML 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 HILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG---HIMLSDFDLSlqsfvsptliqstsq 276
Cdd:cd14082  90 EMILSSEKGR-LPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFA--------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpMLIAEPTAARSMsfVGTHEYLAPEII 356
Cdd:cd14082 154 ------------------------------------------------------RIIGEKSFRRSV--VGTPAYLAPEVL 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFkgngNRETLFNVVGQPLKF-----PEGSISFAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd14082 178 RNKGYNRSLDMWSVGVIIYVSLSGTFPF----NEDEDINDQIQNAAFmyppnPWKEISPDAIDLINNLLQVKMRKRYSVD 253

                .
gi 15242554 432 K 432
Cdd:cd14082 254 K 254
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
114-442 1.36e-23

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: 99.72  E-value: 1.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14184   3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLI--ENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREdghimlsdfdlslqsfvsptliqs 273
Cdd:cd14184  81 VKGGDL--FDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCE------------------------ 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkprflnnKPRKAKTEKAGSDSLPMLIAEPTaarsMSFVGTHEYLAP 353
Cdd:cd14184 135 -----------------------------------------YPDGTKSLKLGDFGLATVVEGPL----YTVCGTPTYVAP 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGN-RETLFN--VVGQpLKFPE---GSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14184 170 EIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlQEDLFDqiLLGK-LEFPSpywDNITDSAKELISHMLQVNVEAR 248
                       330
                ....*....|....*
gi 15242554 428 LgfkkGATEIKQHPF 442
Cdd:cd14184 249 Y----TAEQILSHPW 259
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
114-427 2.07e-23

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: 99.26  E-value: 2.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREmGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDSS-GRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd14161  84 ASRGDLYdYISERQR---LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS----------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 STSQPSCHIASYCiqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLA 352
Cdd:cd14161 150 NLYNQDKFLQTYC------------------------------------------------------------GSPLYAS 169
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 353 PEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPegSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14161 170 PEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREP--TKPSDACGLIRWLLMVNPERR 243
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
111-442 2.22e-23

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: 100.04  E-value: 2.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLI-----------------------GRKKLVRAQTEREILG 167
Cdd:cd14199   1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMrqagfprrppprgaraapegctqPRGPIERVYQEIAILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 168 LLDHPFLPTLYSHFE--TEKFSCLLMEFCSGGDLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENV 245
Cdd:cd14199  81 KLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVMEVPTLKP---LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 246 MVREDGHIMLSDFDLSLQsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscFKprflnnkprkaktekaG 325
Cdd:cd14199 158 LVGEDGHIKIADFGVSNE-------------------------------------------FE----------------G 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 326 SDSLpmliaeptaarSMSFVGTHEYLAPEII---RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLK 402
Cdd:cd14199 179 SDAL-----------LTNTVGTPAFMAPETLsetRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQPLE 247
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242554 403 FPE-GSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14199 248 FPDqPDISDDLKDLLFRMLDKNPESRI----SVPEIKLHPW 284
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
170-445 4.60e-23

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 98.39  E-value: 4.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  170 DHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VR 248
Cdd:PHA03390  67 DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKE--GKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLyDR 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  249 EDGHIMLSDFDLSlqsfvsptliQSTSQPSCHiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsDs 328
Cdd:PHA03390 145 AKDRIYLCDYGLC----------KIIGTPSCY----------------------------------------------D- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  329 lpmliaeptaarsmsfvGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR----ETLFNVVGQPLKFP 404
Cdd:PHA03390 168 -----------------GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEeldlESLLKRQQKKLPFI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15242554  405 EgSISFAAKDLIRGLLTKDPKKRL-GFKkgatEIKQHPFFNN 445
Cdd:PHA03390 231 K-NVSKNANDFVQSMLKYNINYRLtNYN----EIIKHPFLKI 267
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
120-442 5.82e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 98.06  E-value: 5.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKIIKAR---SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 hILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV--REDGHIMLSDFDLSLQsfvsptliqstsqp 277
Cdd:cd14193  89 -FDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARR-------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 schiasyciqppcidpscklpvaciqpscFKPRflnnkprkaktEKAgsdslpmliaeptaarSMSFvGTHEYLAPEIIR 357
Cdd:cd14193 154 -----------------------------YKPR-----------EKL----------------RVNF-GTPEFLAPEVVN 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 358 GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKRLgfkkGA 434
Cdd:cd14193 177 YEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDeefADISEEAKDFISKLLIKEKSWRM----SA 252

                ....*...
gi 15242554 435 TEIKQHPF 442
Cdd:cd14193 253 SEALKHPW 260
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
107-445 5.91e-23

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: 98.93  E-value: 5.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKlgCgdigsVYLAELREmgcfFAMKVMDKGmligrkklvRAQTEREILGLL---DHPFLPTLYSHFET 183
Cdd:cd14178   9 EDIGIGSYSVCKR--C-----VHKATSTE----YAVKIIDKS---------KRDPSEEIEILLrygQHPNIITLKDVYDD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 184 EKFSCLLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREdghimlsdfdls 261
Cdd:cd14178  69 GKFVYLVMELMRGGELldRILRQK----CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMD------------ 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 lqsfvsptliQSTSQPSCHIASYCIqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSDSLpmliaeptaars 341
Cdd:cd14178 133 ----------ESGNPESIRICDFGF--------------------------------AKQLRAENGLL------------ 158
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 MSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFkGNGNRET---LFNVVGQPLKFPEG----SISFAAKD 414
Cdd:cd14178 159 MTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF-ANGPDDTpeeILARIGSGKYALSGgnwdSISDAAKD 237
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242554 415 LIRGLLTKDPKKRLgfkkGATEIKQHPFFNN 445
Cdd:cd14178 238 IVSKMLHVDPHQRL----TAPQVLRHPWIVN 264
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
137-443 6.14e-23

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 98.04  E-value: 6.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 137 GCF-FAMKVMDKG---------MLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL--HILRQ 204
Cdd:cd14107  13 GTFgFVKRVTHKGngeccaakfIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSEELldRLFLK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 205 KQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV----REDghIMLSDFDLSLQsfvsptliqstsqpsch 280
Cdd:cd14107  93 GV----VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsptRED--IKICDFGFAQE----------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 281 iasyciqppcIDPScklpvaciqpscfKPRFlnnkprkaktekagsdslpmliaeptaarsmSFVGTHEYLAPEIIRGDG 360
Cdd:cd14107 150 ----------ITPS-------------EHQF-------------------------------SKYGSPEFVAPEIVHQEP 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 361 HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF--PE-GSISFAAKDLIRGLLTKDPKKRlgfkKGATEI 437
Cdd:cd14107 176 VSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWdtPEiTHLSEDAKDFIKRVLQPDPEKR----PSASEC 251

                ....*.
gi 15242554 438 KQHPFF 443
Cdd:cd14107 252 LSHEWF 257
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
113-442 6.20e-23

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: 98.48  E-value: 6.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLI------------GRKK-----------LVRAQTEREILGLL 169
Cdd:cd14200   1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLkqygfprrppprGSKAaqgeqakplapLERVYQEIAILKKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 170 DHPFLPTLYSHFETEKFSCLLMEFcsggdlHILRQ----KQPGKH-FSELAARFYASEVLLALEYLHMMGVVYRDLKPEN 244
Cdd:cd14200  81 DHVNIVKLIEVLDDPAEDNLYMVF------DLLRKgpvmEVPSDKpFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 245 VMVREDGHIMLSDFDLSLQSFVSPTLIQSTSqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakteka 324
Cdd:cd14200 155 LLLGDDGHVKIADFGVSNQFEGNDALLSSTA------------------------------------------------- 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 325 gsdslpmliaeptaarsmsfvGTHEYLAPEIIRGDGH---GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPL 401
Cdd:cd14200 186 ---------------------GTPAFMAPETLSDSGQsfsGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPV 244
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242554 402 KFPEG-SISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14200 245 EFPEEpEISEELKDLILKMLDKNPETRI----TVPEIKVHPW 282
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
113-446 8.14e-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: 98.28  E-value: 8.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd06611   6 IWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE---SEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQpGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd06611  83 FCDGGALDSIMLEL-ERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVS----------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKagsdslpmliaepTAARSMSFVGTHEYLA 352
Cdd:cd06611 151 ----------------------------------------------AKNKS-------------TLQKRDTFIGTPYWMA 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEII-----RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV-------VGQPLKFpegSISFaaKDLIRGLL 420
Cdd:cd06611 172 PEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKIlksepptLDQPSKW---SSSF--NDFLKSCL 246
                       330       340
                ....*....|....*....|....*.
gi 15242554 421 TKDPKKRLgfkkGATEIKQHPFFNNV 446
Cdd:cd06611 247 VKDPDDRP----TAAELLKHPFVSDQ 268
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
114-442 9.79e-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: 98.36  E-value: 9.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligRKKLVRaqTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV---DKKIVR--TEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLhILRQKQPGkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvsptl 270
Cdd:cd14085  80 VTGGEL-FDRIVEKG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYatpAPDAPLKIADFGLS--------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqpPCIDPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEY 350
Cdd:cd14085 149 ------------------KIVDQQVTMKTVC--------------------------------------------GTPGY 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFN-VVGQPLKFPE---GSISFAAKDLIRGLLTKDPKK 426
Cdd:cd14085 167 CAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKrILNCDYDFVSpwwDDVSLNAKDLVKKLIVLDPKK 246
                       330
                ....*....|....*.
gi 15242554 427 RLgfkkGATEIKQHPF 442
Cdd:cd14085 247 RL----TTQQALQHPW 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
111-442 1.00e-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: 97.41  E-value: 1.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGR-KKLVraqtEREILGL--LDHPFLPTLYSHFETEKFS 187
Cdd:cd14075   1 IGFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKtQRLL----SREISSMekLHHPNIIRLYEVVETLSKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDL--HILRQkqpGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsf 265
Cdd:cd14075  77 HLVMEYASGGELytKISTE---GK-LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFS---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vsptliqSTSQPSCHIASYCIQPPcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfv 345
Cdd:cd14075 149 -------THAKRGETLNTFCGSPP-------------------------------------------------------- 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 gtheYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGngnrETlfnVVGQPLKFPEGS------ISFAAKDLIRG 418
Cdd:cd14075 166 ----YAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRA----ET---VAKLKKCILEGTytipsyVSEPCQELIRG 234
                       330       340
                ....*....|....*....|....
gi 15242554 419 LLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14075 235 ILQPVPSDRYSID----EIKNSEW 254
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
140-442 1.08e-22

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: 97.79  E-value: 1.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 140 FAMKVMDKgmligRKKLVRAQTEREILGLLD---HPFLPTLYSHFETE-KFSCLLMEFCSGGDL-HILRQKqpgkHFSEL 214
Cdd:cd14173  30 YAVKIIEK-----RPGHSRSRVFREVEMLYQcqgHRNVLELIEFFEEEdKFYLVFEKMRGGSILsHIHRRR----HFNEL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 215 AARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHI---MLSDFDLSlqsfvSPTLIQSTSQPschIASYCIQPPCi 291
Cdd:cd14173 101 EASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLG-----SGIKLNSDCSP---ISTPELLTPC- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 292 dpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIRGDGHGSSV-----D 366
Cdd:cd14173 172 ------------------------------------------------------GSAEYMAPEVVEAFNEEASIydkrcD 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 367 WWTFGIFLYELLTGKTPFKGN--------------GNRETLFNVVGQ-PLKFPE---GSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd14173 198 LWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeacpACQNMLFESIQEgKYEFPEkdwAHISCAAKDLISKLLVRDAKQRL 277
                       330
                ....*....|....
gi 15242554 429 gfkkGATEIKQHPF 442
Cdd:cd14173 278 ----SAAQVLQHPW 287
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
134-428 1.29e-22

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: 98.02  E-value: 1.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 134 REMGCFFAMKVMDKGMligrkklvRAQTEREILGLL---DHPFLPTLYSHFETEKFSCLLMEFCSGGDL--HILRQKqpg 208
Cdd:cd14180  28 RQSGQEYAVKIISRRM--------EANTQREVAALRlcqSHPNIVALHEVLHDQYHTYLVMELLRGGELldRIKKKA--- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 209 kHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH---IMLSDFDLSlqsfvspTLIQSTSQPschiasyc 285
Cdd:cd14180  97 -RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA-------RLRPQGSRP-------- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 286 IQPPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgTHEYLAPEIIRGDGHGSSV 365
Cdd:cd14180 161 LQTPCF-------------------------------------------------------TLQYAAPELFSNQGYDESC 185
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 366 DWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISF----------AAKDLIRGLLTKDPKKRL 428
Cdd:cd14180 186 DLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKEGDFSLegeawkgvseEAKDLVRGLLTVDPAKRL 258
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
113-443 1.37e-22

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 96.99  E-value: 1.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKV--MDKGmligrKKLVRAQTEREILGLLDHPFLPTLY-SHFETEKFsCL 189
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVikLEPG-----DDFEIIQQEISMLKECRHPNIVAYFgSYLRRDKL-WI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvspt 269
Cdd:cd06613  75 VMEYCGGGSLQDIYQVT--GPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQ------ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprfLNNkprkaktekagsdslpmliaepTAARSMSFVGTHE 349
Cdd:cd06613 147 ------------------------------------------LTA----------------------TIAKRKSFIGTPY 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEII---RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLF---NVVGQPLKFPEGSI-SFAAKDLIRGLLTK 422
Cdd:cd06613 163 WMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFlipKSNFDPPKLKDKEKwSPDFHDFIKKCLTK 242
                       330       340
                ....*....|....*....|.
gi 15242554 423 DPKKRlgfkKGATEIKQHPFF 443
Cdd:cd06613 243 NPKKR----PTATKLLQHPFV 259
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
113-427 1.44e-22

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: 97.36  E-value: 1.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdkgmLIGRKKLVRAQTEREI--LGLLDHPF----------LPTLYsh 180
Cdd:cd13996   7 DFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKI----RLTEKSSASEKVLREVkaLAKLNHPNivryytawveEPPLY-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 181 fetekfscLLMEFCSGGDL-HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHIMLSDF 258
Cdd:cd13996  81 --------IQMELCEGGTLrDWIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVKIGDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnKPRKAKTEKAGSDSLPMLIAepTA 338
Cdd:cd13996 153 GLA-----------------------------------------------------TSIGNQKRELNNLNNNNNGN--TS 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 ARSmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLtgkTPFKGNGNRETLFNVVGQpLKFPEgsiSFAAK----- 413
Cdd:cd13996 178 NNS-VGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKTAMERSTILTDLRN-GILPE---SFKAKhpkea 249
                       330
                ....*....|....
gi 15242554 414 DLIRGLLTKDPKKR 427
Cdd:cd13996 250 DLIQSLLSKNPEER 263
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
114-443 1.57e-22

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: 96.57  E-value: 1.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMD-KGMLIGRKKlvraqtEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPvEEDLQEIIK------EISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGG---DLHILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvspt 269
Cdd:cd06612  79 YCGAGsvsDIMKITNKT----LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQ------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprfLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHE 349
Cdd:cd06612 149 ------------------------------------------LTDTMAKRNT----------------------VIGTPF 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEG-SISFaaKDLIRGLLTKDPK 425
Cdd:cd06612 165 WMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPpptLSDPEKwSPEF--NDFVKKCLVKDPE 242
                       330
                ....*....|....*...
gi 15242554 426 KRlgfkKGATEIKQHPFF 443
Cdd:cd06612 243 ER----PSAIQLLQHPFI 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
113-444 1.90e-22

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: 97.19  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMK--VMDKgmligRKKlvraQTEREILGLLDHPFLPTLYSHFET------E 184
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDK-----RYK----NRELQIMRRLKHPNIVKLKYFFYSsgekkdE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGgDLH-ILRQK-QPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHIMLSDFdls 261
Cdd:cd14137  76 VYLNLVMEYMPE-TLYrVIRHYsKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDF--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 lqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSLpMLIAEPtaarS 341
Cdd:cd14137 152 ---------------------------------------------------------------GSAKR-LVPGEP----N 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 MSFVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP--------------LKF 403
Cdd:cd14137 164 VSYICSRYYRAPELIFGATDyTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLveiIKVLGTPtreqikamnpnyteFKF 243
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242554 404 PEG-----------SISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFN 444
Cdd:cd14137 244 PQIkphpwekvfpkRTPPDAIDLLSKILVYNPSKRL----TALEALAHPFFD 291
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
120-442 2.24e-22

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: 96.45  E-value: 2.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMliGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKC--RGREVC--ESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 HIlRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH---IMLSDFDLSLqsfvsptliQSTSQ 276
Cdd:cd14087  85 FD-RIIAKGS-FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLAS---------TRKKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 PSCHIASYCiqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEII 356
Cdd:cd14087 154 PNCLMKTTC------------------------------------------------------------GTPEYIAPEIL 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFNVV--------GQPLKfpegSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd14087 174 LRKPYTQSVDMWAVGVIAYILLSGTMPFD-DDNRTRLYRQIlrakysysGEPWP----SVSNLAKDFIDRLLTVNPGERL 248
                       330
                ....*....|....
gi 15242554 429 gfkkGATEIKQHPF 442
Cdd:cd14087 249 ----SATQALKHPW 258
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
115-427 2.41e-22

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: 96.54  E-value: 2.41e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELREMgcfFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd14187  13 RFLGKGGFAKCYEITDADTKEV---FAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqst 274
Cdd:cd14187  90 RRRSLLELHKRR--KALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLA------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSdslpmliaeptaaRSMSFVGTHEYLAPE 354
Cdd:cd14187 155 --------------------------------------------TKVEYDGE-------------RKKTLCGTPNYIAPE 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14187 178 VLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK-HINPVAASLIQKMLQTDPTAR 249
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
114-445 2.68e-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: 97.23  E-value: 2.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREasICHMLKHPHIVELLETYSSDGMLYMVF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDL--HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENvmvredghIMLSDFDLSlqsfvSPT 269
Cdd:cd14094  85 EFMDGADLcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHC--------VLLASKENS-----APV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 LIqstsqpschiasyciqppcidpsCKLPVAciqpscfkprflnnkprkakTEKAGSDSLpmliaepTAARsmsfVGTHE 349
Cdd:cd14094 152 KL-----------------------GGFGVA--------------------IQLGESGLV-------AGGR----VGTPH 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRetLFNVVGQ---PLKFPEG-SISFAAKDLIRGLLTKDPK 425
Cdd:cd14094 178 FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER--LFEGIIKgkyKMNPRQWsHISESAKDLVRRMLMLDPA 255
                       330       340
                ....*....|....*....|
gi 15242554 426 KRLgfkkGATEIKQHPFFNN 445
Cdd:cd14094 256 ERI----TVYEALNHPWIKE 271
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
114-431 4.55e-22

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: 95.26  E-value: 4.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   114 FRLLKKLGCGDIGSVYLAELREMGCFF----AMKVMDKG-MLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEGaDEEEREDFLE---EASIMKKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   189 LLMEFCSGGDLH-ILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvs 267
Cdd:pfam07714  78 IVTEYMPGGDLLdFLRKHKRKLTLKDLLS--MALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLS------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   268 pTLIQSTSQPSCHiasyciqppcidPSCKLPVAciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgt 347
Cdd:pfam07714 150 -RDIYDDDYYRKR------------GGGKLPIK----------------------------------------------- 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   348 heYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLKFPEG---SIsfaaKDLIRGLLTK 422
Cdd:pfam07714 170 --WMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEdGYRLPQPENcpdEL----YDLMKQCWAY 243

                  ....*....
gi 15242554   423 DPKKRLGFK 431
Cdd:pfam07714 244 DPEDRPTFS 252
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
113-443 6.81e-22

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: 94.92  E-value: 6.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKK--LVraqTEREILGLLDHPFLPTLYSHFETEKFSCL- 189
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKqqLV---SEVNILRELKHPNIVRYYDRIVDRANTTLy 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 -LMEFCSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHM-----MGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd08217  78 iVMEYCEGGDLAqlIKKCKKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGLA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 lqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaars 341
Cdd:cd08217 158 ------------------------------------------------RVLSHDSSFAKT-------------------- 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 msFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV-VGQPLKFPEGsISFAAKDLIRGLL 420
Cdd:cd08217 170 --YVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIkEGKFPRIPSR-YSSELNEVIKSML 246
                       330       340
                ....*....|....*....|...
gi 15242554 421 TKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd08217 247 NVDPDKR----PSVEELLQLPLI 265
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
115-443 7.13e-22

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: 94.73  E-value: 7.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmlIGR-----KKLVRA-QTEREILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd06625   3 KQGKLLGQGAFGQVYLCYDADTGRELAVKQVE----IDPinteaSKEVKAlECEIQLLKNLQHERIVQYYGCLQDEKSLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDL--HIlrqKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS--LQS 264
Cdd:cd06625  79 IFMEYMPGGSVkdEI---KAYGA-LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASkrLQT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 FVSPTLIQstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmSF 344
Cdd:cd06625 155 ICSSTGMK----------------------------------------------------------------------SV 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF--PEGsISFAAKDLIRGLLTK 422
Cdd:cd06625 165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPqlPPH-VSEDARDFLSLIFVR 243
                       330       340
                ....*....|....*....|.
gi 15242554 423 DPKKRlgfkKGATEIKQHPFF 443
Cdd:cd06625 244 NKKQR----PSAEELLSHSFV 260
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
115-431 8.63e-22

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: 94.54  E-value: 8.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    115 RLLKKLGCGDIGSVYLAELREMGCFF----AMKVMDKG-MLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGDGKevevAVKTLKEDaSEQQIEEFLR---EARIMRKLDHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    190 LMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVSPT 269
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    270 LIQStsqpschiasyciqppcidpSCKLPVAciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgthe 349
Cdd:smart00221 159 YKVK--------------------GGKLPIR------------------------------------------------- 169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLKFPEGsisfAAKDLIRGLLT---KDP 424
Cdd:smart00221 170 WMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKkGYRLPKPPN----CPPELYKLMLQcwaEDP 245

                   ....*..
gi 15242554    425 KKRLGFK 431
Cdd:smart00221 246 EDRPTFS 252
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
114-427 2.10e-21

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: 93.57  E-value: 2.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTE--REI---LGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPqlREIdlhRRVSRHPNIITLHDVFETEVAIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLH-ILRQKQPGKHFSELAARFyASEVLLALEYLHMMGVVYRDLKPENVMVRED-GHIMLSDFDLslqsfv 266
Cdd:cd13993  82 IVLEYCPNGDLFeAITENRIYVGKTELIKNV-FLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGL------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKagsdslpmliaeptaaRSMSF-V 345
Cdd:cd13993 155 ----------------------------------------------------ATTEK----------------ISMDFgV 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDGHGS------SVDWWTFGIFLYELLTGKTPFK-----------GNGNRETLFNVvgqplkFPegSI 408
Cdd:cd13993 167 GSEFYMAPECFDEVGRSLkgypcaAGDIWSLGIILLNLTFGRNPWKiasesdpifydYYLNSPNLFDV------IL--PM 238
                       330
                ....*....|....*....
gi 15242554 409 SFAAKDLIRGLLTKDPKKR 427
Cdd:cd13993 239 SDDFYNLLRQIFTVNPNNR 257
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
114-442 3.83e-21

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: 93.57  E-value: 3.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14168  12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSI--ENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLhILRQKQPGkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSlqsfvsptl 270
Cdd:cd14168  90 VSGGEL-FDRIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLS--------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKAGSdslpmliAEPTAArsmsfvGTHEY 350
Cdd:cd14168 159 -------------------------------------------------KMEGKGD-------VMSTAC------GTPGY 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14168 177 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywDDISDSAKDFIRNLMEKDPNKR 256
                       330
                ....*....|....*
gi 15242554 428 LGFKKGAteikQHPF 442
Cdd:cd14168 257 YTCEQAL----RHPW 267
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
162-428 4.77e-21

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: 92.76  E-value: 4.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLYSHFETEKFS-CLLMEFCSGGDLHILRQKqpGKHFSELAARFYASEVLLALEYLHMMGVVYRDL 240
Cdd:cd13994  47 EYIISSKLHHPNIVKVLDLCQDLHGKwCLVMEYCPGGDLFTLIEK--ADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDL 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 241 KPENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpSCFKPRFlnnkprkak 320
Cdd:cd13994 125 KPENILLDEDGVLKLTDFGTA-------------------------------------------EVFGMPA--------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 321 tekagsdslpmliaEPTAARSMSFVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ 399
Cdd:cd13994 153 --------------EKESPMSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEK 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15242554 400 PLKFPEGSISFA-------AKDLIRGLLTKDPKKRL 428
Cdd:cd13994 219 SGDFTNGPYEPIenllpseCRRLIYRMLHPDPEKRI 254
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
115-431 4.81e-21

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 92.59  E-value: 4.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    115 RLLKKLGCGDIGSVYLAELREMGCFF----AMKVMDKG-MLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGGKKkvevAVKTLKEDaSEQQIEEFLR---EARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    190 LMEFCSGGDLH-ILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsp 268
Cdd:smart00219  79 VMEYMEGGDLLsYLRKNRPKLSLSDLLS--FALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD----- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    269 tlIQSTSQpschiasYCIQppcidpSCKLPVAciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgth 348
Cdd:smart00219 152 --LYDDDY-------YRKR------GGKLPIR------------------------------------------------ 168
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554    349 eYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLKFPEGsisfAAKDLIRGLLT---KD 423
Cdd:smart00219 169 -WMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKnGYRLPQPPN----CPPELYDLMLQcwaED 243

                   ....*...
gi 15242554    424 PKKRLGFK 431
Cdd:smart00219 244 PEDRPTFS 251
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
118-443 5.94e-21

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: 92.00  E-value: 5.94e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DL-HILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliqstsq 276
Cdd:cd14188  87 SMaHILKAR---KVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAAR------------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYLAPEII 356
Cdd:cd14188 151 ---------------------------------------------------------LEPLEHRRRTICGTPNYLSPEVL 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKkgatE 436
Cdd:cd14188 174 NKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPS-SLLAPAKHLIASMLSKNPEDRPSLD----E 248

                ....*..
gi 15242554 437 IKQHPFF 443
Cdd:cd14188 249 IIRHDFF 255
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
114-445 6.50e-21

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: 92.37  E-value: 6.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd14183   8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMI--QNEVSILRRVKHPNIVLLIEEMDMPTELYLVMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRE--DGhimlsdfdlslqsfvsptli 271
Cdd:cd14183  86 VKGGDL--FDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqDG-------------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSDSLPMLIAEPTaarsMSFVGTHEYL 351
Cdd:cd14183 144 -----------------------------------------------SKSLKLGDFGLATVVDGPL----YTVCGTPTYV 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG-NRETLFN--VVGQpLKFPE---GSISFAAKDLIRGLLTKDPK 425
Cdd:cd14183 173 APEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGdDQEVLFDqiLMGQ-VDFPSpywDNVSDSAKELITMMLQVDVD 251
                       330       340
                ....*....|....*....|
gi 15242554 426 KRLgfkkGATEIKQHPFFNN 445
Cdd:cd14183 252 QRY----SALQVLEHPWVND 267
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
107-456 8.50e-21

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: 92.40  E-value: 8.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKlgCgdigsVYLAELREmgcfFAMKVMDKGMligrkklvRAQTErEILGLL---DHPFLPTLYSHFET 183
Cdd:cd14175   7 ETIGVGSYSVCKR--C-----VHKATNME----YAVKVIDKSK--------RDPSE-EIEILLrygQHPNIITLKDVYDD 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 184 EKFSCLLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VREDGH---IMLSD 257
Cdd:cd14175  67 GKHVYLVTELMRGGELldKILRQK----FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSLQSFVSPTLIQStsqpschiasyciqpPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaept 337
Cdd:cd14175 143 FGFAKQLRAENGLLMT---------------PCY---------------------------------------------- 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsfvgTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFkGNGNRET----LFNVVGQPLKFPEG---SISF 410
Cdd:cd14175 162 ---------TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF-ANGPSDTpeeiLTRIGSGKFTLSGGnwnTVSD 231
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 411 AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPffnnvnWALIRSTTP 456
Cdd:cd14175 232 AAKDLVSKMLHVDPHQRL----TAKQVLQHP------WITQKDKLP 267
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
141-432 8.86e-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: 91.80  E-value: 8.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 141 AMKVMDKGMlIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL--HILRQKQpgkhFSELAA 216
Cdd:cd14070  31 AIKVIDKKK-AKKDSYVTKNLRREgrIQQMIRHPNITQLLDILETENSYYLVMELCPGGNLmhRIYDKKR----LEEREA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 217 RFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSPTLiqstSQPschIASYCiqppcidpsck 296
Cdd:cd14070 106 RRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLS-NCAGILGY----SDP---FSTQC----------- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 297 lpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYE 376
Cdd:cd14070 167 -------------------------------------------------GSPAYAAPELLARKKYGPKVDVWSIGVNMYA 197
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 377 LLTGKTPFKGNG-NRETLFN--VVGQPLKFPeGSISFAAKDLIRGLLTKDPKKRLGFKK 432
Cdd:cd14070 198 MLTGTLPFTVEPfSLRALHQkmVDKEMNPLP-TDLSPGAISFLRSLLEPDPLKRPNIKQ 255
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
118-443 9.19e-21

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: 91.60  E-value: 9.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMdKGMLIGRKKLVRaqTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd14191   8 ERLGSGKFGQVFRLVEKKTKKVWAGKFF-KAYSAKEKENIR--QEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DLhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VREDG-HIMLSDFDLSlqsfvsptliqsts 275
Cdd:cd14191  85 EL-FERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLA-------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSdsLPMLIaeptaarsmsfvGTHEYLAPEI 355
Cdd:cd14191 150 -------------------------------------------RRLENAGS--LKVLF------------GTPEFVAPEV 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS---ISFAAKDLIRGLLTKDPKKRLgfkk 432
Cdd:cd14191 173 INYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAfdeISDDAKDFISNLLKKDMKARL---- 248
                       330
                ....*....|.
gi 15242554 433 GATEIKQHPFF 443
Cdd:cd14191 249 TCTQCLQHPWL 259
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
149-427 1.21e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 94.70  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  149 MLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHI-----LRQKQPGKHFsELAARFYasEV 223
Cdd:PTZ00267 102 MLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKqikqrLKEHLPFQEY-EVGLLFY--QI 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  224 LLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSfvsptliqstsqpschiasyciqppcidpscklpvaciq 303
Cdd:PTZ00267 179 VLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQY--------------------------------------- 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  304 pscfkprflnnkprkaktekagSDSLPMLIAEptaarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTP 383
Cdd:PTZ00267 220 ----------------------SDSVSLDVAS-------SFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRP 270
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15242554  384 FKGNGNRETLFNVV-GQPLKFPEGsISFAAKDLIRGLLTKDPKKR 427
Cdd:PTZ00267 271 FKGPSQREIMQQVLyGKYDPFPCP-VSSGMKALLDPLLSKNPALR 314
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
112-442 1.61e-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: 91.39  E-value: 1.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYL-----AELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKF 186
Cdd:cd14076   1 GPYILGRTLGEGEFGKVKLgwplpKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQS 264
Cdd:cd14076  81 IGIVLEFVSGGELfdYILARR----RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 FVSPTLIQSTSQPSchiasyciqpPCidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsf 344
Cdd:cd14076 157 DHFNGDLMSTSCGS----------PC------------------------------------------------------ 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 vgtheYLAPEIIRGDG--HGSSVDWWTFGIFLYELLTGKTPFKGN------GNRETLFN-VVGQPLKFPEgSISFAAKDL 415
Cdd:cd14076 173 -----YAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFDDDphnpngDNVPRLYRyICNTPLIFPE-YVTPKARDL 246
                       330       340
                ....*....|....*....|....*..
gi 15242554 416 IRGLLTKDPKKRLGFkkgaTEIKQHPF 442
Cdd:cd14076 247 LRRILVPNPRKRIRL----SAIMRHAW 269
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
104-427 2.61e-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: 90.42  E-value: 2.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 104 SKNEDLGLGHFRLLKKlgCGDIGSVYLAelremgcffAMKVMDKgmligrKKLVRAQTERE--ILGLLDHPFLPTLYSHF 181
Cdd:cd14113  10 SEVAELGRGRFSVVKK--CDQRGTKRAV---------ATKFVNK------KLMKRDQVTHElgVLQSLQHPQLVGLLDTF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ETEKFSCLLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRedghimlsdfd 259
Cdd:cd14113  73 ETPTSYILVLEMADQGRLldYVVRWG----NLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVD----------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 lslqsfvsptliQSTSQPSCHIASY--CIQppcidpscklpvaciqpscfkprfLNNKPRKAKtekagsdslpmliaept 337
Cdd:cd14113 138 ------------QSLSKPTIKLADFgdAVQ------------------------LNTTYYIHQ----------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG---SISFAAKD 414
Cdd:cd14113 165 ------LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDyfkGVSQKAKD 238
                       330
                ....*....|...
gi 15242554 415 LIRGLLTKDPKKR 427
Cdd:cd14113 239 FVCFLLQMDPAKR 251
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
113-427 2.91e-20

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: 90.14  E-value: 2.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKvMDKGMLIGRKKLVRAQTEREILGLL-DHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVK-KSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDL--HILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspt 269
Cdd:cd13997  80 ELCENGSLqdALEELSPISK-LSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA-------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSDSlpmliaeptaarsmsfVGTHE 349
Cdd:cd13997 151 -------------------------------------------------TRLETSGDVE----------------EGDSR 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGD-GHGSSVDWWTFGIFLYELLTG-KTPFKGNGNRETLfnvVGQPLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd13997 166 YLAPELLNENyTHLPKADIFSLGVTVYEAATGePLPRNGQQWQQLR---QGKLPLPPGLVLSQELTRLLKVMLDPDPTRR 242
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-443 3.15e-20

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: 90.02  E-value: 3.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVrAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEA-SKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIM-LSDFDLSlqsfvsptliq 272
Cdd:cd08225  81 CDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGIA----------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLA 352
Cdd:cd08225 150 -------------------------------------RQLNDSMELAYT----------------------CVGTPYYLS 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRlgfkK 432
Cdd:cd08225 171 PEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKVSPRDR----P 246
                       330
                ....*....|.
gi 15242554 433 GATEIKQHPFF 443
Cdd:cd08225 247 SITSILKRPFL 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
118-443 3.90e-20

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: 89.99  E-value: 3.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd14189   7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliqstsq 276
Cdd:cd14189  87 SLaHIWKARHT---LLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAAR------------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYLAPEII 356
Cdd:cd14189 151 ---------------------------------------------------------LEPPEQRKKTICGTPNYLAPEVL 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETlFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRLGFKkgatE 436
Cdd:cd14189 174 LRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKET-YRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLD----Q 248

                ....*..
gi 15242554 437 IKQHPFF 443
Cdd:cd14189 249 ILEHEFF 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
114-427 5.87e-20

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: 89.25  E-value: 5.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMK------VMDKGmliGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFS 187
Cdd:cd08224   2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKkvqifeMMDAK---ARQDCLK---EIDLLQQLNHPNIIKYLASFIENNEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDL-----HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSl 262
Cdd:cd08224  76 NIVLELADAGDLsrlikHFKKQKRL---IPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLG- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 263 qsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPrkaktekagsdslpmliaepTAARSM 342
Cdd:cd08224 152 -----------------------------------------------RFFSSKT--------------------TAAHSL 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 343 sfVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG-NRETLFNVVGQ----PLkfPEGSISFAAKDLIR 417
Cdd:cd08224 165 --VGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKmNLYSLCKKIEKceypPL--PADLYSQELRDLVA 240
                       330
                ....*....|
gi 15242554 418 GLLTKDPKKR 427
Cdd:cd08224 241 ACIQPDPEKR 250
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
151-442 5.90e-20

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: 89.35  E-value: 5.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 151 IGRKKLVRAQT----EREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLA 226
Cdd:cd14120  27 ITKKNLSKSQNllgkEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLADYLQAK--GTLSEDTIRVFLQQIAAA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 227 LEYLHMMGVVYRDLKPENVMVredghimlsdfdlslqsfvsptliqstsqpsCHiasyciqppciDPSCKLPVACIQpsc 306
Cdd:cd14120 105 MKALHSKGIVHRDLKPQNILL-------------------------------SH-----------NSGRKPSPNDIR--- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 307 FK------PRFLNNKPRKAKTekAGSdslPMliaeptaarsmsfvgtheYLAPEIIRGDGHGSSVDWWTFGIFLYELLTG 380
Cdd:cd14120 140 LKiadfgfARFLQDGMMAATL--CGS---PM------------------YMAPEVIMSLQYDAKADLWSIGTIVYQCLTG 196
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 381 KTPFKGNGNRE-TLF---NVVGQPlKFPEGSiSFAAKDLIRGLLTKDPKKRLGFkkgaTEIKQHPF 442
Cdd:cd14120 197 KAPFQAQTPQElKAFyekNANLRP-NIPSGT-SPALKDLLLGLLKRNPKDRIDF----EDFFSHPF 256
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
107-445 6.79e-20

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: 90.85  E-value: 6.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKlgCGDIGSvylaelremGCFFAMKVMDKGMligrkklvRAQTErEILGLL---DHPFLPTLYSHFET 183
Cdd:cd14176  25 EDIGVGSYSVCKR--CIHKAT---------NMEFAVKIIDKSK--------RDPTE-EIEILLrygQHPNIITLKDVYDD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 184 EKFSCLLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VREDGH---IMLSD 257
Cdd:cd14176  85 GKYVYVVTELMKGGELldKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSLQSFVSPTLIQStsqpschiasyciqpPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaept 337
Cdd:cd14176 161 FGFAKQLRAENGLLMT---------------PCY---------------------------------------------- 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsfvgTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFkGNGNRET----LFNVVGQPLKFPEG---SISF 410
Cdd:cd14176 180 ---------TANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTpeeiLARIGSGKFSLSGGywnSVSD 249
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15242554 411 AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFNN 445
Cdd:cd14176 250 TAKDLVSKMLHVDPHQRL----TAALVLRHPWIVH 280
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
114-428 6.95e-20

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: 89.46  E-value: 6.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTL---YSHFETEKFSCLL 190
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLN--LDTDDDDVSDIQKEVALLSQLKLGQPKNIikyYGSYLKGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfVSPTL 270
Cdd:cd06917  81 MDYCEGGSIRTLMRAGP---IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFG------VAASL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 IQSTSQPSchiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmSFVGTHEY 350
Cdd:cd06917 152 NQNSSKRS----------------------------------------------------------------TFVGTPYW 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIR-GDGHGSSVDWWTFGIFLYELLTGKTPFKGngnrETLFNVV-----GQPLKFPEGSISFAAKDLIRGLLTKDP 424
Cdd:cd06917 168 MAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSD----VDALRAVmlipkSKPPRLEGNGYSPLLKEFVAACLDEEP 243

                ....
gi 15242554 425 KKRL 428
Cdd:cd06917 244 KDRL 247
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
120-404 7.80e-20

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


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 88.32  E-value: 7.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLaelremGCFfamkvmdKGMLIGRKKlVRAQTEREILGL--LDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd14059   1 LGSGAQGAVFL------GKF-------RGEEVAVKK-VRDEKETDIKHLrkLNHPNIIKFKGVCTQAPCYCILMEYCPYG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsq 276
Cdd:cd14059  67 QLYeVLRAGRE---ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTS--------------- 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKaktekagsdslpmliaeptaarsMSFVGTHEYLAPEII 356
Cdd:cd14059 129 ---------------------------------KELSEKSTK-----------------------MSFAGTVAWMAPEVI 152
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFP 404
Cdd:cd14059 153 RNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLP 200
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
114-447 1.38e-19

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: 88.94  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06644  14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLH-ILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd06644  91 CPGGAVDaIMLELDRG--LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVS----------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKagsdslpmliaepTAARSMSFVGTHEYLA 352
Cdd:cd06644 158 ----------------------------------------------AKNVK-------------TLQRRDSFIGTPYWMA 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEII-----RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV-------VGQPLKFpegSISFaaKDLIRGLL 420
Cdd:cd06644 179 PEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIaksepptLSQPSKW---SMEF--RDFLKTAL 253
                       330       340
                ....*....|....*....|....*..
gi 15242554 421 TKDPKKRlgfkKGATEIKQHPFFNNVN 447
Cdd:cd06644 254 DKHPETR----PSAAQLLEHPFVSSVT 276
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
120-440 1.41e-19

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: 88.48  E-value: 1.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMD-KGMligrKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGD 198
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKvKGA----KEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 199 LhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM-VREDGH-IMLSDFDLSLQsfvsptliqstsq 276
Cdd:cd14192  88 L-FDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARR------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciqpscFKPRflnnkpRKAKTEkagsdslpmliaeptaarsmsfVGTHEYLAPEII 356
Cdd:cd14192 154 ------------------------------YKPR------EKLKVN----------------------FGTPEFLAPEVV 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS---ISFAAKDLIRGLLTKDPKKRLgfkkG 433
Cdd:cd14192 176 NYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAfenLSEEAKDFISRLLVKEKSCRM----S 251

                ....*..
gi 15242554 434 ATEIKQH 440
Cdd:cd14192 252 ATQCLKH 258
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-427 1.71e-19

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: 88.33  E-value: 1.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMG-CFFAMKVMDKGMLI-GRKKLVRAQTEREILG-------LLDHPFLPTLYSHFETE 184
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEINMTNPAfGRTEQERDKSVGDIISevniikeQLRHPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDL--HILRQKQPGKHFSElaARFYA--SEVLLALEYLHM-MGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd08528  82 DRLYIVMELIEGAPLgeHFSSLKEKNEHFTE--DRIWNifVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 260 LSLQSfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSLPMliaeptaa 339
Cdd:cd08528 160 LAKQK------------------------------------------------------------GPESSKM-------- 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 340 rsMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFN--VVGQPLKFPEGSISFAAKDLIR 417
Cdd:cd08528 172 --TSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYST-NMLTLATkiVEAEYEPLPEGMYSDDITFVIR 248
                       330
                ....*....|
gi 15242554 418 GLLTKDPKKR 427
Cdd:cd08528 249 SCLTPDPEAR 258
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
120-443 2.08e-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: 87.91  E-value: 2.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKgmligrKKLVRAQTER------EILGLLDHPFLPTLYSHFET-EKFSCLLME 192
Cdd:cd14165   9 LGEGSYAKVKSAYSERLKCNVAIKIIDK------KKAPDDFVEKflprelEILARLNHKSIIKTYEIFETsDGKVYIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd14165  83 LGVQGDL--LEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFS----------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGSDSLpmliaeptaarSMSFVGTHEYLA 352
Cdd:cd14165 150 --------------------------------------------KRCLRDENGRIVL-----------SKTFCGSAAYAA 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSV-DWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG-SISFAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd14165 175 PEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSkNLTSECKDLIYRLLQPDVSQRLCI 254
                       330
                ....*....|...
gi 15242554 431 kkgaTEIKQHPFF 443
Cdd:cd14165 255 ----DEVLSHPWL 263
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
120-442 2.77e-19

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: 88.16  E-value: 2.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVR-------AQTEREILGLLDHpflptlyshFETEKFSCLLME 192
Cdd:cd14174  10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFRevetlyqCQGNKNILELIEF---------FEDDTRFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDlhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHI---MLSDFDLSlqsfvspt 269
Cdd:cd14174  81 KLRGGS--ILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVspvKICDFDLG-------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidPSCKLPVACIqpscfkprflnnkprkaktekagsdslPMLIAEPTAArsmsfVGTHE 349
Cdd:cd14174 151 -----------------------SGVKLNSACT---------------------------PITTPELTTP-----CGSAE 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEII-----RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGN--------------RETLFNVVGQ-PLKFPEGS-- 407
Cdd:cd14174 176 YMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGtdcgwdrgevcrvcQNKLFESIQEgKYEFPDKDws 255
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15242554 408 -ISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14174 256 hISSEAKDLISKLLVRDAKERL----SAAQVLQHPW 287
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
118-443 2.85e-19

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: 87.68  E-value: 2.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKgmligRKKLVRAQTE--REILGL---LDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14197  15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRK-----RRKGQDCRMEiiHEIAVLelaQANPWVINLHEVYETASEMILVLE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRED---GHIMLSDFDLSlqsfvspt 269
Cdd:cd14197  90 YAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLS-------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNkprkaktekagSDSLpmliaeptaarsMSFVGTHE 349
Cdd:cd14197 162 ----------------------------------------RILKN-----------SEEL------------REIMGTPE 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS---ISFAAKDLIRGLLTKDPKK 426
Cdd:cd14197 179 YVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEfehLSESAIDFIKTLLIKKPEN 258
                       330
                ....*....|....*..
gi 15242554 427 RlgfkKGATEIKQHPFF 443
Cdd:cd14197 259 R----ATAEDCLKHPWL 271
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
113-443 2.90e-19

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 88.89  E-value: 2.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGM--LIGRK------KLVRAQTEREILGLLDhPFLPTlySHFETE 184
Cdd:cd07851  16 RYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFqsAIHAKrtyrelRLLKHMKHENVIGLLD-VFTPA--SSLEDF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFcSGGDLH-ILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlq 263
Cdd:cd07851  93 QDVYLVTHL-MGADLNnIVKCQK----LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLA-- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 sfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGsdslpmliaeptaarsms 343
Cdd:cd07851 166 -----------------------------------------------------RHTDDEMTG------------------ 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 FVGTHEYLAPEIIRGDGHGS-SVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP-LKFPEGSISFAAKDLIRG 418
Cdd:cd07851 175 YVATRWYRAPEIMLNWMHYNqTVDIWSVGCIMAELLTGKTLFPGSDHIDQLkriMNLVGTPdEELLKKISSESARNYIQS 254
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 419 L--------------------------LTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07851 255 LpqmpkkdfkevfsganplaidllekmLVLDPDKRI----TAAEALAHPYL 301
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
114-443 4.30e-19

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: 86.67  E-value: 4.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGML-----IGRKKLVRAQTEREILGLLD---HPFLPTLYSHFETEK 185
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvdtwVRDRKLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLME-FCSGGDLHILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqs 264
Cdd:cd14004  82 FYYLVMEkHGSGMDLFDFIERKPN--MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG----- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvSPTLIqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnKPRKAKTekagsdslpmliaeptaarsmsF 344
Cdd:cd14004 155 --SAAYI-------------------------------------------KSGPFDT----------------------F 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKgngnreTLFNVVGQPLKFPEgSISFAAKDLIRGLLTKD 423
Cdd:cd14004 168 VGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFY------NIEEILEADLRIPY-AVSEDLIDLISRMLNRD 240
                       330       340
                ....*....|....*....|
gi 15242554 424 PKKRLgfkkGATEIKQHPFF 443
Cdd:cd14004 241 VGDRP----TIEELLTDPWL 256
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
113-447 4.50e-19

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: 87.39  E-value: 4.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd06643   6 FWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGG--DLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptl 270
Cdd:cd06643  83 FCAGGavDAVMLELERP---LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVS--------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKagsdslpmliaepTAARSMSFVGTHEY 350
Cdd:cd06643 151 ------------------------------------------------AKNTR-------------TLQRRDSFIGTPYW 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEII-----RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV-------VGQPLKFpegSISFaaKDLIRG 418
Cdd:cd06643 170 MAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIaksepptLAQPSRW---SPEF--KDFLRK 244
                       330       340
                ....*....|....*....|....*....
gi 15242554 419 LLTKDPKKRLgfkkGATEIKQHPFFNNVN 447
Cdd:cd06643 245 CLEKNVDARW----TTSQLLQHPFVSVLV 269
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
117-442 6.00e-19

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: 87.09  E-value: 6.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKV---MDKGMLigRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCL--LM 191
Cdd:cd06621   6 LSSLGEGAGGSVTKCRLRNTKTIFALKTittDPNPDV--QKQILR---ELEINKSCASPYIVKYYGAFLDEQDSSIgiAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHIL--RQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfVSPT 269
Cdd:cd06621  81 EYCEGGSLDSIykKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFG------VSGE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 LIQSTsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarSMSFVGTHE 349
Cdd:cd06621 155 LVNSL------------------------------------------------------------------AGTFTGTSY 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNR-----ETLFNVVGQP---LK-FPEGSI--SFAAKDLIRG 418
Cdd:cd06621 169 YMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVNMPnpeLKdEPENGIkwSESFKDFIEK 248
                       330       340
                ....*....|....*....|....
gi 15242554 419 LLTKDPKKRlgfkKGATEIKQHPF 442
Cdd:cd06621 249 CLEKDGTRR----PGPWQMLAHPW 268
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
118-427 7.46e-19

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: 86.51  E-value: 7.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligRKKLVRAQTEREILGL---LDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRR---RGQDCRAEILHEIAVLelaKSNPRVVNLHEVYETTSEIILILEYA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRED---GHIMLSDFDLSLQsfvsptli 271
Cdd:cd14198  91 AGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK-------- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcIDPSCKLpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYL 351
Cdd:cd14198 163 -------------------IGHACEL--------------------------------------------REIMGTPEYL 179
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14198 180 APEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfSSVSQLATDFIQKLLVKNPEKR 258
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
159-443 8.47e-19

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: 85.94  E-value: 8.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 159 AQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLH--ILRQKqpGKHFSELAARFYASEVLLALEYLHMMGVV 236
Cdd:cd08221  46 ALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHdkIAQQK--NQLFPEEVVLWYLYQIVSAVSHIHKAGIL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 237 YRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKP 316
Cdd:cd08221 124 HRDIKTLNIFLTKADLVKLGDFGIS------------------------------------------------KVLDSES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 317 RKAKtekagsdslpmliaeptaarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV 396
Cdd:cd08221 156 SMAE----------------------SIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKI 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15242554 397 VGQPLKFPEGSISFAAKDLIRGLLTKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd08221 214 VQGEYEDIDEQYSEEIIQLVHDCLHQDPEDR----PTAEELLERPLL 256
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
111-443 8.48e-19

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: 85.96  E-value: 8.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFrllKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmligrkklVRAQTERE-------ILGLLDHPFLPTLYSHFET 183
Cdd:cd06648   9 LDNF---VKIGEGSTGIVCIATDKSTGRQVAVKKMD----------LRKQQRREllfnevvIMRDYQHPNIVEMYSSYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 184 EKFSCLLMEFCSGGDL-HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlsl 262
Cdd:cd06648  76 GDELWVVMEFLEGGALtDIVTHTR----MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDF---- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 263 qsfvsptliqstsqpschiaSYCIQPpcidpscklpvaciqpscfkprflnnkprkaktekagSDSLPmliaeptaaRSM 342
Cdd:cd06648 148 --------------------GFCAQV-------------------------------------SKEVP---------RRK 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 343 SFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFkgngnretlFNVvgQPLK--------FPEGS-----IS 409
Cdd:cd06648 162 SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPY---------FNE--PPLQamkrirdnEPPKLknlhkVS 230
                       330       340       350
                ....*....|....*....|....*....|....
gi 15242554 410 FAAKDLIRGLLTKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd06648 231 PRLRSFLDRMLVRDPAQR----ATAAELLNHPFL 260
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
114-427 1.64e-18

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: 85.25  E-value: 1.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLiGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKM-SPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqs 273
Cdd:cd08218  81 CDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIA------------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLAP 353
Cdd:cd08218 149 ------------------------------------RVLNSTVELART----------------------CIGTPYYLSP 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGnGNRETLFnvvgqpLKFPEGSI-------SFAAKDLIRGLLTKDPKK 426
Cdd:cd08218 171 EICENKPYNNKSDIWALGCVLYEMCTLKHAFEA-GNMKNLV------LKIIRGSYppvpsrySYDLRSLVSQLFKRNPRD 243

                .
gi 15242554 427 R 427
Cdd:cd08218 244 R 244
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
151-444 2.78e-18

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 84.68  E-value: 2.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 151 IGRKKLVRAQT----EREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL----HILRQkqpgkhFSELAARFYASE 222
Cdd:cd14202  36 INKKNLAKSQTllgkEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLadylHTMRT------LSEDTIRLFLQQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 223 VLLALEYLHMMGVVYRDLKPENVMvredghimlsdfdlslqsfvsptLIQSTSQPSchiasyciQPPCIdpscklpvaCI 302
Cdd:cd14202 110 IAGAMKMLHSKGIIHRDLKPQNIL-----------------------LSYSGGRKS--------NPNNI---------RI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 303 QPSCFK-PRFLNNKprkaktekagsdslpMLIAeptaarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGK 381
Cdd:cd14202 150 KIADFGfARYLQNN---------------MMAA--------TLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGK 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 382 TPFKGNGNRE-TLFNVVGQPL--KFPEGSiSFAAKDLIRGLLTKDPKKRLGFKkgatEIKQHPFFN 444
Cdd:cd14202 207 APFQASSPQDlRLFYEKNKSLspNIPRET-SSHLRQLLLGLLQRNQKDRMDFD----EFFHHPFLD 267
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
114-442 2.99e-18

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: 84.44  E-value: 2.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGrkklvrAQTEREILG--LLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKID------ENVQREIINhrSLRHPNIIRFKEVVLTPTHLAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLhILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVreDG----HIMLSDFDLSlqsfvs 267
Cdd:cd14662  76 EYAAGGEL-FERICNAGR-FSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL--DGspapRLKICDFGYS------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsqpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRkaktekagsdslpmliaeptaarsmSFVGT 347
Cdd:cd14662 146 ----------------------------------------KSSVLHSQPK-------------------------STVGT 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 HEYLAPEII-RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGN----RETLFNVVGQPLKFPEG-SISFAAKDLIRGLLT 421
Cdd:cd14662 161 PAYIAPEVLsRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfRKTIQRIMSVQYKIPDYvRVSQDCRHLLSRIFV 240
                       330       340
                ....*....|....*....|.
gi 15242554 422 KDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14662 241 ANPAKRITIP----EIKNHPW 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
112-442 3.11e-18

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: 84.66  E-value: 3.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmLIGRKKlVRAQTEREIL-GLLDHPFLPTLYSHFETEKFSC-- 188
Cdd:cd06608   6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD---IIEDEE-EEIKLEINILrKFSNHPNIATFYGAFIKKDPPGgd 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 ----LLMEFCSGG---DLhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd06608  82 dqlwLVMEYCGGGsvtDL-VKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 LQsfvsptlIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaaRS 341
Cdd:cd06608 161 AQ-------LDSTLG---------------------------------------------------------------RR 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 MSFVGTHEYLAPEIIRGD-----GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEG-SISFaa 412
Cdd:cd06608 171 NTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPpptLKSPEKwSKEF-- 248
                       330       340       350
                ....*....|....*....|....*....|
gi 15242554 413 KDLIRGLLTKDPKKRlgfkKGATEIKQHPF 442
Cdd:cd06608 249 NDFISECLIKNYEQR----PFTEELLEHPF 274
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
113-444 3.27e-18

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: 85.65  E-value: 3.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAelremgcffamkvMDK--GMLIGRKKLVRA--------QTEREI--LGLLDHP-------- 172
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSA-------------YDKrtGRKVAIKKISNVfddlidakRILREIkiLRHLKHEniiglldi 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 173 FLPTLYSHFE-----TEkfsclLMEfcsgGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM 246
Cdd:cd07834  68 LRPPSPEEFNdvyivTE-----LME----TDLHkVIKSPQP---LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNIL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 247 VREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRK-AKTEkag 325
Cdd:cd07834 136 VNSNCDLKICDFGLA------------------------------------------------RGVDPDEDKgFLTE--- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 326 sdslpmliaeptaarsmsFVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP- 400
Cdd:cd07834 165 ------------------YVVTRWYRAPELLLSSKKyTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLnliVEVLGTPs 226
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 401 ---LKFPEGS--------------ISFA---------AKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFN 444
Cdd:cd07834 227 eedLKFISSEkarnylkslpkkpkKPLSevfpgaspeAIDLLEKMLVFNPKKRI----TADEALAHPYLA 292
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
120-442 4.24e-18

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: 84.03  E-value: 4.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAeLREMGCFFAMK--VMD-KGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd06631   9 LGKGAYGTVYCG-LTSTGQLIAVKqvELDtSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptliqsts 275
Cdd:cd06631  88 GSIaSILARFGA---LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDF----------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpSCKLPVACIQPSCFKPRFLnnkprkaktekagsdslpmliaeptaaRSMSfvGTHEYLAPEI 355
Cdd:cd06631 148 ------------------GCAKRLCINLSSGSQSQLL---------------------------KSMR--GTPYWMAPEV 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV---VGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLgfkk 432
Cdd:cd06631 181 INETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsgRKPVPRLPD-KFSPEARDFVHACLTRDQDERP---- 255
                       330
                ....*....|
gi 15242554 433 GATEIKQHPF 442
Cdd:cd06631 256 SAEQLLKHPF 265
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
140-443 4.39e-18

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: 84.20  E-value: 4.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 140 FAMKVMD--KGMLIGRKKL--VRAQTEREILGLLD---HPFLPTLYSHFETEKFSCLLMEFCSGGDL-HILRQKQPgkhF 211
Cdd:cd14182  31 YAVKIIDitGGGSFSPEEVqeLREATLKEIDILRKvsgHPNIIQLKDTYETNTFFFLVFDLMKKGELfDYLTEKVT---L 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 212 SELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliqstsqpschiasyciqppcI 291
Cdd:cd14182 108 SEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ---------------------------L 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 292 DPSCKLPVACiqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIR------GDGHGSSV 365
Cdd:cd14182 161 DPGEKLREVC--------------------------------------------GTPGYLAPEIIEcsmddnHPGYGKEV 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 366 DWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKF--PE-GSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14182 197 DMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPEwDDRSDTVKDLISRFLVVQPQKRY----TAEEALAHPF 272

                .
gi 15242554 443 F 443
Cdd:cd14182 273 F 273
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
113-427 6.01e-18

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: 83.92  E-value: 6.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREIL-GLLDHPFLPTLYSH----FETEKFS 187
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFN---DEEQLRVAIKEIEIMkRLCGHPNIVQYYDSailsSEGRKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDLHILRqKQPGKHFSELAARFYASEVLLALEYLHMMG--VVYRDLKPENVMVREDGHIMLSDFdlslqSF 265
Cdd:cd13985  78 LLLMEYCPGSLVDILE-KSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDF-----GS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 VSPTLIQSTSQPSCHIASyciqppcidpscklpvaciqpscfkprflnnkprkaktEKAGSDSLPMliaeptaarsmsfv 345
Cdd:cd13985 152 ATTEHYPLERAEEVNIIE--------------------------------------EEIQKNTTPM-------------- 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 gtheYLAPEII---RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPlKFPEGSISFaaKDLIRGLLTK 422
Cdd:cd13985 180 ----YRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKYSIP-EQPRYSPEL--HDLIRHMLTP 252

                ....*
gi 15242554 423 DPKKR 427
Cdd:cd13985 253 DPAER 257
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
142-443 7.08e-18

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: 83.91  E-value: 7.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 142 MKVMDK--GMLIGRKKL--------VRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQPGk 209
Cdd:cd07833  18 LKCRNKatGEIVAIKKFkeseddedVKKTALREVkvLRQLRHENIVNLKEAFRRKGRLYLVFEYVERTLLELLEASPGG- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 210 hFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqpp 289
Cdd:cd07833  97 -LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFA---------------------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 290 cidpscklpvaciqpscfkpRFLNNKPRKAKTEkagsdslpmliaeptaarsmsFVGTHEYLAPEIIRGDG-HGSSVDWW 368
Cdd:cd07833 148 --------------------RALTARPASPLTD---------------------YVATRWYRAPELLVGDTnYGKPVDVW 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 369 TFGIFLYELLTGKTPFKGNGNRETLF---NVVGqPL-----------------KFPE------------GSISFAAKDLI 416
Cdd:cd07833 187 AIGCIMAELLDGEPLFPGDSDIDQLYliqKCLG-PLppshqelfssnprfagvAFPEpsqpeslerrypGKVSSPALDFL 265
                       330       340
                ....*....|....*....|....*..
gi 15242554 417 RGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07833 266 KACLRMDPKERL----TCDELLQHPYF 288
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
114-443 8.06e-18

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: 83.77  E-value: 8.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdkgmligrkKlVRAQTERE-----------ILGLLDHPFLPTLYshfE 182
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALK-----------K-IRMENEKEgfpitaireikLLQKLDHPNVVRLK---E 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 183 --TEKFSC-------LLMEFCSGgDLH-ILRQkqPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH 252
Cdd:cd07840  66 ivTSKGSAkykgsiyMVFEYMDH-DLTgLLDN--PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 253 IMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTEKagsdslpml 332
Cdd:cd07840 143 LKLADFGLA------------------------------------------------RPYTKENNADYTNR--------- 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 333 iaeptaarsmsfVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP-------- 400
Cdd:cd07840 166 ------------VITLWYRPPELLLGATRyGPEVDMWSVGCILAELFTGKPIFQGKTELEQLekiFELCGSPteenwpgv 233
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 401 --------LKFPE-----------GSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07840 234 sdlpwfenLKPKKpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRI----SADQALQHEYF 291
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
120-442 8.96e-18

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: 83.20  E-value: 8.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLI------GRKKLVRA-QTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKTSsdradsRQKTVVDAlKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL-HILRQkqPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptli 271
Cdd:cd06629  89 YVPGGSIgSCLRK--YGK-FEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDF------------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qSTSQPSCHIASyciqppcidpscklpvaciqpscfkprflNNkprkaktekagsdslpmliaeptAARSMSfvGTHEYL 351
Cdd:cd06629 153 -GISKKSDDIYG-----------------------------NN-----------------------GATSMQ--GSVFWM 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEII--RGDGHGSSVDWWTFGIFLYELLTGKTPFkgngNRETLFNV---VGQ-----PLKfPEGSISFAAKDLIRGLLT 421
Cdd:cd06629 178 APEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW----SDDEAIAAmfkLGNkrsapPVP-EDVNLSPEALDFLNACFA 252
                       330       340
                ....*....|....*....|.
gi 15242554 422 KDPKKRlgfkKGATEIKQHPF 442
Cdd:cd06629 253 IDPRDR----PTAAELLSHPF 269
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
114-427 1.07e-17

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: 82.71  E-value: 1.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIR--LPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqs 273
Cdd:cd08219  80 CDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFG-------------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfKPRFLNNkprkaktekagsdslPMliaeptaARSMSFVGTHEYLAP 353
Cdd:cd08219 146 ----------------------------------SARLLTS---------------PG-------AYACTYVGTPYYVPP 169
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd08219 170 EIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNPRSR 243
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
120-384 1.29e-17

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: 83.27  E-value: 1.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHP------FLPTLYSHFETEKFSCLLMEF 193
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPnvvsarDVPPELEKLSPNDLPLLAMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDL-HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIM---LSDF----DLSLQSF 265
Cdd:cd13989  81 CSGGDLrKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRViykLIDLgyakELDQGSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 VSptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmSFV 345
Cdd:cd13989 161 CT---------------------------------------------------------------------------SFV 165
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15242554 346 GTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPF 384
Cdd:cd13989 166 GTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
114-442 1.75e-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: 82.60  E-value: 1.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVY-LAELREMGCFFAMKVMDKGmliGRKKLVRaqTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14104   2 YMIAEELGRGQFGIVHrCVETSSKKTYMAKFVKVKG---ADQVLVK--KEISILNIARHRNILRLHESFESHEELVMIFE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM--VREDGHIMLSDFDLSLQsfvsptl 270
Cdd:cd14104  77 FISGVDI-FERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIycTRRGSYIKIIEFGQSRQ------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVgTHEY 350
Cdd:cd14104 149 ---------------------------------------------------------------LKPGDKFRLQYT-SAEF 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS---ISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14104 165 YAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAfknISIEALDFVDRLLVKERKSR 244
                       330
                ....*....|....*
gi 15242554 428 LgfkkGATEIKQHPF 442
Cdd:cd14104 245 M----TAQEALNHPW 255
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
114-443 3.39e-17

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: 81.94  E-value: 3.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVM-----DKGMLIGrkklvraqTEREIlGLL------DHPFLPTLY---- 178
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVrvplsEEGIPLS--------TIREI-ALLkqlesfEHPNVVRLLdvch 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 179 -SHFETEKFSCLLMEFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSD 257
Cdd:cd07838  72 gPRTDRELKLTLVFEHVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLAD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSlqsfvsptliqstsqpschiASYCIQppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpMLIAept 337
Cdd:cd07838 151 FGLA--------------------RIYSFE-------------------------------------------MALT--- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK------------ 402
Cdd:cd07838 165 -----SVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLgkiFDVIGLPSEeewprnsalprs 239
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242554 403 -FPEGS----------ISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07838 240 sFPSYTprpfksfvpeIDEEGLDLLKKMLTFNPHKRI----SAFEALQHPYF 287
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
109-442 3.88e-17

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: 80.77  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 109 LGLGHFRLLKKlgCgdigsVYLAELREMgcffAMKVMDKGMligrKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd14115   1 IGRGRFSIVKK--C-----LHKATRKDV----AVKFVSKKM----KKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLhiLRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVredghimlsdfdlslqsfvsp 268
Cdd:cd14115  66 LVLELMDDGRL--LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--------------------- 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpSCKLPVACIQPSCFKPrflnnkprkaKTEKAGSDSLPMLIAEPtaarsmsfvgth 348
Cdd:cd14115 123 -------------------------DLRIPVPRVKLIDLED----------AVQISGHRHVHHLLGNP------------ 155
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPK 425
Cdd:cd14115 156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDeyfGDVSQAARDFINVILQEDPR 235
                       330
                ....*....|....*..
gi 15242554 426 KRlgfkKGATEIKQHPF 442
Cdd:cd14115 236 RR----PTAATCLQHPW 248
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
107-466 5.08e-17

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: 81.60  E-value: 5.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKlgcgdigSVYLAELREmgcfFAMKVMDKGmligrkklvRAQTEREILGLL---DHPFLPTLYSHFET 183
Cdd:cd14177  10 EDIGVGSYSVCKR-------CIHRATNME----FAVKIIDKS---------KRDPSEEIEILMrygQHPNIITLKDVYDD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 184 EKFSCLLMEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG----HIMLSD 257
Cdd:cd14177  70 GRYVYLVTELMKGGELldRILRQK----FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSLQSFVSPTLIQStsqpschiasyciqpPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaept 337
Cdd:cd14177 146 FGFAKQLRGENGLLLT---------------PCY---------------------------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsfvgTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGN---RETLFNVVGQPLKFPEG---SISFA 411
Cdd:cd14177 165 ---------TANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNdtpEEILLRIGSGKFSLSGGnwdTVSDA 235
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 412 AKDLIRGLLTKDPKKRLgfkkGATEIKQHpffnnvNWALIRSTTPPEIPKPIDLS 466
Cdd:cd14177 236 AKDLLSHMLHVDPHQRY----TAEQVLKH------SWIACRDQLPHYQLNRQDAP 280
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
114-442 6.80e-17

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: 80.41  E-value: 6.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRkklvraQTEREILG--LLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDE------NVQREIINhrSLRHPNIVRFKEVILTPTHLAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHiLRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENvmvredghimlsdfdlslqsfvspTLI 271
Cdd:cd14665  76 EYAAGGELF-ERICNAGR-FSEDEARFFFQQLISGVSYCHSMQICHRDLKLEN------------------------TLL 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 QSTSQPSCHIASYCIQppcidpscklpvaciqpscfKPRFLNNKPRkaktekagsdslpmliaeptaarsmSFVGTHEYL 351
Cdd:cd14665 130 DGSPAPRLKICDFGYS--------------------KSSVLHSQPK-------------------------STVGTPAYI 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEII-RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGN----RETLFNVVGQPLKFPEG-SISFAAKDLIRGLLTKDPK 425
Cdd:cd14665 165 APEVLlKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfRKTIQRILSVQYSIPDYvHISPECRHLISRIFVADPA 244
                       330
                ....*....|....*..
gi 15242554 426 KRLGFKkgatEIKQHPF 442
Cdd:cd14665 245 TRITIP----EIRNHEW 257
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
158-442 7.87e-17

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: 80.83  E-value: 7.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 158 RAQTEREILGLLDHPFLPTLYSHFETEKFS-CLLMEFCSGGDLH-ILRQKqpgKHFSELAARFYASEVLLALEYL--HMM 233
Cdd:cd13990  50 HALREYEIHKSLDHPRIVKLYDVFEIDTDSfCTVLEYCDGNDLDfYLKQH---KSIPEREARSIIMQVVSALKYLneIKP 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 234 GVVYRDLKPENVMVRED---GHIMLSDFDLSLQ----SFVSPTlIQSTSQpschiasyciqppcidpscklpvaciqpsc 306
Cdd:cd13990 127 PIIHYDLKPGNILLHSGnvsGEIKITDFGLSKImddeSYNSDG-MELTSQ------------------------------ 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 307 fkprflnnkprkaktekagsdslpmliaeptaarsmsFVGTHEYLAPEI-IRGDGH---GSSVDWWTFGIFLYELLTGKT 382
Cdd:cd13990 176 -------------------------------------GAGTYWYLPPECfVVGKTPpkiSSKVDVWSVGVIFYQMLYGRK 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 383 PFKGNGNRET-LFNvvGQPLK-----FP-EGSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd13990 219 PFGHNQSQEAiLEE--NTILKateveFPsKPVVSSEAKDFIRRCLTYRKEDRP----DVLQLANDPY 279
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
118-441 8.35e-17

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: 80.41  E-value: 8.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVM---DKGmligRKKL---VRAQTEREILGLLDhpflptLYSHFETEKfSCLL- 190
Cdd:cd14089   7 QVLGLGINGKVLECFHKKTGEKFALKVLrdnPKA----RREVelhWRASGCPHIVRIID------VYENTYQGR-KCLLv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 -MEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRE---DGHIMLSDFdlslqSFV 266
Cdd:cd14089  76 vMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDF-----GFA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 SPTliqstsqpschIASYCIQPPCIDPScklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvg 346
Cdd:cd14089 151 KET-----------TTKKSLQTPCYTPY---------------------------------------------------- 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 theYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN-------GNRETLFNvvGQpLKFPE---GSISFAAKDLI 416
Cdd:cd14089 168 ---YVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaispGMKKRIRN--GQ-YEFPNpewSNVSEEAKDLI 241
                       330       340
                ....*....|....*....|....*
gi 15242554 417 RGLLTKDPKKRLGFkkgaTEIKQHP 441
Cdd:cd14089 242 RGLLKTDPSERLTI----EEVMNHP 262
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
191-442 1.12e-16

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: 80.14  E-value: 1.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL-HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRE-DGHIMLSDFdlslqsfvsp 268
Cdd:cd06624  84 MEQVPGGSLsALLRSKWGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDF---------- 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqSTSQPschiasyciqppcidpscklpVACIQPSCfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTH 348
Cdd:cd06624 154 ----GTSKR---------------------LAGINPCT-----------------------------------ETFTGTL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEII-RGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPE--GSISFAAKDLIRGLLTKDP 424
Cdd:cd06624 174 QYMAPEVIdKGQrGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMFKIHPEipESLSEEAKSFILRCFEPDP 253
                       250
                ....*....|....*...
gi 15242554 425 KKRlgfkKGATEIKQHPF 442
Cdd:cd06624 254 DKR----ATASDLLQDPF 267
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
117-442 1.14e-16

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: 79.95  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAeLREMGCFFAMKVMDkgmLIGR------------KKLVRAQTEREILGLLDhpflptlYSHFETE 184
Cdd:cd14131   6 LKQLGKGGSSKVYKV-LNPKKKIYALKRVD---LEGAdeqtlqsykneiELLKKLKGSDRIIQLYD-------YEVTDED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEfCSGGDL-HILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPEN-VMVreDGHIMLSDFDLSL 262
Cdd:cd14131  75 DYLYMVME-CGEIDLaTILKKKRPKP-IDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLV--KGRLKLIDFGIAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 263 QSFVSPTLIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsm 342
Cdd:cd14131 151 AIQNDTTSIVRDSQ------------------------------------------------------------------ 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 343 sfVGTHEYLAPE---IIRGDGHGSSV-------DWWTFGIFLYELLTGKTPFKG------------NGNRETLFNVVGQP 400
Cdd:cd14131 165 --VGTLNYMSPEaikDTSASGEGKPKskigrpsDVWSLGCILYQMVYGKTPFQHitnpiaklqaiiDPNHEIEFPDIPNP 242
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242554 401 lkfpegsisfAAKDLIRGLLTKDPKKRLGFkkgaTEIKQHPF 442
Cdd:cd14131 243 ----------DLIDVMKRCLQRDPKKRPSI----PELLNHPF 270
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
114-443 1.20e-16

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: 79.62  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmLIGRKKLVR-AQTEREILGLL------DHPFLPTLYSHFETEKF 186
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKI-----IKNNKDYLDqSLDEIRLLELLnkkdkaDKYHIVRLKDVFYFKNH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGGDLHILRQ-KQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENvmvredghIMLSDFDlslqsf 265
Cdd:cd14133  76 LCIVFELLSQNLYEFLKQnKFQY--LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPEN--------ILLASYS------ 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vsptliqstsqpschiasyciqppcidpSCKLPVACIQPSCFKPRFLNnkprkaktekagsdslpmliaeptaarsmSFV 345
Cdd:cd14133 140 ----------------------------RCQIKIIDFGSSCFLTQRLY-----------------------------SYI 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAA------KDLIRGL 419
Cdd:cd14133 163 QSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKaddelfVDFLKKL 242
                       330       340
                ....*....|....*....|....
gi 15242554 420 LTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd14133 243 LEIDPKERP----TASQALSHPWL 262
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
118-431 1.34e-16

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: 79.51  E-value: 1.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFF---AMKVMDKGMLIG-RKKLVRaqtEREILGLLDHPFLPTLYsHFETEKFS-CLLME 192
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDGKTvdvAVKTLKEDASESeRKDFLK---EARVMKKLGHPNVVRLL-GVCTEEEPlYLVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDL-HILRQKQPGKHF--------SELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQ 263
Cdd:cd00192  77 YMEGGDLlDFLRKSRPVFPSpepstlslKDLLS--FAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 SFVSPTLIQSTsqpschiasyciqppcidpSCKLPVAciqpscfkprflnnkprkaktekagsdslpmliaeptaarsms 343
Cdd:cd00192 155 IYDDDYYRKKT-------------------GGKLPIR------------------------------------------- 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 fvgtheYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLKFPEGsISFAAKDLIRGLLT 421
Cdd:cd00192 173 ------WMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRkGYRLPKPEN-CPDELYELMLSCWQ 245
                       330
                ....*....|
gi 15242554 422 KDPKKRLGFK 431
Cdd:cd00192 246 LDPEDRPTFS 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
152-428 2.24e-16

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: 78.91  E-value: 2.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 152 GRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLH--ILRQKqpgkHFSELAARFYASEVLLALEY 229
Cdd:cd14088  39 GRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFdwILDQG----YYSERDTSNVIRQVLEAVAY 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 230 LHMMGVVYRDLKPENVMV---REDGHIMLSDFDLslqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpsc 306
Cdd:cd14088 115 LHSLKIVHRNLKLENLVYynrLKNSKIVISDFHL---------------------------------------------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 307 fkprflnnkprkAKTEKAgsdslpmLIAEPtaarsmsfVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG 386
Cdd:cd14088 149 ------------AKLENG-------LIKEP--------CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYD 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15242554 387 --------NGNRETLFNVVGQPLKFPE---GSISFAAKDLIRGLLTKDPKKRL 428
Cdd:cd14088 202 eaeeddyeNHDKNLFRKILAGDYEFDSpywDDISQAAKDLVTRLMEVEQDQRI 254
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
115-451 2.29e-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: 79.15  E-value: 2.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd06619   4 QYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQI--MSELEILYKCDSPYIIGFYGAFFVENRISICTEFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHILRqKQPGKHFSELAArfyasEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptLIQST 274
Cdd:cd06619  82 DGGSLDVYR-KIPEHVLGRIAV-----AVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQ------LVNSI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTekagsdslpmliaeptaarsmsFVGTHEYLAPE 354
Cdd:cd06619 150 --------------------------------------------AKT----------------------YVGTNAYMAPE 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPF-KGNGNRETLFN-------VVGQPLKFPEGSISFAAKDLIRGLLTKDPKK 426
Cdd:cd06619 164 RISGEQYGIHSDVWSLGISFMELALGRFPYpQIQKNQGSLMPlqllqciVDEDPPVLPVGQFSEKFVHFITQCMRKQPKE 243
                       330       340
                ....*....|....*....|....*...
gi 15242554 427 RLgfkkGATEIKQHPF---FNNVNWALI 451
Cdd:cd06619 244 RP----APENLMDHPFivqYNDGNAEVV 267
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
117-460 2.63e-16

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: 79.54  E-value: 2.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd07841   5 GKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGINFTALREIklLQELKHPNIIGLLDVFGHKSNINLVFEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGgDL-HILRQKQPgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSPTLIQs 273
Cdd:cd07841  85 ET-DLeKVIKDKSI--VLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA-RSFGSPNRKM- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfVGTHEYLAP 353
Cdd:cd07841 160 THQ--------------------------------------------------------------------VVTRWYRAP 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPL-----------------KFPEGSIS--F 410
Cdd:cd07841 172 ELLFGARHyGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLgkiFEALGTPTeenwpgvtslpdyvefkPFPPTPLKqiF 251
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 411 AAK-----DLIRGLLTKDPKKRLgfkkGATEIKQHPFFNNvnwaLIRSTTPPEIP 460
Cdd:cd07841 252 PAAsddalDLLQRLLTLNPNKRI----TARQALEHPYFSN----DPAPTPPSQLP 298
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
172-443 2.73e-16

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: 78.74  E-value: 2.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 172 PFLPTLYSHFETEKFSCLLMEFCSGGDL--HI---LRQKQPGKHFSEL------AARFY---------ASEVLLALEYLH 231
Cdd:cd05576  51 PNMVCLRKYIISEESVFLVLQHAEGGKLwsYLskfLNDKEIHQLFADLderlaaASRFYipeeciqrwAAEMVVALDALH 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 232 MMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptliqstSQPSChiasyciqppcidpscklpvacIQPSCfkprf 311
Cdd:cd05576 131 REGIVCRDLNPNNILLNDRGHIQLTYF----------------SRWSE----------------------VEDSC----- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 312 lnnkprkaktekaGSDSLPMLiaeptaarsmsfvgtheYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG--- 388
Cdd:cd05576 168 -------------DSDAIENM-----------------YCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHPagi 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 389 NRETLFNVvgqplkfPEgSISFAAKDLIRGLLTKDPKKRLGF-KKGATEIKQHPFF 443
Cdd:cd05576 218 NTHTTLNI-------PE-WVSEEARSLLQQLLQFNPTERLGAgVAGVEDIKSHPFF 265
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
114-444 2.75e-16

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: 79.30  E-value: 2.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRkklVRAQTEREILGLL---DHPFLPTLYSHF-ETEKFScL 189
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGG---IPNQALREIKALQacqGHPYVVKLRDVFpHGTGFV-L 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCsGGDLH-ILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSP 268
Cdd:cd07832  78 VFEYM-LSSLSeVLRDEE--RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA-RLFSEE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 TLIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfVGTH 348
Cdd:cd07832 154 DPRLYSHQ--------------------------------------------------------------------VATR 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRG-DGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK--FPE-------GSISF----- 410
Cdd:cd07832 166 WYRAPELLYGsRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLaivLRTLGTPNEktWPEltslpdyNKITFpeskg 245
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 411 ------------AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFN 444
Cdd:cd07832 246 irleeifpdcspEAIDLLKGLLVYNPKKRL----SAEEALRHPYFF 287
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
121-432 2.88e-16

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: 78.46  E-value: 2.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 121 GCGDIGSVYLAelremgcffamKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLH 200
Cdd:cd14060   2 GGGSFGSVYRA-----------IWVSQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 201 -ILRQKQPGK-HFSELAArfYASEVLLALEYLHM---MGVVYRDLKPENVMVREDGHIMLSDFDLSlqSFVSPTLIqsts 275
Cdd:cd14060  71 dYLNSNESEEmDMDQIMT--WATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGAS--RFHSHTTH---- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYLAPEI 355
Cdd:cd14060 143 ------------------------------------------------------------------MSLVGTFPWMAPEV 156
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQPLKFPEG-SISFAakDLIRGLLTKDPKKRLGFKK 432
Cdd:cd14060 157 IQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVekNERPTIPSScPRSFA--ELMRRCWEADVKERPSFKQ 234
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
119-443 4.24e-16

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: 78.87  E-value: 4.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMDKgmligRKKLVRAQTEREILGLLD--HPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd06659  28 KIGEGSTGVVCIAREKHSGRQVAVKMMDL-----RKQQRRELLFNEVVIMRDyqHPNVVEMYKSYLVGEELWVLMEYLQG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL-HILRQKQpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqsts 275
Cdd:cd06659 103 GALtDIVSQTR----LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGF--------------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaCIQPSCFKPRflnnkpRKaktekagsdslpmliaeptaarsmSFVGTHEYLAPEI 355
Cdd:cd06659 164 -------------------------CAQISKDVPK------RK------------------------SLVGTPYWMAPEV 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS--ISFAAKDLIRGLLTKDPKKRlgfkKG 433
Cdd:cd06659 189 ISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNShkASPVLRDFLERMLVRDPQER----AT 264
                       330
                ....*....|
gi 15242554 434 ATEIKQHPFF 443
Cdd:cd06659 265 AQELLDHPFL 274
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
118-442 6.22e-16

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: 78.27  E-value: 6.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVmdkgmLIGRKKlvrAQTEREILGLL-DHPFLPTLYSHF--------ETEKFSC 188
Cdd:cd14171  12 QKLGTGISGPVRVCVKKSTGERFALKI-----LLDRPK---ARTEVRLHMMCsGHPNIVQIYDVYansvqfpgESSPRAR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LL--MEFCSGGDL--HILRQKqpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVR---EDGHIMLSDF--- 258
Cdd:cd14171  84 LLivMELMEGGELfdRISQHR----HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKdnsEDAPIKLCDFgfa 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLQSFVSPtliqstsqpscHIASYCIQPPCIDPScklpvaciqpscfkprflnnkpRKAKTEKAGSDSlpmliaepta 338
Cdd:cd14171 160 KVDQGDLMTP-----------QFTPYYVAPQVLEAQ----------------------RRHRKERSGIPT---------- 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 arsmsfVGTHEYlapeiirgdgHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPL-----KFPEGS---ISF 410
Cdd:cd14171 197 ------SPTPYT----------YDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDMKRKImtgsyEFPEEEwsqISE 260
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 411 AAKDLIRGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14171 261 MAKDIVRKLLCVDPEERMTIE----EVLHHPW 288
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
120-427 6.77e-16

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 79.91  E-value: 6.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  120 LGCGDIGSVYLAELREMGCFFAMKVMD-KGMLIGRKKlvRAQTEreILGLLDHPFLPTLYSHfetEKFS----------- 187
Cdd:PTZ00283  40 LGSGATGTVLCAKRVSDGEPFAVKVVDmEGMSEADKN--RAQAE--VCCLLNCDFFSIVKCH---EDFAkkdprnpenvl 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  188 --CLLMEFCSGGDL--HILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlq 263
Cdd:PTZ00283 113 miALVLDYANAGDLrqEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFS-- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  264 sfvsptliqstsqpschiasyciqppcidpscKLPVACIqpscfkprflnnkprkaktekagSDSLpmliaeptaarSMS 343
Cdd:PTZ00283 191 --------------------------------KMYAATV-----------------------SDDV-----------GRT 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  344 FVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV-GQPLKFPEgSISFAAKDLIRGLLTK 422
Cdd:PTZ00283 205 FCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLaGRYDPLPP-SISPEMQEIVTALLSS 283

                 ....*
gi 15242554  423 DPKKR 427
Cdd:PTZ00283 284 DPKRR 288
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
113-442 7.59e-16

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: 77.37  E-value: 7.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVM--DKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFE--TEKFSC 188
Cdd:cd06653   3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDlhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsp 268
Cdd:cd06653  83 IFVEYMPGGS--VKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG--------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiASYCIQPPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaEPTAARSMSfvGTH 348
Cdd:cd06653 152 -------------ASKRIQTICM-------------------------------------------SGTGIKSVT--GTP 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLK--FPEGsISFAAKDLIRGLLTKDPKK 426
Cdd:cd06653 174 YWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKpqLPDG-VSDACRDFLRQIFVEEKRR 252
                       330
                ....*....|....*.
gi 15242554 427 RLgfkkgATEIKQHPF 442
Cdd:cd06653 253 PT-----AEFLLRHPF 263
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
114-442 8.88e-16

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: 77.42  E-value: 8.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIID--LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliqs 273
Cdd:cd06641  84 LGGGSALDLLEPGP---LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQ---------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYLAP 353
Cdd:cd06641 151 ------------------------------------------------------------LTDTQIKRN*FVGTPFWMAP 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKkrlgFKKG 433
Cdd:cd06641 171 EVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPS----FRPT 246

                ....*....
gi 15242554 434 ATEIKQHPF 442
Cdd:cd06641 247 AKELLKHKF 255
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
120-389 8.98e-16

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: 77.11  E-value: 8.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVM--DKGMLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLhsSPNCIEERKALLK---EAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DL-HILRQKQPGKHFSeLAARFyASEVLLALEYLHMM--GVVYRDLKPENVMVREDGHIMLSDFDLSlqSFVSPTLIQSt 274
Cdd:cd13978  78 SLkSLLEREIQDVPWS-LRFRI-IHEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLS--KLGMKSISAN- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGsdslpmliaeptaarsmsfvGTHEYLAPE 354
Cdd:cd13978 153 ------------------------------------------RRRGTENLG--------------------GTPIYMAPE 170
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15242554 355 IIRgDGHG---SSVDWWTFGIFLYELLTGKTPFKGNGN 389
Cdd:cd13978 171 AFD-DFNKkptSKSDVYSFAIVIWAVLTRKEPFENAIN 207
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
205-463 9.84e-16

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 77.46  E-value: 9.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 205 KQPGKHFSELAARFYASEVLLALEYLH-MMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptLIQSTsqpschias 283
Cdd:cd06617  94 YDKGLTIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGISGY------LVDSV--------- 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 284 yciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSdslpmliaeptaarsmsfvgtHEYLAPEIIRGDGH-- 361
Cdd:cd06617 159 -----------------------------------AKTIDAGC---------------------KPYMAPERINPELNqk 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 362 GSSV--DWWTFGIFLYELLTGKTPFKGNGNR-ETLFNVV-GQPLKFPEGSISFAAKDLIRGLLTKDPKKRLGFkkgaTEI 437
Cdd:cd06617 183 GYDVksDVWSLGITMIELATGRFPYDSWKTPfQQLKQVVeEPSPQLPAEKFSPEFQDFVNKCLKKNYKERPNY----PEL 258
                       250       260
                ....*....|....*....|....*.
gi 15242554 438 KQHPFFNNvnwALIRSTTPPEIPKPI 463
Cdd:cd06617 259 LQHPFFEL---HLSKNTDVASFVSLI 281
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
113-261 1.14e-15

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 77.11  E-value: 1.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdkgmligRKKLVRAQTERE--ILGLL-DHPFLPTLYSHFETEKFSCL 189
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIE-------KKDSKHPQLEYEakVYKLLqGGPGIPRLYWFGQEGDYNVM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCsGGDLHILRQKQPGKhFSE-----LAarfyaSEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLS 261
Cdd:cd14016  74 VMDLL-GPSLEDLFNKCGRK-FSLktvlmLA-----DQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLA 146
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
151-444 1.43e-15

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 76.97  E-value: 1.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 151 IGRKKLVRAQ----TEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLA 226
Cdd:cd14201  40 INKKNLSKSQillgKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLQAK--GTLSEDTIRVFLQQIAAA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 227 LEYLHMMGVVYRDLKPENVMVREDGHimlsdfdlsLQSFVSPTLIQstsqpschIASYCIqppcidpscklpvaciqpsc 306
Cdd:cd14201 118 MRILHSKGIIHRDLKPQNILLSYASR---------KKSSVSGIRIK--------IADFGF-------------------- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 307 fkPRFLNNKprkaktekagsdslpMLIAeptaarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG 386
Cdd:cd14201 161 --ARYLQSN---------------MMAA--------TLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQA 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 387 NGNRE-TLF---NVVGQPLKFPEGSISFAakDLIRGLLTKDPKKRLGFKKgateIKQHPFFN 444
Cdd:cd14201 216 NSPQDlRMFyekNKNLQPSIPRETSPYLA--DLLLGLLQRNQKDRMDFEA----FFSHPFLE 271
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
114-443 1.83e-15

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: 76.12  E-value: 1.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMD------KGMLIGRKKLVRAQTEREILGLLDhpflptlySHFETEKFs 187
Cdd:cd06647   9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNlqqqpkKELIINEILVMRENKNPNIVNYLD--------SYLVGDEL- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDL-HILRQKQPGKhfSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfv 266
Cdd:cd06647  80 WVVMEYLAGGSLtDVVTETCMDE--GQIAA--VCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsqpschiaSYCIQppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVG 346
Cdd:cd06647 148 ----------------GFCAQ----------------------------------------------ITPEQSKRSTMVG 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQP-LKFPEgSISFAAKDLIRGLLTKD 423
Cdd:cd06647 166 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtnGTPeLQNPE-KLSAIFRDFLNRCLEMD 244
                       330       340
                ....*....|....*....|
gi 15242554 424 PKKRlgfkKGATEIKQHPFF 443
Cdd:cd06647 245 VEKR----GSAKELLQHPFL 260
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
114-440 3.68e-15

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: 75.87  E-value: 3.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLY-SHFETEKFScLLME 192
Cdd:cd14046   8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK--LRSESKNNSRILREVMLLSRLNHQHVVRYYqAWIERANLY-IQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGgdlHILRQK-QPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptli 271
Cdd:cd14046  85 YCEK---STLRDLiDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL----------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSDSLPMLIAEPTAAR------SMSFV 345
Cdd:cd14046 151 -----------------------------------------------ATSNKLNVELATQDINKSTSAAlgssgdLTGNV 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDG--HGSSVDWWTFGIFLYELLtgkTPFKGNGNRetlFNVVGQ--------PLKFPEGSISFAAKdL 415
Cdd:cd14046 184 GTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPFSTGMER---VQILTAlrsvsiefPPDFDDNKHSKQAK-L 256
                       330       340
                ....*....|....*....|....*
gi 15242554 416 IRGLLTKDPKKRlgfkKGATEIKQH 440
Cdd:cd14046 257 IRWLLNHDPAKR----PSAQELLKS 277
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
162-427 3.97e-15

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: 75.24  E-value: 3.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGD-LHILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDL 240
Cdd:cd14111  49 EYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKElLHSLIDR---FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDI 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 241 KPENVMVREDGHIMLSDFdlslqsfvsptliqSTSQPschiasyciqppcidpscklpvaciqpscFKPRFLNNKPRKak 320
Cdd:cd14111 126 KPDNIMVTNLNAIKIVDF--------------GSAQS-----------------------------FNPLSLRQLGRR-- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 321 tekagsdslpmliaeptaarsmsfVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG-- 398
Cdd:cd14111 161 ------------------------TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVak 216
                       250       260       270
                ....*....|....*....|....*....|.
gi 15242554 399 -QPLK-FPegSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14111 217 fDAFKlYP--NVSQSASLFLKKVLSSYPWSR 245
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
115-436 4.29e-15

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: 75.11  E-value: 4.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELRemGCFFAMKVMDKGmligRKKLVRAQT---EREILGLlDHPF---LPTLYSHFETEKFSC 188
Cdd:cd13979   6 RLQEPLGSGGFGSVYKATYK--GETVAVKIVRRR----RKNRASRQSfwaELNAARL-RHENivrVLAAETGTDFASLGL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHILRQKQPGKHFSELAARfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFvsp 268
Cdd:cd13979  79 IIMEYCGNGTLQQLIYEGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLG--- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciQPSCFKPRFLNNKprkaktekagsdslpmliaeptaarsmsfvGTH 348
Cdd:cd13979 155 ----------------------------------EGNEVGTPRSHIG------------------------------GTY 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNgNRETLFNVVGQPLKfPE--GSISFAAKDLIRGLLTKDPKK 426
Cdd:cd13979 171 TYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL-RQHVLYAVVAKDLR-PDlsGLEDSEFGQRLRSLISRCWSA 248
                       330
                ....*....|
gi 15242554 427 RLGFKKGATE 436
Cdd:cd13979 249 QPAERPNADE 258
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
154-443 5.06e-15

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: 74.94  E-value: 5.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 154 KKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGgDLHILRQKQPGKHFSELaaRFYASEVLLALEYLHMM 233
Cdd:cd14108  40 KKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE-ELLERITKRPTVCESEV--RSYMRQLLEGIEYLHQN 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 234 GVVYRDLKPENVMVREDG--HIMLSDFDLSLQsfVSPtliqstsqpschiasyciqppcidpscklpvaciqpscfkprf 311
Cdd:cd14108 117 DVLHLDLKPENLLMADQKtdQVRICDFGNAQE--LTP------------------------------------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 312 lnNKPRKAKtekagsdslpmliaeptaarsmsfVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRE 391
Cdd:cd14108 152 --NEPQYCK------------------------YGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRT 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 392 TLFNVVGQPLKFPEG---SISFAAKDLIRGLLTKDpkkRLgfKKGATEIKQHPFF 443
Cdd:cd14108 206 TLMNIRNYNVAFEESmfkDLCREAKGFIIKVLVSD---RL--RPDAEETLEHPWF 255
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
188-442 8.27e-15

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: 74.64  E-value: 8.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLL--MEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFdlsl 262
Cdd:cd14172  75 CLLiiMECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDF---- 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 263 qSFVSPTLIQSTsqpschiasycIQPPCIDPScklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsm 342
Cdd:cd14172 151 -GFAKETTVQNA-----------LQTPCYTPY------------------------------------------------ 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 343 sfvgtheYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNV-----VGQpLKFPE---GSISFAAKD 414
Cdd:cd14172 171 -------YVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMkrrirMGQ-YGFPNpewAEVSEEAKQ 242
                       250       260
                ....*....|....*....|....*...
gi 15242554 415 LIRGLLTKDPKKRLGFkkgaTEIKQHPF 442
Cdd:cd14172 243 LIRHLLKTDPTERMTI----TQFMNHPW 266
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
101-443 9.43e-15

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 75.04  E-value: 9.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 101 VKCSKnedlgLGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKL--VRAQTEREILGLLDHP-FLPTL 177
Cdd:cd07866   2 YGCSK-----LRDYEILGKLGEGTFGEVYKARQIKTGRVVALK---KILMHNEKDGfpITALREIKILKKLKHPnVVPLI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 178 ---YSHFETEKFS--CLLMEF---CS--GGDLHilrqkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV 247
Cdd:cd07866  74 dmaVERPDKSKRKrgSVYMVTpymDHdlSGLLE-----NPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 248 REDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTEKAGSD 327
Cdd:cd07866 149 DNQGILKIADFGLA------------------------------------------------RPYDGPPPNPKGGGGGGT 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 328 slpmliaeptaARSMSFVGTHEYLAPEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK- 402
Cdd:cd07866 181 -----------RKYTNLVVTRWYRPPELLLGErRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLhliFKLCGTPTEe 249
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 403 -FP--------EGSISFAAK----------------DLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07866 250 tWPgwrslpgcEGVHSFTNYprtleerfgklgpeglDLLSKLLSLDPYKRL----TASDALEHPYF 311
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
104-442 1.01e-14

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: 74.72  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 104 SKNEDLGLGHFRLLKKLGCGDIGSVYlaelremgcffAMKVMDKGMLIGRKKLVRAQTERE---ILGLLD-----H--PF 173
Cdd:cd06618   7 GKKYKADLNDLENLGEIGSGTCGQVY-----------KMRHKKTGHVMAVKQMRRSGNKEEnkrILMDLDvvlksHdcPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 174 LPTLYSHF--ETEKFSCL-LMEFCSggDLHILRQKQPgkhFSELAARFYASEVLLALEYL---HmmGVVYRDLKPENVMV 247
Cdd:cd06618  76 IVKCYGYFitDSDVFICMeLMSTCL--DKLLKRIQGP---IPEDILGKMTVSIVKALHYLkekH--GVIHRDVKPSNILL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 248 REDGHIMLSDFDlslqsfVSPTLIQStsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSd 327
Cdd:cd06618 149 DESGNVKLCDFG------ISGRLVDS--------------------------------------------KAKTRSAGC- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 328 slpmliaeptAArsmsfvgtheYLAPEIIRGDGHGS---SVDWWTFGIFLYELLTGKTPFKG-NGNRETLFNVVGQPLKF 403
Cdd:cd06618 178 ----------AA----------YMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNcKTEFEVLTKILNEEPPS 237
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242554 404 PEGSISFAA--KDLIRGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd06618 238 LPPNEGFSPdfCSFVDLCLTKDHRYRPKYR----ELLQHPF 274
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
120-261 1.03e-14

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: 73.90  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMdkgmligRKKLVRAQT-EREI---LGLLDHPFLPTLYS-HFETEKFSCLLMEFC 194
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFV-------PKPSTKLKDfLREYnisLELSVHPHIIKTYDvAFETEDYYVFAQEYA 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 195 SGGDLHILRQKQPGKHfsELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV--REDGHIMLSDFDLS 261
Cdd:cd13987  74 PYGDLFSIIPPQVGLP--EERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLT 140
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
114-427 1.07e-14

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: 74.13  E-value: 1.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKgmLIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFE-TEKFSCLL 190
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDR--RRASPDFVQKFLPRElsILRRVNHPNIVQMFECIEvANGRLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEfcsGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG-HIMLSDFDLSLQSFVSPT 269
Cdd:cd14164  80 ME---AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 LiqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarSMSFVGTHE 349
Cdd:cd14164 157 L----------------------------------------------------------------------STTFCGSRA 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGS-SVDWWTFGIFLYELLTGKTPFKGNGNRetLFNVVGQPLKFPEG-SISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14164 167 YTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDETNVR--RLRLQQRGVLYPSGvALEEPCRALIRTLLQFNPSTR 244
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
120-442 1.37e-14

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: 73.72  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMK--VMDKGMLIG---RKKLVRA-QTEREILGLLDHP-FLPTLYSHFETEKFSCLLmE 192
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENkdrKKSMLDAlQREIALLRELQHEnIVQYLGSSSDANHLNIFL-E 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQkQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptlIQ 272
Cdd:cd06628  87 YVPGGSVATLLN-NYGA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKK-------LE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 STSqpschiasyciqppcidpscklpvaciqpscfkprfLNNKPRKAKTekagsdslpmliaeptaarsmSFVGTHEYLA 352
Cdd:cd06628 158 ANS------------------------------------LSTKNNGARP---------------------SLQGSVFWMA 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRlgfkK 432
Cdd:cd06628 181 PEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPSNISSEARDFLEKTFEIDHNKR----P 256
                       330
                ....*....|
gi 15242554 433 GATEIKQHPF 442
Cdd:cd06628 257 TADELLKHPF 266
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
119-387 1.46e-14

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: 74.23  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFL------PTLYSHFETEKFSCLLME 192
Cdd:cd14038   1 RLGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRE--RWCLEIQIMKRLNHPNVvaardvPEGLQKLAPNDLPLLAME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLH-ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVmvredghimlsdfdlslqsfvsptLI 271
Cdd:cd14038  79 YCQGGDLRkYLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENI------------------------VL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 QSTSQPSCHiasyciqpPCIDPScklpvaciqpscfkprflnnkprKAKTEKAGSdslpmliaeptaaRSMSFVGTHEYL 351
Cdd:cd14038 135 QQGEQRLIH--------KIIDLG-----------------------YAKELDQGS-------------LCTSFVGTLQYL 170
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN 387
Cdd:cd14038 171 APELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPN 206
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
113-443 1.57e-14

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: 73.42  E-value: 1.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMlIGRKKLVRAQTE--REI-----LGLLDHPFLPTLYSHFETEK 185
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSR-VTEWAMINGPVPvpLEIalllkASKPGVPGVIRLLDWYERPD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLME----------FCSG-GDLhilrqkqpgkhfSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHI 253
Cdd:cd14005  80 GFLLIMErpepcqdlfdFITErGAL------------SENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLInLRTGEV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 254 MLSDFDlslqsfvsptliqstsqpschiasyciqppCIDPscklpvacIQPSCFKprflnnkprkaktekagsdslpmli 333
Cdd:cd14005 148 KLIDFG------------------------------CGAL--------LKDSVYT------------------------- 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 334 aeptaarsmSFVGTHEYLAPEIIR-GDGHGSSVDWWTFGIFLYELLTGKTPFkgngnRETLFNVVGQPLKFPegSISFAA 412
Cdd:cd14005 165 ---------DFDGTRVYSPPEWIRhGRYHGRPATVWSLGILLYDMLCGDIPF-----ENDEQILRGNVLFRP--RLSKEC 228
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242554 413 KDLIRGLLTKDPKKRLGFKkgatEIKQHPFF 443
Cdd:cd14005 229 CDLISRCLQFDPSKRPSLE----QILSHPWF 255
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
176-482 2.01e-14

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 74.55  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 176 TLYSHFETEKFSCLLMEFCSGGDLHILR-------------QKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKP 242
Cdd:cd07879  66 TLLKHMQHENVIGLLDVFTSAVSGDEFQdfylvmpymqtdlQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKP 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 243 ENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTE 322
Cdd:cd07879 146 GNLAVNEDCELKILDFGLA-------------------------------------------------------RHADAE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 323 KAGsdslpmliaeptaarsmsFVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVG 398
Cdd:cd07879 171 MTG------------------YVVTRWYRAPEVILNWMHyNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLtqiLKVTG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 399 QP-----------------------------LKFPEGSISfaAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFNNvnwa 449
Cdd:cd07879 233 VPgpefvqkledkaaksyikslpkyprkdfsTLFPKASPQ--AVDLLEKMLELDVDKRL----TATEALEHPYFDS---- 302
                       330       340       350
                ....*....|....*....|....*....|...
gi 15242554 450 lIRSTTPPEIPKPIDLSILNETLksSVQQQGKH 482
Cdd:cd07879 303 -FRDADEETEQQPYDDSLENEKL--SVDEWKKH 332
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
120-431 2.14e-14

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: 72.85  E-value: 2.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMgcFFAMKVMDkgMLIGRKKlvrAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14058   1 VGRGSFGVVCKARWRNQ--IVAVKIIE--SESEKKA---FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 H-ILRQKQPGKHFSELAARFYASEVLLALEYLHMM---GVVYRDLKPENVMVREDGHIM-LSDFDLslqsfvsptliqst 274
Cdd:cd14058  74 YnVLHGKEPKPIYTAAHAMSWALQCAKGVAYLHSMkpkALIHRDLKPPNLLLTNGGTVLkICDFGT-------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpSCHIASYciqppcidpscklpvaciqpscfkprFLNNKprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPE 354
Cdd:cd14058 140 ---ACDISTH--------------------------MTNNK------------------------------GSAAWMAPE 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG-------------NGNRETLFNVVGQPLkfpegsisfaaKDLIRGLLT 421
Cdd:cd14058 161 VFEGSKYSEKCDVFSWGIILWEVITRRKPFDHiggpafrimwavhNGERPPLIKNCPKPI-----------ESLMTRCWS 229
                       330
                ....*....|
gi 15242554 422 KDPKKRLGFK 431
Cdd:cd14058 230 KDPEKRPSMK 239
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
114-442 2.68e-14

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: 73.16  E-value: 2.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06640   6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIID--LEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliqs 273
Cdd:cd06640  84 LGGGSALDLLRAGP---FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQ---------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYLAP 353
Cdd:cd06640 151 ------------------------------------------------------------LTDTQIKRNTFVGTPFWMAP 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPkkrlGFKKG 433
Cdd:cd06640 171 EVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEFIDACLNKDP----SFRPT 246

                ....*....
gi 15242554 434 ATEIKQHPF 442
Cdd:cd06640 247 AKELLKHKF 255
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
114-443 2.71e-14

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: 73.31  E-value: 2.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALK---KIRLDTETEGVPSTAIREIslLKELNHPNIVKLLDVIHTENKLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSPtli 271
Cdd:cd07860  79 EFLHQ-DLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLA-RAFGVP--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschIASYciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgTHE-- 349
Cdd:cd07860 154 ---------VRTY--------------------------------------------------------------THEvv 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 ---YLAPEIIRGDGHGSS-VDWWTFGIFLYELLTGKTPFKGNGNRETLFNV---VGQP--------LKFPEGSISFA--- 411
Cdd:cd07860 163 tlwYRAPEILLGCKYYSTaVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIfrtLGTPdevvwpgvTSMPDYKPSFPkwa 242
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 412 --------------AKDLIRGLLTKDPKKRLGFKKGATeikqHPFF 443
Cdd:cd07860 243 rqdfskvvppldedGRDLLSQMLHYDPNKRISAKAALA----HPFF 284
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
120-387 3.92e-14

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: 73.03  E-value: 3.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFLPTLYS-----HFETEKFSCLLMEFC 194
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKD--RWCHEIQIMKKLNHPNVVKACDvpeemNFLVNDVPLLAMEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHILRQKQP---GKHFSELAARFyaSEVLLALEYLHMMGVVYRDLKPENVMVRE-DGHIMLSDFDLSLqsfvsptl 270
Cdd:cd14039  79 SGGDLRKLLNKPEnccGLKESQVLSLL--SDIGSGIQYLHENKIIHRDLKPENIVLQEiNGKIVHKIIDLGY-------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSdslpmliaeptaaRSMSFVGTHEY 350
Cdd:cd14039 149 ------------------------------------------------AKDLDQGS-------------LCTSFVGTLQY 167
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN 387
Cdd:cd14039 168 LAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHN 204
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
114-442 1.74e-13

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: 70.84  E-value: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06645  13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIK---LEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfVSPTLiq 272
Cdd:cd06645  90 CGGGSLQdIYHVTGP---LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQ--ITATI-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaARSMSFVGTHEYLA 352
Cdd:cd06645 163 ------------------------------------------------------------------AKRKSFIGTPYWMA 176
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 PEII---RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG---QPLKFPEG-SISFAAKDLIRGLLTKDPK 425
Cdd:cd06645 177 PEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKsnfQPPKLKDKmKWSNSFHHFVKMALTKNPK 256
                       330
                ....*....|....*..
gi 15242554 426 KRlgfkKGATEIKQHPF 442
Cdd:cd06645 257 KR----PTAEKLLQHPF 269
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
159-441 1.88e-13

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: 70.15  E-value: 1.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 159 AQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYR 238
Cdd:cd08220  46 ALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 239 DLKPENVMVREDGHIM-LSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKpR 317
Cdd:cd08220 126 DLKTQNILLNKKRTVVkIGDFGIS------------------------------------------------KILSSK-S 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 318 KAKTekagsdslpmliaeptaarsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGngnrETLFNVV 397
Cdd:cd08220 157 KAYT----------------------VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEA----ANLPALV 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 398 gqpLKFPEGSISFAA-------KDLIRGLLTKDPKKRLGFKkgatEIKQHP 441
Cdd:cd08220 211 ---LKIMRGTFAPISdryseelRHLILSMLHLDPNKRPTLS----EIMAQP 254
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
114-443 2.05e-13

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: 70.38  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligrKKLVRAQTEREILG---LLDHPFLPTLYSHFETEKFSCL- 189
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHF----KSLEQVNNLREIQAlrrLSPHPNILRLIEVLFDRKTGRLa 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 ----LMEfcsgGDLHILRQKQPgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDgHIMLSDFDlslqsf 265
Cdd:cd07831  77 lvfeLMD----MNLYELIKGRK-RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG------ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vsptliqstsqpSChiASYCIQPPcidpscklpvaciqpscfkprflnnkprkaKTEkagsdslpmliaeptaarsmsFV 345
Cdd:cd07831 145 ------------SC--RGIYSKPP------------------------------YTE---------------------YI 159
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP---------------LKFP-- 404
Cdd:cd07831 160 STRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIakiHDVLGTPdaevlkkfrksrhmnYNFPsk 239
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15242554 405 EGS--------ISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07831 240 KGTglrkllpnASAEGLDLLKKLLAYDPDERI----TAKQALRHPYF 282
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
114-442 2.79e-13

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: 70.09  E-value: 2.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06642   6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIID--LEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptliqs 273
Cdd:cd06642  84 LGGGSALDLLKPGP---LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQ---------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYLAP 353
Cdd:cd06642 151 ------------------------------------------------------------LTDTQIKRNTFVGTPFWMAP 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKkrlgFKKG 433
Cdd:cd06642 171 EVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPR----FRPT 246

                ....*....
gi 15242554 434 ATEIKQHPF 442
Cdd:cd06642 247 AKELLKHKF 255
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
114-446 3.82e-13

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: 70.16  E-value: 3.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVylaelremgcffaMKVMDK--GMLIGRKKL-------VRAQTERE--ILGLLDHPFLPTLYSHFE 182
Cdd:cd06615   3 FEKLGELGAGNGGVV-------------TKVLHRpsGLIMARKLIhleikpaIRNQIIRElkVLHECNSPYIVGFYGAFY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 183 TEKFSCLLMEFCSGGDLHILrQKQPGKHFSELAARFyASEVLLALEYLH-MMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd06615  70 SDGEISICMEHMDGGSLDQV-LKKAGRIPENILGKI-SIAVLRGLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 LQsfvsptLIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaars 341
Cdd:cd06615 148 GQ------LIDSMAN----------------------------------------------------------------- 156
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 mSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPF--KGNGNRETLFN------------------------ 395
Cdd:cd06615 157 -SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIppPDAKELEAMFGrpvsegeakeshrpvsghppdspr 235
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 396 -----------VVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRLGFKkgatEIKQHPFFNNV 446
Cdd:cd06615 236 pmaifelldyiVNEPPPKLPSGAFSDEFQDFVDKCLKKNPKERADLK----ELTKHPFIKRA 293
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
107-404 5.49e-13

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: 69.30  E-value: 5.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 107 EDLGLGHFRLLKKLGCGDIGSVYLA--ELREMGCFFAMKVMDKGMligRKKLVRAQTEREILGLLDHPFLPTLYSHFETE 184
Cdd:cd14145   1 LEIDFSELVLEEIIGIGGFGKVYRAiwIGDEVAVKAARHDPDEDI---SQTIENVRQEAKLFAMLKHPNIIALRGVCLKE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDLHilrQKQPGKHFSELAARFYASEVLLALEYLH---MMGVVYRDLKPENVMVREdghiMLSDFDLS 261
Cdd:cd14145  78 PNLCLVMEFARGGPLN---RVLSGKRIPPDILVNWAVQIARGMNYLHceaIVPVIHRDLKSSNILILE----KVENGDLS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 LQSFvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKAGsdslpmLIAEPTAARS 341
Cdd:cd14145 151 NKIL------------------------------------------------------KITDFG------LAREWHRTTK 170
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 342 MSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFP 404
Cdd:cd14145 171 MSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP 233
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
137-378 6.11e-13

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 69.07  E-value: 6.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 137 GCFF-AMKVMDK--GMLIGRKKLVRAQ--------TEREILGLLDHP----FLPTLYShfetEKFSCLLMEFCSGGDLHI 201
Cdd:cd14154   4 GFFGqAIKVTHRetGEVMVMKELIRFDeeaqrnflKEVKVMRSLDHPnvlkFIGVLYK----DKKLNLITEYIPGGTLKD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 202 LrQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSPtliqstsqpschi 281
Cdd:cd14154  80 V-LKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLA-RLIVEE------------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 282 asyciqppcidpscKLPVACIQPSCFKPRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLAPEIIRGDGH 361
Cdd:cd14154 145 --------------RLPSGNMSPSETLRHLKSPDRKKRYT----------------------VVGNPYWMAPEMLNGRSY 188
                       250
                ....*....|....*..
gi 15242554 362 GSSVDWWTFGIFLYELL 378
Cdd:cd14154 189 DEKVDIFSFGIVLCEII 205
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
111-427 6.49e-13

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: 69.29  E-value: 6.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd08229  23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd08229 103 LELADAGDLSrmIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG------- 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKprkaktekagsdslpmliaePTAARSMsfVGTH 348
Cdd:cd08229 176 -----------------------------------------RFFSSK--------------------TTAAHSL--VGTP 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG-NRETLFNVVGQ----PLkfPEGSISFAAKDLIRGLLTKD 423
Cdd:cd08229 193 YYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmNLYSLCKKIEQcdypPL--PSDHYSEELRQLVNMCINPD 270

                ....
gi 15242554 424 PKKR 427
Cdd:cd08229 271 PEKR 274
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
112-442 7.73e-13

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: 68.88  E-value: 7.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmligrkklVRAQTEREI---LGLLD----HPFLPTLYSHFETE 184
Cdd:cd06636  16 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----------VTEDEEEEIkleINMLKkyshHRNIATYYGAFIKK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFS------CLLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd06636  86 SPPghddqlWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLQsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTA 338
Cdd:cd06636 166 GVSAQ----------------------------------------------------------------------LDRTV 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 ARSMSFVGTHEYLAPEIIRGDGHGSSV-----DWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEGSISF 410
Cdd:cd06636 176 GRRNTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPppkLKSKKWSKKF 255
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 411 AakDLIRGLLTKDPKKRlgfkKGATEIKQHPF 442
Cdd:cd06636 256 I--DFIEGCLVKNYLSR----PSTEQLLKHPF 281
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
159-427 9.90e-13

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: 68.41  E-value: 9.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 159 AQTEREILGLLDHPFLPTLYShfETEKFSCLLMEFCSGGDL-HILRQ-KQPGKHFSELAARFYASEVLLALEYLHMMGVV 236
Cdd:cd14000  57 LRQELTVLSHLHHPSIVYLLG--IGIHPLMLVLELAPLGSLdHLLQQdSRSFASLGRTLQQRIALQVADGLRYLHSAMII 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 237 YRDLKPENVMV-----REDGHIMLSDFDLSLQSFvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprf 311
Cdd:cd14000 135 YRDLKSHNVLVwtlypNSAIIIKIADYGISRQCC---------------------------------------------- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 312 lnnkPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGNGNR 390
Cdd:cd14000 169 ----RMGAKG----------------------SEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLKF 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15242554 391 ETLFNVVGQ---PLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd14000 223 PNEFDIHGGlrpPLKQYECAPWPEVEVLMKKCWKENPQQR 262
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
120-409 1.05e-12

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: 69.06  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDK-GMLigRKKLVRAQtEREILGLLDHPFLPTLYSHFE--TEKFSCLLMEFCSG 196
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFM--RPLDVQMR-EFEVLKKLNHKNIVKLFAIEEelTTRHKVLVMELCPC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLH-ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVM--VREDGHIM--LSDFDlslqsfvsptli 271
Cdd:cd13988  78 GSLYtVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSVykLTDFG------------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKAGSDSLpmliaeptaarsMSFVGTHEYL 351
Cdd:cd13988 146 -----------------------------------------------AARELEDDEQF------------VSLYGTEEYL 166
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIR--------GDGHGSSVDWWTFGIFLYELLTGKTPFK----GNGNRETLFNVVGQPlkfPEGSIS 409
Cdd:cd13988 167 HPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPFRpfegPRRNKEVMYKIITGK---PSGAIS 233
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
119-443 1.13e-12

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: 68.45  E-value: 1.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVM-----DKGMLIGRkklVRAQTEREILGLLDHPFLPTLY-----SHFETEKFSC 188
Cdd:cd07863   7 EIGVGAYGTVYKARDPHSGHFVALKSVrvqtnEDGLPLST---VREVALLKRLEAFDHPNIVRLMdvcatSRTDRETKVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd07863  84 LVFEHVDQ-DLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstSQPSCHIAsyciqppcIDPscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsFVGTH 348
Cdd:cd07863 156 ------RIYSCQMA--------LTP--------------------------------------------------VVVTL 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP--------LKFPEGS---------- 407
Cdd:cd07863 172 WYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLgkiFDLIGLPpeddwprdVTLPRGAfsprgprpvq 251
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242554 408 -----ISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07863 252 svvpeIEESGAQLLLEMLTFNPHKRI----SAFRALQHPFF 288
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
113-442 1.79e-12

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: 67.38  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKVM--DKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFE--TEKFSC 188
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRdpQERTLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDlhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsp 268
Cdd:cd06652  83 IFMEYMPGGS--IKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG--------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiASYCIQPPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaepTAARSMSFVGTH 348
Cdd:cd06652 152 -------------ASKRLQTICL---------------------------------------------SGTGMKSVTGTP 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPL--KFPeGSISFAAKDLIRGLLTkDPKK 426
Cdd:cd06652 174 YWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTnpQLP-AHVSDHCRDFLKRIFV-EAKL 251
                       330
                ....*....|....*.
gi 15242554 427 RlgfkKGATEIKQHPF 442
Cdd:cd06652 252 R----PSADELLRHTF 263
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
117-443 1.81e-12

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: 67.82  E-value: 1.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMD------KGMLIGRKKLVRAQTEREILGLLDhpflptlySHFETEKFsCLL 190
Cdd:cd06656  24 FEKIGQGASGTVYTAIDIATGQEVAIKQMNlqqqpkKELIINEILVMRENKNPNIVNYLD--------SYLVGDEL-WVV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQPGKHfSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptl 270
Cdd:cd06656  95 MEYLAGGSLTDVVTETCMDE-GQIAA--VCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF------------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiaSYCIQppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEY 350
Cdd:cd06656 160 ------------GFCAQ----------------------------------------------ITPEQSKRSTMVGTPYW 181
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQP-LKFPEgSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd06656 182 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtnGTPeLQNPE-RLSAVFRDFLNRCLEMDVDRR 260
                       330
                ....*....|....*.
gi 15242554 428 lgfkKGATEIKQHPFF 443
Cdd:cd06656 261 ----GSAKELLQHPFL 272
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
117-443 1.94e-12

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: 67.78  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKvmdkgmligrkKLVRAQTE--------REI--LGLLDHPFLPTLYSHFETEKF 186
Cdd:cd07847   6 LSKIGEGSYGVVFKCRNRETGQIVAIK-----------KFVESEDDpvikkialREIrmLKQLKHPNLVNLIEVFRRKRK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGGDLHILRQKQPGkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfv 266
Cdd:cd07847  75 LHLVFEYCDHTVLNELEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFA----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNnkprkaktekagsdslpmliaePTAARSMSFVG 346
Cdd:cd07847 148 -------------------------------------------RILT----------------------GPGDDYTDYVA 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 THEYLAPEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGN-------RETLFNVVGQ------------------- 399
Cdd:cd07847 163 TRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPLWPGKSDvdqlyliRKTLGDLIPRhqqifstnqffkglsipep 242
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15242554 400 ----PL--KFPegSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07847 243 etrePLesKFP--NISSPALSFLKGCLQMDPTERL----SCEELLEHPYF 286
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
120-444 2.15e-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: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLV--RAQTEREILGLLDhpflptLYSH-FETEKFSCLLMEFCSG 196
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELhwRASQCPHIVRIVD------VYENlYAGRKCLLIVMECLDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLSLQSFVSPTLiqs 273
Cdd:cd14170  84 GELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYtskRPNAILKLTDFGFAKETTSHNSL--- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciQPPCIDPScklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgtheYLAP 353
Cdd:cd14170 161 -------------TTPCYTPY-------------------------------------------------------YVAP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN-------GNRETLfnVVGQpLKFPE---GSISFAAKDLIRGLLTKD 423
Cdd:cd14170 173 EVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaispGMKTRI--RMGQ-YEFPNpewSEVSEEVKMLIRNLLKTE 249
                       330       340
                ....*....|....*....|.
gi 15242554 424 PKKRLGFkkgaTEIKQHPFFN 444
Cdd:cd14170 250 PTQRMTI----TEFMNHPWIM 266
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
223-445 2.31e-12

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: 67.35  E-value: 2.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 223 VLLALEYLH-MMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqstsqpschiasYCIQPPcidpscklpvac 301
Cdd:cd14011 123 ISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFD------------------------FCISSE------------ 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 302 iQPSCFKPRFLNNKPRKAktekagSDSLPMLiaeptaarsmsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELL-TG 380
Cdd:cd14011 167 -QATDQFPYFREYDPNLP------PLAQPNL----------------NYLAPEYILSKTCDPASDMFSLGVLIYAIYnKG 223
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 381 KTPFKGNGNRET---LFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFNN 445
Cdd:cd14011 224 KPLFDCVNNLLSykkNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRP----DAEQLSKIPFFDD 287
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
114-440 2.41e-12

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: 67.13  E-value: 2.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdkgmligRKKLVRAQTEREI--LGLLDHP--------------FLPTL 177
Cdd:cd14047   8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIK---------RVKLNNEKAEREVkaLAKLDHPnivryngcwdgfdyDPETS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 178 YSHFETEKFSCLL--MEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIML 255
Cdd:cd14047  79 SSNSSRSKTKCLFiqMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 256 SDFDLslqsfvsptliqSTSQPSchiasyciqppcidpscklpvaciqpscfkprflNNKPRKAKtekagsdslpmliae 335
Cdd:cd14047 159 GDFGL------------VTSLKN----------------------------------DGKRTKSK--------------- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 336 ptaarsmsfvGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTpfKGNGNRETLFNVVGQ--PLKFPEGsiSFAAK 413
Cdd:cd14047 178 ----------GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCD--SAFEKSKFWTDLRNGilPDIFDKR--YKIEK 243
                       330       340
                ....*....|....*....|....*..
gi 15242554 414 DLIRGLLTKDPKKRlgfkKGATEIKQH 440
Cdd:cd14047 244 TIIKKMLSKKPEDR----PNASEILRT 266
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
114-443 2.60e-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: 68.05  E-value: 2.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGM---LIGRK-----KLVRAQTEREILGLLDhPFLPTLyshfETEK 185
Cdd:cd07880  17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFqseLFAKRayrelRLLKHMKHENVIGLLD-VFTPDL----SLDR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FS--CLLMEFCsGGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlq 263
Cdd:cd07880  92 FHdfYLVMPFM-GTDLGKLMKHE---KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA-- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 sfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGsdslpmliaeptaarsms 343
Cdd:cd07880 166 -----------------------------------------------------RQTDSEMTG------------------ 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 FVGTHEYLAPEIIRGDGHGS-SVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK----------------- 402
Cdd:cd07880 175 YVVTRWYRAPEVILNWMHYTqTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLmeiMKVTGTPSKefvqklqsedaknyvkk 254
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 403 FPE------GSI----SFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07880 255 LPRfrkkdfRSLlpnaNPLAVNVLEKMLVLDAESRI----TAAEALAHPYF 301
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
114-247 2.99e-12

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: 66.87  E-value: 2.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdkgmligRKKLVRAQTEREILGLLD---------HPFLPTLYSHFETE 184
Cdd:cd14139   2 FLELEKIGVGEFGSVYKCIKRLDGCVYAIK---------RSMRPFAGSSNEQLALHEvyahavlghHPHVVRYYSAWAED 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 185 KFSCLLMEFCSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV 247
Cdd:cd14139  73 DHMIIQNEYCNGGSLQdaISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI 137
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
117-443 3.66e-12

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: 67.06  E-value: 3.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMD------KGMLIGRKKLVRAQTEREILGLLDhpflptlySHFETEKFsCLL 190
Cdd:cd06654  25 FEKIGQGASGTVYTAMDVATGQEVAIRQMNlqqqpkKELIINEILVMRENKNPNIVNYLD--------SYLVGDEL-WVV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQPGKHfSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptl 270
Cdd:cd06654  96 MEYLAGGSLTDVVTETCMDE-GQIAA--VCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF------------ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiaSYCIQppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEY 350
Cdd:cd06654 161 ------------GFCAQ----------------------------------------------ITPEQSKRSTMVGTPYW 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQP-LKFPEgSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd06654 183 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtnGTPeLQNPE-KLSAIFRDFLNRCLEMDVEKR 261
                       330
                ....*....|....*.
gi 15242554 428 lgfkKGATEIKQHPFF 443
Cdd:cd06654 262 ----GSAKELLQHQFL 273
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
114-443 4.39e-12

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: 66.74  E-value: 4.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmlIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIH----LDAEEGTPSTAIREIslMKELKHENIVRLHDVIHTENKLMLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGgDL--HILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFvspt 269
Cdd:cd07836  78 EYMDK-DLkkYMDTHGVRGA-LDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA-RAF---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscKLPVAciqpscfkpRFLNNkprkaktekagsdslpmliaeptaarsmsfVGTHE 349
Cdd:cd07836 151 --------------------------GIPVN---------TFSNE------------------------------VVTLW 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP--------LKFPEGSISFA------ 411
Cdd:cd07836 166 YRAPDVLLGSrTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLlkiFRIMGTPtestwpgiSQLPEYKPTFPryppqd 245
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15242554 412 -----------AKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07836 246 lqqlfphadplGIDLLHRLLQLNPELRI----SAHDALQHPWF 284
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
111-427 5.68e-12

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: 66.20  E-value: 5.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd08228   1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd08228  81 LELADAGDLSqmIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKprkaktekagsdslpmliaePTAARSMsfVGTH 348
Cdd:cd08228 154 -----------------------------------------RFFSSK--------------------TTAAHSL--VGTP 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG-NRETLFNVVGQ----PLkfPEGSISFAAKDLIRGLLTKD 423
Cdd:cd08228 171 YYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmNLFSLCQKIEQcdypPL--PTEHYSEKLRELVSMCIYPD 248

                ....
gi 15242554 424 PKKR 427
Cdd:cd08228 249 PDQR 252
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
119-443 6.47e-12

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: 66.22  E-value: 6.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMDKgmligRKKLVRAQTEREILGLLD--HPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd06658  29 KIGEGSTGIVCIATEKHTGKQVAVKKMDL-----RKQQRRELLFNEVVIMRDyhHENVVDMYNSYLVGDELWVVMEFLEG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsq 276
Cdd:cd06658 104 GALTDIVTHT---RMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGF---------------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaCIQPSCFKPRflnnkpRKaktekagsdslpmliaeptaarsmSFVGTHEYLAPEII 356
Cdd:cd06658 165 ------------------------CAQVSKEVPK------RK------------------------SLVGTPYWMAPEVI 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ-PLKFPEG-SISFAAKDLIRGLLTKDPKKRlgfkKGA 434
Cdd:cd06658 191 SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNlPPRVKDShKVSSVLRGFLDLMLVREPSQR----ATA 266

                ....*....
gi 15242554 435 TEIKQHPFF 443
Cdd:cd06658 267 QELLQHPFL 275
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
112-445 6.61e-12

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: 66.28  E-value: 6.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmligrkklVRAQTEREI---LGLLD----HPFLPTLYSHF--- 181
Cdd:cd06637   6 GIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----------VTGDEEEEIkqeINMLKkyshHRNIATYYGAFikk 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ---ETEKFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd06637  76 nppGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLQsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTA 338
Cdd:cd06637 156 GVSAQ----------------------------------------------------------------------LDRTV 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 ARSMSFVGTHEYLAPEIIRGDGHGSSV-----DWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEGSISF 410
Cdd:cd06637 166 GRRNTFIGTPYWMAPEVIACDENPDATydfksDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPaprLKSKKWSKKF 245
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15242554 411 aaKDLIRGLLTKDPKKRlgfkKGATEIKQHPFFNN 445
Cdd:cd06637 246 --QSFIESCLVKNHSQR----PSTEQLMKHPFIRD 274
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
117-442 7.18e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 66.77  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  117 LKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmLIG-RKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:PLN00034  79 VNRIGSGAGGTVYKVIHRPTGRLYALKV-----IYGnHEDTVRRQICREIeiLRDVNHPNVVKCHDMFDHNGEIQVLLEF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  194 CSGGDLHilrqkqpGKHF-SELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfVSPTLIQ 272
Cdd:PLN00034 154 MDGGSLE-------GTHIaDEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFG------VSRILAQ 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  273 StsqpschiasyciqppcIDPsCKlpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmSFVGTHEYLA 352
Cdd:PLN00034 221 T-----------------MDP-CN----------------------------------------------SSVGTIAYMS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  353 PEIIRGD-GHGS----SVDWWTFGIFLYELLTGKTPF--KGNGNRETLFNVV--GQPLKFPeGSISFAAKDLIRGLLTKD 423
Cdd:PLN00034 237 PERINTDlNHGAydgyAGDIWSLGVSILEFYLGRFPFgvGRQGDWASLMCAIcmSQPPEAP-ATASREFRHFISCCLQRE 315
                        330
                 ....*....|....*....
gi 15242554  424 PKKRLgfkkGATEIKQHPF 442
Cdd:PLN00034 316 PAKRW----SAMQLLQHPF 330
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
114-430 8.59e-12

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: 65.44  E-value: 8.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELRemGCFFAMKVM----DKGMLIGRKKLvraQTEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd14147   5 LRLEEVIGIGGFGKVYRGSWR--GELVAVKAArqdpDEDISVTAESV---RQEARLFAMLAHPNIIALKAVCLEEPNLCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDLhilRQKQPGKHFSELAARFYASEVLLALEYLH---MMGVVYRDLKPENVMV--------REDGHIMLSDF 258
Cdd:cd14147  80 VMEYAAGGPL---SRALAGRRVPPHVLVNWAVQIARGMHYLHceaLVPVIHRDLKSNNILLlqpienddMEHKTLKITDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLQSFvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaKTEKagsdslpmliaepta 338
Cdd:cd14147 157 GLAREWH------------------------------------------------------KTTQ--------------- 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 arsMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSI---SFAakDL 415
Cdd:cd14147 168 ---MSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTcpePFA--QL 242
                       330
                ....*....|....*
gi 15242554 416 IRGLLTKDPKKRLGF 430
Cdd:cd14147 243 MADCWAQDPHRRPDF 257
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
118-443 8.92e-12

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: 65.90  E-value: 8.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMD------KGMLIGRKKLVRAQTEREILGLLDHPFLptlyshfETEKFscLLM 191
Cdd:cd06655  25 EKIGQGASGTVFTAIDVATGQEVAIKQINlqkqpkKELIINEILVMKELKNPNIVNFLDSFLV-------GDELF--VVM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQPGKHfSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptli 271
Cdd:cd06655  96 EYLAGGSLTDVVTETCMDE-AQIAA--VCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDF------------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiaSYCIQppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSMSFVGTHEYL 351
Cdd:cd06655 160 -----------GFCAQ----------------------------------------------ITPEQSKRSTMVGTPYWM 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV--GQP-LKFPEgSISFAAKDLIRGLLTKDPKKRl 428
Cdd:cd06655 183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtnGTPeLQNPE-KLSPIFRDFLNRCLEMDVEKR- 260
                       330
                ....*....|....*
gi 15242554 429 gfkKGATEIKQHPFF 443
Cdd:cd06655 261 ---GSAKELLQHPFL 272
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
114-442 1.03e-11

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: 65.49  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVM--DKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFE--TEKFSCL 189
Cdd:cd06651   9 WRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVqfDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDlhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvspt 269
Cdd:cd06651  89 FMEYMPGGS--VKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG---------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiASYCIQPPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaEPTAARSMSfvGTHE 349
Cdd:cd06651 157 ------------ASKRLQTICM-------------------------------------------SGTGIRSVT--GTPY 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS-ISFAAKDLIRGLLTkDPKKRl 428
Cdd:cd06651 180 WMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPShISEHARDFLGCIFV-EARHR- 257
                       330
                ....*....|....
gi 15242554 429 gfkKGATEIKQHPF 442
Cdd:cd06651 258 ---PSAEELLRHPF 268
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
114-443 1.20e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 65.64  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmLIGRKK-LVRAQTEREILGLL------DHPFLPTLYSHFETEKF 186
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKI-----IRNKKRfHQQALVEVKILKHLndndpdDKHNIVRYKDSFIFRGH 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH--IMLSDFDLSlqS 264
Cdd:cd14210  90 LCIVFELLSI-NLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSS--C 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 FV---SPTLIQStsqpschiasyciqppcidpscklpvaciqpscfkpRFlnnkprkaktekagsdslpmliaeptaars 341
Cdd:cd14210 167 FEgekVYTYIQS------------------------------------RF------------------------------ 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 msfvgtheYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN------------------------GNRETLFNVV 397
Cdd:cd14210 181 --------YRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGEneeeqlacimevlgvppkslidkaSRRKKFFDSN 252
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 398 GQPL--------KFPEGSISFAAK---------DLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd14210 253 GKPRpttnskgkKRRPGSKSLAQVlkcddpsflDFLKKCLRWDPSERM----TPEEALQHPWI 311
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
114-442 1.36e-11

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: 65.03  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklvrAQTEREIL-GLLDHPFLPTLYS-HFETEKFS---- 187
Cdd:cd06638  20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEE----IEAEYNILkALSDHPNVVKFYGmYYKKDVKNgdql 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDLHILRQK--QPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsF 265
Cdd:cd06638  96 WLVLELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ-L 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 VSPTLIQSTSqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfV 345
Cdd:cd06638 175 TSTRLRRNTS---------------------------------------------------------------------V 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGD-----GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPE-GSISFaaKDLI 416
Cdd:cd06638 186 GTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPpptLHQPElWSNEF--NDFI 263
                       330       340
                ....*....|....*....|....*.
gi 15242554 417 RGLLTKDPKKRlgfkKGATEIKQHPF 442
Cdd:cd06638 264 RKCLTKDYEKR----PTVSDLLQHVF 285
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
119-443 1.46e-11

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: 65.04  E-value: 1.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMDKgmligRKKLVRAQTEREILGLLD--HPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd06657  27 KIGEGSTGIVCIATVKSSGKLVAVKKMDL-----RKQQRRELLFNEVVIMRDyqHENVVEMYNSYLVGDELWVVMEFLEG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsq 276
Cdd:cd06657 102 GALTDIVTHT---RMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGF---------------- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaCIQPSCFKPRflnnkpRKaktekagsdslpmliaeptaarsmSFVGTHEYLAPEII 356
Cdd:cd06657 163 ------------------------CAQVSKEVPR------RK------------------------SLVGTPYWMAPELI 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 357 RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ-PLKFPEG-SISFAAKDLIRGLLTKDPKKRlgfkKGA 434
Cdd:cd06657 189 SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlPPKLKNLhKVSPSLKGFLDRLLVRDPAQR----ATA 264

                ....*....
gi 15242554 435 TEIKQHPFF 443
Cdd:cd06657 265 AELLKHPFL 273
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
113-427 1.64e-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: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMK---VMDKGMLIGRKKLVRAQTE----REILGLLDHPFLPTLYSHFETek 185
Cdd:cd14037   4 HVTIEKYLAEGGFAHVYLVKTSNGGNRAALKrvyVNDEHDLNVCKREIEIMKRlsghKNIVGYIDSSANRSGNGVYEV-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 fsCLLMEFCSGGdlHILRQKQpgkhfSELAARFYASEVL-------LALEYLHMMG--VVYRDLKPENVMVREDGHIMLS 256
Cdd:cd14037  82 --LLLMEYCKGG--GVIDLMN-----QRLQTGLTESEILkifcdvcEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 257 DFDlslqsfvsptliqstsqpschIASYCIQPPcidpscklpvaciqpscfkprflnnkprkakTEKAGSDSLPMLIAEP 336
Cdd:cd14037 153 DFG---------------------SATTKILPP-------------------------------QTKQGVTYVEEDIKKY 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 337 TaarsmsfvgTHEYLAPEII---RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNretlFNVVGQPLKFPEGS-ISFAA 412
Cdd:cd14037 181 T---------TLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPFEESGQ----LAILNGNFTFPDNSrYSKRL 247
                       330
                ....*....|....*
gi 15242554 413 KDLIRGLLTKDPKKR 427
Cdd:cd14037 248 HKLIRYMLEEDPEKR 262
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
346-443 1.99e-11

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: 63.91  E-value: 1.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDG--HGSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFNVV--GQpLKFPEgSISFAAKDLIRGLLT 421
Cdd:cd14023 148 GCPAYVSPEILNTTGtySGKSADVWSLGVMLYTLLVGRYPFH-DSDPSALFSKIrrGQ-FCIPD-HVSPKARCLIRSLLR 224
                        90       100
                ....*....|....*....|..
gi 15242554 422 KDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd14023 225 REPSERL----TAPEILLHPWF 242
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
111-427 2.28e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 66.30  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVM--------DKGMLIGRKKLVRAQTEREILGLLDHpFL----PTLY 178
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIsyrglkerEKSQLVIEVNVMRELKHKNIVRYIDR-FLnkanQKLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   179 shfetekfscLLMEFCSGGDLHILRQ---KQPGKhFSELAARFYASEVLLALEYLHMMG-------VVYRDLKPENVmvr 248
Cdd:PTZ00266   91 ----------ILMEFCDAGDLSRNIQkcyKMFGK-IEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNI--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   249 edghimlsdfdlslqsFVSpTLIQstsqpscHIASYCIQppcidpscklpvaciqpscfkPRFLNNKPrkakTEKAGSDS 328
Cdd:PTZ00266  157 ----------------FLS-TGIR-------HIGKITAQ---------------------ANNLNGRP----IAKIGDFG 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554   329 LPMLIAEPTAARSMsfVGTHEYLAPEII--RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEG 406
Cdd:PTZ00266  188 LSKNIGIESMAHSC--VGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQLISELKRGPDLPIK 265
                         330       340
                  ....*....|....*....|.
gi 15242554   407 SISFAAKDLIRGLLTKDPKKR 427
Cdd:PTZ00266  266 GKSKELNILIKNLLNLSAKER 286
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
120-430 2.60e-11

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: 64.29  E-value: 2.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLA--ELREMGCFFAMKVMDKGMLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd14146   2 IGVGGFGKVYRAtwKGQEVAVKAARQDPDEDIKATAESVRQ---EAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DLHILRQKQPGKHFSELAARF-------YASEVLLALEYLH---MMGVVYRDLKPENVMVREdghimlsdfdlslqsfvs 267
Cdd:cd14146  79 TLNRALAAANAAPGPRRARRIpphilvnWAVQIARGMLYLHeeaVVPILHRDLKSSNILLLE------------------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSDSLPM----LIAEPTAARSMS 343
Cdd:cd14146 141 --------------------------------------------------KIEHDDICNKTLKItdfgLAREWHRTTKMS 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 FVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSI---SFAakDLIRGLL 420
Cdd:cd14146 171 AAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLPIPSTcpePFA--KLMKECW 248
                       330
                ....*....|
gi 15242554 421 TKDPKKRLGF 430
Cdd:cd14146 249 EQDPHIRPSF 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
191-386 2.74e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 65.59  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  191 MEFCSGGDL-HILRQKQPgkhfseL----AARfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsf 265
Cdd:NF033483  86 MEYVDGRTLkDYIREHGP------LspeeAVE-IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFG------ 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  266 vsptliqstsqpschIAsyciqppcidpscklpvaciqpscfkprflnnkprKAktekagsdslpmlIAEPTAARSMSFV 345
Cdd:NF033483 153 ---------------IA-----------------------------------RA-------------LSSTTMTQTNSVL 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15242554  346 GTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG 386
Cdd:NF033483 170 GTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG 210
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
114-478 2.89e-11

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: 64.89  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYlaelremgcffamKVMDK--GMLIGRKKLVRA--------QTEREIL---GLLDHPFLPTL--- 177
Cdd:cd07852   9 YEILKKLGKGAYGIVW-------------KAIDKktGEVVALKKIFDAfrnatdaqRTFREIMflqELNDHPNIIKLlnv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 178 ---------YSHFEtekfsclLMEfcsgGDLH------ILRqkqpgkhfsELAARFYASEVLLALEYLHMMGVVYRDLKP 242
Cdd:cd07852  76 iraendkdiYLVFE-------YME----TDLHaviranILE---------DIHKQYIMYQLLKALKYLHSGGVIHRDLKP 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 243 ENVMVREDGHIMLSDFDLSlQSFvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakTE 322
Cdd:cd07852 136 SNILLNSDCRVKLADFGLA-RSL-------------------------------------------------------SQ 159
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 323 KAGSDSLPMLiaeptaarsMSFVGTHEYLAPEIIRGDGHGS-SVDWWTFGIFLYELLTGKTPFKGNG--NR-ETLFNVVG 398
Cdd:cd07852 160 LEEDDENPVL---------TDYVATRWYRAPEILLGSTRYTkGVDMWSVGCILGEMLLGKPLFPGTStlNQlEKIIEVIG 230
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 399 QP-------LKFPEGS-----------ISFA---------AKDLIRGLLTKDPKKRLgfkkGATEIKQHPF---FNNvnw 448
Cdd:cd07852 231 RPsaediesIQSPFAAtmleslppsrpKSLDelfpkaspdALDLLKKLLVFNPNKRL----TAEEALRHPYvaqFHN--- 303
                       410       420       430
                ....*....|....*....|....*....|
gi 15242554 449 alirSTTPPEIPKPIDLSILNETlKSSVQQ 478
Cdd:cd07852 304 ----PADEPSLPGPIVIPLDDNK-KLTVDE 328
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
120-258 3.42e-11

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 60.92  E-value: 3.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMDKgmligRKKLVRAQTEREILGLLD----HPFLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDD-----VNNEEGEDLESEMDILRRlkglELNIPKVLVTEDVDGPNILLMELVK 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 196 GGDLhilRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd13968  76 GGTL---IAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDF 135
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
114-258 3.55e-11

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: 63.98  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELR-EMGCFFAMKVMDKGMLIGRKKLVRAQtEREILGLLD---HPFLPTLYSHFETEKFSCL 189
Cdd:cd14052   2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLE-EVSILRELTldgHDNIVQLIDSWEYHGHLYI 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 190 LMEFCSGGDLHILRQKQpGKHFSELAARFYAS--EVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd14052  81 QTELCENGSLDVFLSEL-GLLGRLDEFRVWKIlvELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDF 150
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
118-445 3.65e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 64.40  E-value: 3.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  118 KKLGCGDIGSVYLAELREMGCFFAMKVMD----KGMLIGRKKLV-------RAQTEREILGLLDHPFLPTLYSHFETEKF 186
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKiieiSNDVTKDRQLVgmcgihfTTLRELKIMNEIKHENIMGLVDVYVEGDF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  187 SCLLMEFCSGGDLHILRQKqpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfv 266
Cdd:PTZ00024  95 INLVMDIMASDLKKVVDRK---IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGL------ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  267 sptliqstsqpschiASYCIQPPCIDPSCKLPvaciqpscfkprflNNKPRKAKTEKagsdslpmliaeptaarsmsfVG 346
Cdd:PTZ00024 166 ---------------ARRYGYPPYSDTLSKDE--------------TMQRREEMTSK---------------------VV 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  347 THEYLAPEIIRG-DGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP--LKFPEGS-------ISFAAK 413
Cdd:PTZ00024 196 TLWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLgriFELLGTPneDNWPQAKklplyteFTPRKP 275
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 15242554  414 ---------------DLIRGLLTKDPKKRLgfkkGATEIKQHPFFNN 445
Cdd:PTZ00024 276 kdlktifpnasddaiDLLQSLLKLNPLERI----SAKEALKHEYFKS 318
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
113-261 3.88e-11

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: 63.94  E-value: 3.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAEL-------REMgcfFAMKVMDKGMligrKKLVRAQTEREI--LGLLDHPFLPTL--YSHF 181
Cdd:cd05038   5 HLKFIKQLGEGHFGSVELCRYdplgdntGEQ---VAVKSLQPSG----EEQHMSDFKREIeiLRTLDHEYIVKYkgVCES 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ETEKFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFyASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05038  78 PGRRSLRLIMEYLPSGSLRDYLQRHRDQIDLKRLLLF-ASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLA 156
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
117-443 7.90e-11

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 63.53  E-value: 7.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSV---YLAELREMgcfFAMKVMDK---GMLIGRK-----KLVRAQTEREILGLLDhPFLPTLyshfETEK 185
Cdd:cd07878  20 LTPVGSGAYGSVcsaYDTRLRQK---VAVKKLSRpfqSLIHARRtyrelRLLKHMKHENVIGLLD-VFTPAT----SIEN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FS-CLLMEFCSGGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqs 264
Cdd:cd07878  92 FNeVYLVTNLMGADLNNIVKCQ---KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLA--- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGsdslpmliaeptaarsmsF 344
Cdd:cd07878 166 ----------------------------------------------------RQADDEMTG------------------Y 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP----LK-------------- 402
Cdd:cd07878 176 VATRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLkriMEVVGTPspevLKkisseharkyiqsl 255
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15242554 403 --FPEGSISFA-------AKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07878 256 phMPQQDLKKIfrganplAIDLLEKMLVLDSDKRI----SASEALAHPYF 301
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
114-442 8.19e-11

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: 62.47  E-value: 8.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDkgmLIGRKKLVRAQ---TEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMS---YSGKQSTEKWQdiiKEVKFLRQLRHPNTIEYKGCYLREHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptl 270
Cdd:cd06607  80 MEYCLGSASDIVEVHKKPLQEVEIAA--ICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADF------------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSLpmliaeptAARSMSFVGTHEY 350
Cdd:cd06607 146 ------------------------------------------------------GSASL--------VCPANSFVGTPYW 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGS---SVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV-GQPLKFPEGSISFAAKDLIRGLLTKDPKK 426
Cdd:cd06607 164 MAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAqNDSPTLSSGEWSDDFRNFVDSCLQKIPQD 243
                       330
                ....*....|....*.
gi 15242554 427 RlgfkKGATEIKQHPF 442
Cdd:cd06607 244 R----PSAEDLLKHPF 255
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-427 8.71e-11

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: 62.45  E-value: 8.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVrAQTEREILGLLDHPFLPTLYSHFETEK-FSCLLME 192
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKA-AEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliq 272
Cdd:cd08223  81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIA----------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 stsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTekagsdslpmliaeptaarsmsFVGTHEYLA 352
Cdd:cd08223 150 -------------------------------------RVLESSSDMATT----------------------LIGTPYYMS 170
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 353 PEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd08223 171 PELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQDPEKR 245
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
162-442 8.72e-11

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: 62.24  E-value: 8.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDL 240
Cdd:cd14110  49 EYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELlYNLAERNS---YSEAEVTDYLWQILSAVDYLHSRRILHLDL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 241 KPENVMVREDGHIMLSDFDlSLQSFvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnNKPRKAK 320
Cdd:cd14110 126 RSENMIITEKNLLKIVDLG-NAQPF------------------------------------------------NQGKVLM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 321 TEKAGSDSLPMliaeptaarsmsfvgtheylAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP 400
Cdd:cd14110 157 TDKKGDYVETM--------------------APELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGK 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15242554 401 LKF-------PEGSISFaakdlIRGLLTKDPKKRlgfkKGATEIKQHPF 442
Cdd:cd14110 217 VQLsrcyaglSGGAVNF-----LKSTLCAKPWGR----PTASECLQNPW 256
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
114-247 9.59e-11

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: 62.35  E-value: 9.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGML--IGRKKLVRAQTEREILGllDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd14138   7 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAgsVDEQNALREVYAHAVLG--QHSHVVRYYSAWAEDDHMLIQN 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 192 EFCSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV 247
Cdd:cd14138  85 EYCNGGSLAdaISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFI 142
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
137-378 9.94e-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: 62.28  E-value: 9.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 137 GCFF-AMKVMDK--GMLIGRKKLVR--AQTER------EILGLLDHP----FLPTLYShfetEKFSCLLMEFCSGGDLHI 201
Cdd:cd14221   4 GCFGqAIKVTHRetGEVMVMKELIRfdEETQRtflkevKVMRCLEHPnvlkFIGVLYK----DKRLNFITEYIKGGTLRG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 202 LrQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvSPTLIQSTSQPSchi 281
Cdd:cd14221  80 I-IKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGL------ARLMVDEKTQPE--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 282 asyciqppcidpscklpvaciqpscfKPRFLNNKPRKAKtekagsdslpmliaeptaarsMSFVGTHEYLAPEIIRGDGH 361
Cdd:cd14221 150 --------------------------GLRSLKKPDRKKR---------------------YTVVGNPYWMAPEMINGRSY 182
                       250
                ....*....|....*..
gi 15242554 362 GSSVDWWTFGIFLYELL 378
Cdd:cd14221 183 DEKVDVFSFGIVLCEII 199
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
118-261 1.03e-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: 61.98  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCF---FAMKVMDKG-MLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFsCLLMEF 193
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKSGKeveVAVKTLKQEhEKAGKKEFLR---EASVMAQLDHPCIVRLIGVCKGEPL-MLVMEL 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 194 CSGGDLHILRQKQPgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05060  77 APLGPLLKYLKKRR--EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMS 142
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
119-443 1.35e-10

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: 61.86  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMDKGMLiGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSC--LLMEFCSG 196
Cdd:cd13983   8 VLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKL-PKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEviFITELMTS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMG--VVYRDLKPENVMVR-EDGHIMLSDFDLSlqsfvsptliqs 273
Cdd:cd13983  87 GTLKQYLKRF--KRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLA------------ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakTEKAGSdslpmliaeptaaRSMSFVGTHEYLAP 353
Cdd:cd13983 153 -----------------------------------------------TLLRQS-------------FAKSVIGTPEFMAP 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIrGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKfPEgsiSFA------AKDLIRGLLTKdPKKR 427
Cdd:cd13983 173 EMY-EEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIK-PE---SLSkvkdpeLKDFIEKCLKP-PDER 246
                       330
                ....*....|....*.
gi 15242554 428 LgfkkGATEIKQHPFF 443
Cdd:cd13983 247 P----SARELLEHPFF 258
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
114-263 1.36e-10

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: 61.89  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLvraqtEREILGLLD-HPFLPTLYSHFETEKFSCLLME 192
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKM-----EVAVLKKLQgKPHFCRLIGCGRTERYNYIVMT 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 193 FCsGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPEN-VMVREDGH---IMLSDFDLSLQ 263
Cdd:cd14017  77 LL-GPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNfAIGRGPSDertVYILDFGLARQ 150
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
113-427 1.41e-10

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: 61.93  E-value: 1.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHF-----ETEKFS 187
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALK---KILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQivkeaGGKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDL--HILRQKQPGKHFSELAARFYASEVLLALEYLH---MMGVVYRDLKPENVMVREDGHIMLSDFDlsl 262
Cdd:cd13986  78 YLLLPYYKRGSLqdEIERRLVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDEPILMDLG--- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 263 qsfvsptliqSTSQpschiasyciqppcidpscklpvACIQpscfkprflnnkprkaktekAGSDSLPMLIAEPTAARSm 342
Cdd:cd13986 155 ----------SMNP-----------------------ARIE--------------------IEGRREALALQDWAAEHC- 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 343 sfvgTHEYLAPEIIRGDGHG---SSVDWWTFGIFLYELLTGKTPFK---GNGNRETLfNVVGQPLKFPEGS-ISFAAKDL 415
Cdd:cd13986 181 ----TMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFErifQKGDSLAL-AVLSGNYSFPDNSrYSEELHQL 255
                       330
                ....*....|..
gi 15242554 416 IRGLLTKDPKKR 427
Cdd:cd13986 256 VKSMLVVNPAER 267
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
350-443 1.47e-10

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: 61.29  E-value: 1.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIRGDGH--GSSVDWWTFGIFLYELLTGKTPFKGNGNrETLFNVV--GQpLKFPEGsISFAAKDLIRGLLTKDPK 425
Cdd:cd13976 152 YVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEP-ASLFAKIrrGQ-FAIPET-LSPRARCLIRSLLRREPS 228
                        90
                ....*....|....*...
gi 15242554 426 KRLgfkkGATEIKQHPFF 443
Cdd:cd13976 229 ERL----TAEDILLHPWL 242
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
162-385 2.73e-10

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: 60.77  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHilrQKQPGKHFSELAARFYASEVLLALEYLH---MMGVVYR 238
Cdd:cd14148  43 EARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALN---RALAGKKVPPHVLVNWAVQIARGMNYLHneaIVPIIHR 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 239 DLKPENVMVREDghimLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpSCKLpvaciqpscfkprflnnkprk 318
Cdd:cd14148 120 DLKSSNILILEP----IENDDLS--------------------------------GKTL--------------------- 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 319 aKTEKAGsdslpmLIAEPTAARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFK 385
Cdd:cd14148 143 -KITDFG------LAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR 202
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
162-443 2.86e-10

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: 61.13  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREIlGLL----DHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFYA--SEVLLALEYLHMMGV 235
Cdd:cd13982  42 DREV-QLLresdEHPNVIRYFCTEKDRQFLYIALELCAASLQDLVESPRESKLFLRPGLEPVRllRQIASGLAHLHSLNI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 236 VYRDLKPENVMV-----REDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpr 310
Cdd:cd13982 121 VHRDLKPQNILIstpnaHGNVRAMISDFGLC------------------------------------------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 311 flnnkprkaKTEKAGSDSLpmliaeptaaRSMSFV-GTHEYLAPEIIRGDGHGS---SVDWWTFG-IFLYELLTGKTPFK 385
Cdd:cd13982 152 ---------KKLDVGRSSF----------SRRSGVaGTSGWIAPEMLSGSTKRRqtrAVDIFSLGcVFYYVLSGGSHPFG 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 386 GNGNRET--LFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd13982 213 DKLEREAniLKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKR----PSAEEVLNHPFF 268
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
108-393 2.97e-10

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: 61.18  E-value: 2.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 108 DLGLGHFRLLKKLGCGDIGSVYLAELREMGcffamkvMDKGMLIGRKKL---------VRAQTEREILGLLDHPFLPTLY 178
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIYKGHLYLPG-------MDHAQLVAIKTLkdynnpqqwNEFQQEASLMTELHHPNIVCLL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 179 SHFETEKFSCLLMEFCSGGDLH---ILRQ---------KQPGKHFSELAARFY---ASEVLLALEYLHMMGVVYRDLKPE 243
Cdd:cd05090  74 GVVTQEQPVCMLFEFMNQGDLHeflIMRSphsdvgcssDEDGTVKSSLDHGDFlhiAIQIAAGMEYLSSHFFVHKDLAAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 244 NVMVREDGHIMLSDFDLSLQSFVSPTliqstsqpschiasYCIQPPCIdpsckLPVaciqpscfkprflnnkprkaktek 323
Cdd:cd05090 154 NILVGEQLHVKISDLGLSREIYSSDY--------------YRVQNKSL-----LPI------------------------ 190
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 324 agsdslpmliaeptaarsmsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL 393
Cdd:cd05090 191 -------------------------RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVI 236
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
102-443 3.31e-10

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: 61.43  E-value: 3.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 102 KCSKNEDLGlGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmligrkklVR--------AQTEREILGLL---- 169
Cdd:cd14134   3 IYKPGDLLT-NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKI------------IRnvekyreaAKIEIDVLETLaekd 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 170 --DHPFLPTLYSHFETEKFSCLLMEFCsGGDLH-ILRQKQ----PGKHFselaaRFYASEVLLALEYLHMMGVVYRDLKP 242
Cdd:cd14134  70 pnGKSHCVQLRDWFDYRGHMCIVFELL-GPSLYdFLKKNNygpfPLEHV-----QHIAKQLLEAVAFLHDLKLTHTDLKP 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 243 ENvmvredghIMLSDFDLSLQSFVSptliqsTSQPSCHIASYCIQppCIDPSCklpvaciqpSCFKPRFlnnkprkakte 322
Cdd:cd14134 144 EN--------ILLVDSDYVKVYNPK------KKRQIRVPKSTDIK--LIDFGS---------ATFDDEY----------- 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 323 kagsDSlpmliaeptaarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL--------- 393
Cdd:cd14134 188 ----HS--------------SIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLammerilgp 249
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 394 ---------------FNVVGQPLKFPEGSISFAAK----------------------DLIRGLLTKDPKKRLgfkkGATE 436
Cdd:cd14134 250 lpkrmirrakkgakyFYFYHGRLDWPEGSSSGRSIkrvckplkrlmllvdpehrllfDLIRKMLEYDPSKRI----TAKE 325

                ....*..
gi 15242554 437 IKQHPFF 443
Cdd:cd14134 326 ALKHPFF 332
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
114-443 3.32e-10

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: 61.23  E-value: 3.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKV--MDK---GMLIgrkklvraQTEREILGLLD--HPFLPTLY-----SHF 181
Cdd:cd07845   9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKvrMDNerdGIPI--------SSLREITLLLNlrHPNIVELKevvvgKHL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ETeKFscLLMEFCSGgDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07845  81 DS-IF--LVMEYCEQ-DLASLLDNMPTP-FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 lqsfvsptliqSTSQPSCHiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslPMliaEPTaars 341
Cdd:cd07845 156 -----------RTYGLPAK-------------------------------------------------PM---TPK---- 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 342 msfVGTHEYLAPEIIRG-DGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL--------------------------F 394
Cdd:cd07845 169 ---VVTLWYRAPELLLGcTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLdliiqllgtpnesiwpgfsdlplvgkF 245
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242554 395 NVVGQP---LKFPEGSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07845 246 TLPKQPynnLKHKFPWLSEAGLRLLNFLLMYDPKKRA----TAEEALESSYF 293
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
139-378 3.80e-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: 60.73  E-value: 3.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 139 FF--AMKVMDK--GMLIGRKKLVRAQ--------TEREILGLLDHP----FLPTLYShfetEKFSCLLMEFCSGGDLH-I 201
Cdd:cd14222   5 FFgqAIKVTHKatGKVMVMKELIRCDeetqktflTEVKVMRSLDHPnvlkFIGVLYK----DKRLNLLTEFIEGGTLKdF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 202 LRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspTLIQSTSqpschi 281
Cdd:cd14222  81 LRADDP---FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLS-------RLIVEEK------ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 282 asycIQPPCIDPSCklpvaciqpscfKPRFLNNKPRKAKtekagsdslpmliaeptaarsMSFVGTHEYLAPEIIRGDGH 361
Cdd:cd14222 145 ----KKPPPDKPTT------------KKRTLRKNDRKKR---------------------YTVVGNPYWMAPEMLNGKSY 187
                       250
                ....*....|....*..
gi 15242554 362 GSSVDWWTFGIFLYELL 378
Cdd:cd14222 188 DEKVDIFSFGIVLCEII 204
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
120-432 3.89e-10

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: 60.48  E-value: 3.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELRemGCFFAMKVM----DKGMLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd14061   2 IGVGGFGKVYRGIWR--GEEVAVKAArqdpDEDISVTLENVRQ---EARLFWMLRHPNIIALRGVCLQPPNLCLVMEYAR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDLHilrqkqpgKHfseLAARFYASEVLL--------ALEYLH---MMGVVYRDLKPENVMVRED-GHIMLSDFDLSLQ 263
Cdd:cd14061  77 GGALN--------RV---LAGRKIPPHVLVdwaiqiarGMNYLHneaPVPIIHRDLKSSNILILEAiENEDLENKTLKIT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 SFvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGsdslpmLIAEPTAARSMS 343
Cdd:cd14061 146 DF-----------------------------------------------------------G------LAREWHKTTRMS 160
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 FVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISFAA-KDLIRGLLTK 422
Cdd:cd14061 161 AAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTLPIPSTCPEPfAQLMKDCWQP 240
                       330
                ....*....|
gi 15242554 423 DPKKRLGFKK 432
Cdd:cd14061 241 DPHDRPSFAD 250
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
117-459 4.26e-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: 60.82  E-value: 4.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd06633  26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCLG 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDLHILR-QKQPGKHFsELAARFYASevLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptliqsts 275
Cdd:cd06633 106 SASDLLEvHKKPLQEV-EIAAITHGA--LQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADF----------------- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSlpmlIAEPtaarSMSFVGTHEYLAPEI 355
Cdd:cd06633 166 -------------------------------------------------GSAS----IASP----ANSFVGTPYWMAPEV 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGS---SVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVV---GQPLKFPEGSISFaaKDLIRGLLTKDPKKRLg 429
Cdd:cd06633 189 ILAMDEGQydgKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAqndSPTLQSNEWTDSF--RGFVDYCLQKIPQERP- 265
                       330       340       350
                ....*....|....*....|....*....|
gi 15242554 430 fkkGATEIKQHPFfnnvnwalIRSTTPPEI 459
Cdd:cd06633 266 ---SSAELLRHDF--------VRRERPPRV 284
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
113-444 4.57e-10

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: 60.88  E-value: 4.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAEL--REMGCFFAMK----VMDKGMLIGR-----KKLVRAQTEREILGL--LDHPF---LPT 176
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNaeTSEEETVAIKkitnVFSKKILAKRalrelKLLRHFRGHKNITCLydMDIVFpgnFNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 177 LYSHFEtekfsclLMEFcsggDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIML 255
Cdd:cd07857  81 LYLYEE-------LMEA----DLHqIIRSGQP---LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 256 SDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpSCFKPRFLNNKPrkaktekagsdslpmLIAE 335
Cdd:cd07857 147 CDFGLA-------------------------------------------RGFSENPGENAG---------------FMTE 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 336 ptaarsmsFVGTHEYLAPEI-IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNG---------------NRETLFNV--- 396
Cdd:cd07857 169 --------YVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDyvdqlnqilqvlgtpDEETLSRIgsp 240
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 397 --------VGQPLKFPEGSI----SFAAKDLIRGLLTKDPKKRLGFKkgatEIKQHPFFN 444
Cdd:cd07857 241 kaqnyirsLPNIPKKPFESIfpnaNPLALDLLEKLLAFDPTKRISVE----EALEHPYLA 296
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
346-443 4.73e-10

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: 60.05  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDGH--GSSVDWWTFGIFLYELLTGKTPFKgNGNRETLFNVV--GQpLKFPEgSISFAAKDLIRGLLT 421
Cdd:cd14022 148 GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFH-DIEPSSLFSKIrrGQ-FNIPE-TLSPKAKCLIRSILR 224
                        90       100
                ....*....|....*....|..
gi 15242554 422 KDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd14022 225 REPSERL----TSQEILDHPWF 242
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
198-473 5.37e-10

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: 60.85  E-value: 5.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsq 276
Cdd:cd07858  94 DLHqIIRSSQT---LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLA--------------- 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 277 pschiasyciqppcidpscklpvaciQPSCFKPRFLnnkprkakTEkagsdslpmliaeptaarsmsFVGTHEYLAPE-I 355
Cdd:cd07858 156 --------------------------RTTSEKGDFM--------TE---------------------YVVTRWYRAPElL 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLTGKTPFKG----------------------------NGNR--ETLFNVVGQPL--KF 403
Cdd:cd07858 181 LNCSEYTTAIDVWSVGCIFAELLGRKPLFPGkdyvhqlklitellgspseedlgfirneKARRyiRSLPYTPRQSFarLF 260
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 404 PEgsISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFNnvnwALIRSTTPPEIPKPIDLSILNETLK 473
Cdd:cd07858 261 PH--ANPLAIDLLEKMLVFDPSKRI----TVEEALAHPYLA----SLHDPSDEPVCQTPFSFDFEEDALT 320
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
114-247 5.95e-10

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: 60.11  E-value: 5.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmliGRKKLVRAQTEREILG-------LLDHPFLPTLYSHFETEKF 186
Cdd:cd14051   2 FHEVEKIGSGEFGSVYKCINRLDGCVYAIKK-------SKKPVAGSVDEQNALNevyahavLGKHPHVVRYYSAWAEDDH 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 187 SCLLMEFCSGGDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV 247
Cdd:cd14051  75 MIIQNEYCNGGSLAdaISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFI 137
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
111-440 7.53e-10

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: 59.89  E-value: 7.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdkGMLIGRKKLVRAQTEREI--LGLLDHPFL-----------PTL 177
Cdd:cd14048   5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVK----RIRLPNNELAREKVLREVraLAKLDHPGIvryfnawlerpPEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 178 YSHFETEKFSCLLMEFCSGGDLhilRQKQPGKHFSELAARFYASEVLL----ALEYLHMMGVVYRDLKPENVMVREDGHI 253
Cdd:cd14048  81 WQEKMDEVYLYIQMQLCRKENL---KDWMNRRCTMESRELFVCLNIFKqiasAVEYLHSKGLIHRDLKPSNVFFSLDDVV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 254 MLSDFDlslqsfvsptLIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSLPMLI 333
Cdd:cd14048 158 KVGDFG----------LVTAMDQ------------------------------------------------GEPEQTVLT 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 334 AEPTAARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLtgkTPFKGNGNRETLFNVVgQPLKFPegsISFAAK 413
Cdd:cd14048 180 PMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQMERIRTLTDV-RKLKFP---ALFTNK 252
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242554 414 -----DLIRGLLTKDPKKRlgfkKGATEIKQH 440
Cdd:cd14048 253 ypeerDMVQQMLSPSPSER----PEAHEVIEH 280
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
114-427 8.65e-10

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: 60.07  E-value: 8.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligrKKLVRAQTERE--ILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd06650   7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEI----KPAIRNQIIRElqVLHECNSPYIVGFYGAFYSDGEISICM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDL-HILrqKQPGKHFSELAARFYASeVLLALEYL-HMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvspt 269
Cdd:cd06650  83 EHMDGGSLdQVL--KKAGRIPEQILGKVSIA-VIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQ------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 LIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmSFVGTHE 349
Cdd:cd06650 154 LIDSMAN------------------------------------------------------------------SFVGTRS 167
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNREtLFNVVGQPLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd06650 168 YMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKE-LELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR 244
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
190-443 1.07e-09

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: 60.07  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEfcsgGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd07855  91 LME----SDLHhIIHSDQP---LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMA------- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAK---TEkagsdslpmliaeptaarsmsFV 345
Cdd:cd07855 157 -----------------------------------------RGLCTSPEEHKyfmTE---------------------YV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRG-DGHGSSVDWWTFGIFLYELLTGKTPFKGN---GNRETLFNVVGQPlkfPEGSI------------- 408
Cdd:cd07855 175 ATRWYRAPELMLSlPEYTQAIDMWSVGCIFAEMLGRRQLFPGKnyvHQLQLILTVLGTP---SQAVInaigadrvrryiq 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242554 409 SFAAK-----------------DLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07855 252 NLPNKqpvpwetlypkadqqalDLLSQMLRFDPSERI----TVAEALQHPFL 299
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
114-443 1.14e-09

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: 60.05  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGM--LIGRKK------LVRAQTEREILGLLDhPFLP-TLYSHFETE 184
Cdd:cd07877  19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFqsIIHAKRtyrelrLLKHMKHENVIGLLD-VFTPaRSLEEFNDV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMefcsGGDLH-ILR-QKQPGKHfselaARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLsl 262
Cdd:cd07877  98 YLVTHLM----GADLNnIVKcQKLTDDH-----VQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGL-- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 263 qsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliAEPTAARSM 342
Cdd:cd07877 167 -----------------------------------------------------------------------ARHTDDEMT 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 343 SFVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP-----LKFPEGS------ 407
Cdd:cd07877 176 GYVATRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLkliLRLVGTPgaellKKISSESarnyiq 255
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242554 408 -------ISFA---------AKDLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07877 256 sltqmpkMNFAnvfiganplAVDLLEKMLVLDSDKRI----TAAQALAHAYF 303
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
120-443 1.31e-09

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: 58.98  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFFAMKVMD--KGMLIGRKKLVRAQTER-EILGLLDHP-FLPTLYSHFETEKFScLLMEFCS 195
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEVVEAIREEiRMMARLNHPnIVRMLGATQHKSHFN-IFVEWMA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIM-LSDFDLSLQsfvsptliqs 273
Cdd:cd06630  87 GGSVaSLLSKYGA---FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLrIADFGAAAR---------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvaciqpscfkprfLNNKPRKAKtEKAGSdslpmliaeptaarsmsFVGTHEYLAP 353
Cdd:cd06630 154 --------------------------------------LASKGTGAG-EFQGQ-----------------LLGTIAFMAP 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVG--QPLKFPEgSISFAAKDLIRGLLTKDPKKRl 428
Cdd:cd06630 178 EVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLaliFKIASatTPPPIPE-HLSPGLRDVTLRCLELQPEDR- 255
                       330
                ....*....|....*
gi 15242554 429 gfkKGATEIKQHPFF 443
Cdd:cd06630 256 ---PPARELLKHPVF 267
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
120-384 1.42e-09

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: 58.82  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREmGCFFAMKVMdkGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDL 199
Cdd:cd14066   1 IGSGGFGTVYKGVLEN-GTVVAVKRL--NEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 200 -HILRQKQPGKHFSeLAARF-YASEVLLALEYLHMMG---VVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqst 274
Cdd:cd14066  78 eDRLHCHKGSPPLP-WPQRLkIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLA------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTEKAgsdslpmliaeptaarsmsfVGTHEYLAPE 354
Cdd:cd14066 144 -----------------------------------RLIPPSESVSKTSAV--------------------KGTIGYLAPE 168
                       250       260       270
                ....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLTGKTPF 384
Cdd:cd14066 169 YIRTGRVSTKSDVYSFGVVLLELLTGKPAV 198
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
114-443 1.44e-09

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: 58.97  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmliGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd07846   3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLES---EDDKMVKKIAMREIkmLKQLRHENLVNLIEVFRRKKRWYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQPGKHFSELaaRFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd07846  80 EFVDHTVLDDLEKYPNGLDESRV--RKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA---------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNkPRKAKTEkagsdslpmliaeptaarsmsFVGTHEYL 351
Cdd:cd07846 148 --------------------------------------RTLAA-PGEVYTD---------------------YVATRWYR 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 352 APEIIRGD-GHGSSVDWWTFGIFLYELLTGKTPFKGN-------------GN----RETLF--NVVGQPLKFPE------ 405
Cdd:cd07846 168 APELLVGDtKYGKAVDVWAVGCLVTEMLTGEPLFPGDsdidqlyhiikclGNliprHQELFqkNPLFAGVRLPEvkevep 247
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15242554 406 -----GSISFAAKDLIRGLLTKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd07846 248 lerryPKLSGVVIDLAKKCLHIDPDKR----PSCSELLHHEFF 286
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
111-261 1.98e-09

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: 58.54  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAEL-----REMGCFFAMKVMDKGMLIGRKKLVRaqTEREILGLLDHPFLPTLYSHFETEK 185
Cdd:cd05048   4 LSAVRFLEELGEGAFGKVYKGELlgpssEESAISVAIKTLKENASPKTQQDFR--REAELMSDLQHPNIVCLLGVCTKEQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLMEFCSGGDLH-ILRQKQP-----------GKHFSELAARFY--ASEVLLALEYLHMMGVVYRDLKPENVMVREDG 251
Cdd:cd05048  82 PQCMLFEYMAHGDLHeFLVRHSPhsdvgvssdddGTASSLDQSDFLhiAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGL 161
                       170
                ....*....|
gi 15242554 252 HIMLSDFDLS 261
Cdd:cd05048 162 TVKISDFGLS 171
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
114-443 2.45e-09

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 58.08  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKgmLIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHFE-TEKFSCLL 190
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDK--SGGPEEFIQRFLPRElqIVERLDHKNIIHVYEMLEsADGKIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDlhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVmvredghiMLSDFDLSLQSFvsptl 270
Cdd:cd14163  80 MELAEDGD--VFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENA--------LLQGFTLKLTDF----- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 271 iqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKtekagsdslpmliaeptaARSMSFVGTHEY 350
Cdd:cd14163 145 ---------------------------------------GFAKQLPKGGR------------------ELSQTFCGSTAY 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRGDGHGSSV-DWWTFGIFLYELLTGKTPFKGNGNRETLFNvVGQPLKFPEG-SISFAAKDLIRGLLTKDpkkrL 428
Cdd:cd14163 168 AAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQ-QQKGVSLPGHlGVSRTCQDLLKRLLEPD----M 242
                       330
                ....*....|....*
gi 15242554 429 GFKKGATEIKQHPFF 443
Cdd:cd14163 243 VLRPSIEEVSWHPWL 257
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
114-280 2.57e-09

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: 58.53  E-value: 2.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdkgmLIGRKKL---VRAQTEREILGLLDHP----------FLPTLYSH 180
Cdd:cd07865  14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKV----LMENEKEgfpITALREIKILQLLKHEnvvnlieicrTKATPYNR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 181 FETEKFscLLMEFCSGgDLHILRQkQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:cd07865  90 YKGSIY--LVFEFCEH-DLAGLLS-NKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGL 165
                       170       180
                ....*....|....*....|
gi 15242554 261 SlQSFVSPTliqsTSQPSCH 280
Cdd:cd07865 166 A-RAFSLAK----NSQPNRY 180
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
116-267 2.93e-09

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: 58.46  E-value: 2.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLG--CGDIGSVYLAELREMGCFFAMK-----VMDKgmligrKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd08216   2 LLYEIGkcFKGGGVVHLAKHKPTNTLVAVKkinleSDSK------EDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLY 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 189 LLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlSLQSFVS 267
Cdd:cd08216  76 VVTPLMAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLR-YAYSMVK 153
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
114-427 2.97e-09

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: 57.73  E-value: 2.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVM-----DKGMLIGRKKLVRAQTEReilglldHPFLPTLYSHFETEKFsC 188
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIklepgDDFSLIQQEIFMVKECKH-------CNIVAYFGSYLSREKL-W 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvs 267
Cdd:cd06646  83 ICMEYCGGGSLQdIYHVTGP---LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVA------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 ptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEKagsdslpmliaepTAARSMSFVGT 347
Cdd:cd06646 154 ---------------------------------------------------AKITA-------------TIAKRKSFIGT 169
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 HEYLAPEII---RGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG---QPLKFPEGS-ISFAAKDLIRGLL 420
Cdd:cd06646 170 PYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKsnfQPPKLKDKTkWSSTFHNFVKISL 249

                ....*..
gi 15242554 421 TKDPKKR 427
Cdd:cd06646 250 TKNPKKR 256
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
114-436 3.37e-09

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: 58.15  E-value: 3.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLA-ELREMGcFFAMKV--MDKGMLIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHF--ETEKF 186
Cdd:cd14041   8 YLLLHLLGRGGFSEVYKAfDLTEQR-YVAVKIhqLNKNWRDEKKENYHKHACREyrIHKELDHPRIVKLYDYFslDTDSF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 sCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMG--VVYRDLKPENVMVRED---GHIMLSDFDLS 261
Cdd:cd14041  87 -CTVLEYCEGNDLDFYLKQH--KLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGtacGEIKITDFGLS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 262 L----QSFVSPTLIQSTSQPSchiASYCIQPpcidpscklpvaciqPSCFkprflnnkprkaktekagsdslpMLIAEPt 337
Cdd:cd14041 164 KimddDSYNSVDGMELTSQGA---GTYWYLP---------------PECF-----------------------VVGKEP- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsfvgtheylaPEIirgdghGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFN----VVGQPLKF-PEGSISFAA 412
Cdd:cd14041 202 ---------------PKI------SNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQentiLKATEVQFpPKPVVTPEA 260
                       330       340
                ....*....|....*....|....
gi 15242554 413 KDLIRGLLTKDPKKRLGFKKGATE 436
Cdd:cd14041 261 KAFIRRCLAYRKEDRIDVQQLACD 284
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
114-260 5.18e-09

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: 56.93  E-value: 5.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdKGMLIGRKKLVRAQTE---REILGllDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRS-RSRFRGEKDRKRKLEEverHEKLG--EHPNCVRFIKAWEEKGILYIQ 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:cd14050  80 TELCDTSLQQYCEETH---SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGL 146
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
117-442 5.86e-09

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: 57.17  E-value: 5.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd06622   6 LDELGKGNYGSVYKVLHRPTGVTMAMKEIR--LELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL-HILRQKQPGKHFSELAARFYASEVLLALEYL-HMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfVSPTLIQST 274
Cdd:cd06622  84 GSLdKLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFG------VSGNLVASL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkAKTEkagsdslpmliaeptaarsmsfVGTHEYLAPE 354
Cdd:cd06622 158 --------------------------------------------AKTN----------------------IGCQSYMAPE 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDG------HGSSVDWWTFGIFLYELLTGKTPFKgngnRETLFNVVGQ--------PLKFPEGsISFAAKDLIRGLL 420
Cdd:cd06622 172 RIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYP----PETYANIFAQlsaivdgdPPTLPSG-YSDDAQDFVAKCL 246
                       330       340
                ....*....|....*....|..
gi 15242554 421 TKDPKKRLGFkkgaTEIKQHPF 442
Cdd:cd06622 247 NKIPNRRPTY----AQLLEHPW 264
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
114-443 6.87e-09

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: 57.04  E-value: 6.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMK---KIRLESEEEGVPSTAIREIslLKELQHPNIVCLEDVLMQENRLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFvsptli 271
Cdd:cd07861  79 EFLSMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLA-RAF------ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscKLPVAciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfVGTHE-- 349
Cdd:cd07861 152 ------------------------GIPVR--------------------------------------------VYTHEvv 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 ---YLAPEIIRGDGHGSS-VDWWTFGIFLYELLTGKTPFKGNGNRETLF---NVVGQPLK---------------FP--- 404
Cdd:cd07861 164 tlwYRAPEVLLGSPRYSTpVDIWSIGTIFAEMATKKPLFHGDSEIDQLFrifRILGTPTEdiwpgvtslpdykntFPkwk 243
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 405 EGSISFAAK-------DLIRGLLTKDPKKRLGFKKGATeikqHPFF 443
Cdd:cd07861 244 KGSLRTAVKnldedglDLLEKMLIYDPAKRISAKKALV----HPYF 285
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
217-443 6.90e-09

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: 56.85  E-value: 6.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 217 RFYASEV-------LLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsFVSPtliqstsqpschiasyciqpp 289
Cdd:cd07843 102 PFLQSEVkclmlqlLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE-YGSP--------------------- 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 290 cidpscklpvaciqpscfkprflnnkpRKAKTEKagsdslpmliaeptaarsmsfVGTHEYLAPEIIRGDGH-GSSVDWW 368
Cdd:cd07843 160 ---------------------------LKPYTQL---------------------VVTLWYRAPELLLGAKEySTAIDMW 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 369 TFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP----------------------------LKFPEGSISFAAKDLIR 417
Cdd:cd07843 192 SVGCIFAELLTKKPLFPGKSEIDQLnkiFKLLGTPtekiwpgfselpgakkktftkypynqlrKKFPALSLSDNGFDLLN 271
                       250       260
                ....*....|....*....|....*.
gi 15242554 418 GLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07843 272 RLLTYDPAKRI----SAEDALKHPYF 293
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
120-404 7.04e-09

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: 56.50  E-value: 7.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELRemGCFFAMKVMDK--GMLIGRKKLVraqtereILGLLDHPFLPTLYSHFETEKFscLLMEFCSGG 197
Cdd:cd14068   2 LGDGGFGSVYRAVYR--GEDVAVKIFNKhtSFRLLRQELV-------VLSHLHHPSLVALLAAGTAPRM--LVMELAPKG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 198 DLHILRQKQPGKHFSELAARFyASEVLLALEYLHMMGVVYRDLKPENVMVredghimlsdFDLslqsfvsptliQSTSQP 277
Cdd:cd14068  71 SLDALLQQDNASLTRTLQHRI-ALHVADGLRYLHSAMIIYRDLKPHNVLL----------FTL-----------YPNCAI 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 SCHIASYCIQPPCidpsCKLPvacIQPSCfkprflnnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAPEIIR 357
Cdd:cd14068 129 IAKIADYGIAQYC----CRMG---IKTSE---------------------------------------GTPGFRAPEVAR 162
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15242554 358 GD-GHGSSVDWWTFGIFLYELLTGktpfkgnGNRetlfnvVGQPLKFP 404
Cdd:cd14068 163 GNvIYNQQADVYSFGLLLYDILTC-------GER------IVEGLKFP 197
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
189-407 7.50e-09

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: 56.63  E-value: 7.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHILRQKQPG----KHFSELAARF-------YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSD 257
Cdd:cd14062  53 LFMGYMTKPQLAIVTQWCEGsslyKHLHVLETKFemlqlidIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGD 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSDSLPmliaEPT 337
Cdd:cd14062 133 FGLA--------------------------------------------------------TVKTRWSGSQQFE----QPT 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 338 aarsmsfvGTHEYLAPEIIR-GDGHGSSV--DWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS 407
Cdd:cd14062 153 --------GSILWMAPEVIRmQDENPYSFqsDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYLRPDLS 217
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
108-261 8.60e-09

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: 57.10  E-value: 8.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 108 DLGlGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREILGLLDHPFLPTLY------SHF 181
Cdd:cd07854   2 DLG-SRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVK---KIVLTDPQSVKHALREIKIIRRLDHDNIVKVYevlgpsGSD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 182 ETEKFS--------CLLMEfCSGGDLHILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVR-EDGH 252
Cdd:cd07854  78 LTEDVGsltelnsvYIVQE-YMETDLANVLEQGP---LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLV 153

                ....*....
gi 15242554 253 IMLSDFDLS 261
Cdd:cd07854 154 LKIGDFGLA 162
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
112-442 1.04e-08

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: 56.54  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklvrAQTEREILGLL-DHPFLPTLYSHF-ETEKFS-- 187
Cdd:cd06639  22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEE----IEAEYNILRSLpNHPNVVKFYGMFyKADQYVgg 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 --CLLMEFCSGGDLHILRQK--QPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQ 263
Cdd:cd06639  98 qlWLVLELCNGGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 sFVSPTLIQSTSqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsms 343
Cdd:cd06639 178 -LTSARLRRNTS-------------------------------------------------------------------- 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 fVGTHEYLAPEIIRGD-----GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEG-SISFAakD 414
Cdd:cd06639 189 -VGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPpptLLNPEKwCRGFS--H 265
                       330       340
                ....*....|....*....|....*...
gi 15242554 415 LIRGLLTKDPKKRlgfkKGATEIKQHPF 442
Cdd:cd06639 266 FISQCLIKDFEKR----PSVTHLLEHPF 289
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
152-442 1.07e-08

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: 56.21  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 152 GRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFS------CLLMEFCSGGDLHILrqKQPGKHFSELAARFYASEVLL 225
Cdd:cd14012  38 GKKQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRsdgwkvYLLTEYAPGGSLSEL--LDSVGSVPLDTARRWTLQLLE 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 226 ALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLslqsfvSPTLIQSTSQPSchiasyciqppcidpscklpvaci 302
Cdd:cd14012 116 ALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSL------GKTLLDMCSRGS------------------------ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 303 qpscfkprflnnkprkaktekagsdslpMLIAEPTAarsmsfvgtheYLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGK 381
Cdd:cd14012 166 ----------------------------LDEFKQTY-----------WLPPELAQGSKsPTRKTDVWDLGLLFLQMLFGL 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 382 TPFKgngnRETLFNVVGQPLKFPEgsisfAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd14012 207 DVLE----KYTSPNPVLVSLDLSA-----SLQDFLSKCLSLDPKKRP----TALELLPHEF 254
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
114-261 1.38e-08

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: 56.22  E-value: 1.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLA-ELREMGcFFAMKV--MDKGMLIGRKKLVRAQTERE--ILGLLDHPFLPTLYSHF--ETEKF 186
Cdd:cd14040   8 YLLLHLLGRGGFSEVYKAfDLYEQR-YAAVKIhqLNKSWRDEKKENYHKHACREyrIHKELDHPRIVKLYDYFslDTDTF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 sCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMG--VVYRDLKPENVMVRED---GHIMLSDFDLS 261
Cdd:cd14040  87 -CTVLEYCEGNDLDFYLKQH--KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLS 163
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
117-443 1.47e-08

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: 56.16  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd07873   7 LDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAP--CTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GdlhiLRQ--KQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqst 274
Cdd:cd07873  85 D----LKQylDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTekagsdslpmliaEPTAARSMSFVgTHEYLAPE 354
Cdd:cd07873 148 -------------------------------------------RAKS-------------IPTKTYSNEVV-TLWYRPPD 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK--------------------FPEGSISF 410
Cdd:cd07873 171 ILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLhfiFRILGTPTEetwpgilsneefksynypkyRADALHNH 250
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15242554 411 AAK------DLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07873 251 APRldsdgaDLLSKLLQFEGRKRI----SAEEAMKHPYF 285
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
114-443 1.96e-08

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: 55.37  E-value: 1.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALK---KIRLETEDEGVPSTAIREIslLKELNHPNIVRLLDVVHSENKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlQSFVSPtli 271
Cdd:cd07835  78 EFLDL-DLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLA-RAFGVP--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschIASYciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgTHE-- 349
Cdd:cd07835 153 ---------VRTY--------------------------------------------------------------THEvv 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 ---YLAPEIIRGDGHGS-SVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP--------LKFPEGSISF---- 410
Cdd:cd07835 162 tlwYRAPEILLGSKHYStPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLfriFRTLGTPdedvwpgvTSLPDYKPTFpkwa 241
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 411 -------------AAKDLIRGLLTKDPKKRLGFKKGAteikQHPFF 443
Cdd:cd07835 242 rqdlskvvpsldeDGLDLLSQMLVYDPAKRISAKAAL----QHPYF 283
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
113-432 2.09e-08

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: 55.05  E-value: 2.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELRemGCFFAMKVMdkgmligRKKLVRAQ---TEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd05039   7 DLKLGELIGKGEFGDVMLGDYR--GQKVAVKCL-------KDDSTAAQaflAEASVMTTLRHPNLVQLLGVVLEGNGLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDL-HILRQKqpGKHFSELAARF-YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVS 267
Cdd:cd05039  78 VTEYMAKGSLvDYLRSR--GRAVITRKDQLgFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 268 PTliqstsqpschiasyciqppcidpSCKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgt 347
Cdd:cd05039 156 QD------------------------GGKLPI------------------------------------------------ 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 348 hEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKgngnRETLFNVV-----GQPLKFPEGSISFAAKdLIRGLLT 421
Cdd:cd05039 164 -KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYP----RIPLKDVVphvekGYRMEAPEGCPPEVYK-VMKNCWE 237
                       330
                ....*....|.
gi 15242554 422 KDPKKRLGFKK 432
Cdd:cd05039 238 LDPAKRPTFKQ 248
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
226-443 2.35e-08

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: 55.45  E-value: 2.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 226 ALEYL-HMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQsfvsptLIQSTsqpschiasyciqppcidpscklpvaciqp 304
Cdd:cd06616 121 ALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQ------LVDSI------------------------------ 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 305 scfkprflnnkprkAKTEKAGsdslpmliAEPtaarsmsfvgtheYLAPEII----RGDGHGSSVDWWTFGIFLYELLTG 380
Cdd:cd06616 165 --------------AKTRDAG--------CRP-------------YMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATG 209
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 381 KTPF-KGNGNRETLFNVV-GQPLKFPEG-----SISFaaKDLIRGLLTKDPKKRLGFKkgatEIKQHPFF 443
Cdd:cd06616 210 KFPYpKWNSVFDQLTQVVkGDPPILSNSeerefSPSF--VNFVNLCLIKDESKRPKYK----ELLKHPFI 273
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
120-265 2.62e-08

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: 55.20  E-value: 2.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGcFFAMKVMDKG-MLIGR-KKLVRaqtEREILGLLDHPFLPTLYSH-FETEKFScLLMEFCSG 196
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTGpNCIEHnEALLE---EGKMMNRLRHSRVVKLLGViLEEGKYS-LVMEYMEK 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 197 GDLHILRQKQPGKhfSELAARFYAsEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSdfDLSLQSF 265
Cdd:cd14027  76 GNLMHVLKKVSVP--LSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIA--DLGLASF 139
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
117-400 2.84e-08

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: 55.02  E-value: 2.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVM----DKGmligrkKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLME 192
Cdd:cd07871  10 LDKLGEGTYATVFKGRSKLTENLVALKEIrlehEEG------APCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILrqKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFVsPTLIQ 272
Cdd:cd07871  84 YLDSDLKQYL--DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSV-PTKTY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 STsqpscHIASYCIQPPCIdpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsFVGTHEYLA 352
Cdd:cd07871 161 SN-----EVVTLWYRPPDV----------------------------------------------------LLGSTEYST 183
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 353 PeiirgdghgssVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP 400
Cdd:cd07871 184 P-----------IDMWGVGCILYEMATGRPMFPGSTVKEELhliFRLLGTP 223
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
114-268 3.55e-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: 55.06  E-value: 3.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06635  27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 194 CSGGDLHILR-QKQPGKHFsELAARFYASevLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqSFVSP 268
Cdd:cd06635 107 CLGSASDLLEvHKKPLQEI-EIAAITHGA--LQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA--SIASP 177
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
105-407 3.58e-08

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: 55.05  E-value: 3.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 105 KNEDlglghFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMligrKKLVRAQTERE--ILGLLDHPFLPTLYSHFE 182
Cdd:cd06649   3 KDDD-----FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEI----KPAIRNQIIRElqVLHECNSPYIVGFYGAFY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 183 TEKFSCLLMEFCSGGDL-HILRQkqpGKHFSELAARFYASEVLLALEYL-HMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:cd06649  74 SDGEISICMEHMDGGSLdQVLKE---AKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 261 SLQsfvsptLIQSTSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaar 340
Cdd:cd06649 151 SGQ------LIDSMAN---------------------------------------------------------------- 160
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 341 smSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNREtLFNVVGQPLKFPEGS 407
Cdd:cd06649 161 --SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKE-LEAIFGRPVVDGEEG 224
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
113-400 5.64e-08

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: 54.27  E-value: 5.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLA-ELREMGCFFAMKvmdkgmligrkkLVRAQTEREILGL--------------LDHPFLPTL 177
Cdd:cd07862   2 QYECVAEIGEGAYGKVFKArDLKNGGRFVALK------------RVRVQTGEEGMPLstirevavlrhletFEHPNVVRL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 178 Y-----SHFETEKFSCLLMEFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH 252
Cdd:cd07862  70 FdvctvSRTDRETKLTLVFEHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 253 IMLSDFDLS-LQSFVSPTliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpm 331
Cdd:cd07862 149 IKLADFGLArIYSFQMAL-------------------------------------------------------------- 166
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 332 liaeptaarsMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP 400
Cdd:cd07862 167 ----------TSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLgkiLDVIGLP 228
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
119-261 5.77e-08

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: 54.18  E-value: 5.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVY--LAELREMGCFFAMKVMDKGmligRKKLVRAQ--TEREILGLLDHPFLPTLYSHFETEKFsCLLMEFC 194
Cdd:cd05115  11 ELGSGNFGCVKkgVYKMRKKQIDVAIKVLKQG----NEKAVRDEmmREAQIMHQLDNPYIVRMIGVCEAEAL-MLVMEMA 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 195 SGGDLH-ILRQKQPGKHFSELAARFYasEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05115  86 SGGPLNkFLSGKKDEITVSNVVELMH--QVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLS 151
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
119-427 9.35e-08

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: 53.28  E-value: 9.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMdkgmligRKKLVRAQtEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGD 198
Cdd:cd13991  13 RIGRGSFGEVHRMEDKQTGFQCAVKKV-------RLEVFRAE-ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 199 LHILrQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG-HIMLSDFDLSLqsfvsptliqstsqp 277
Cdd:cd13991  85 LGQL-IKEQGC-LPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAE--------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 278 schiasyciqppCIDPScklpvaciqpscfkprflnnkprkaktekAGSDSLpmliaeptaARSMSFVGTHEYLAPEIIR 357
Cdd:cd13991 148 ------------CLDPD-----------------------------GLGKSL---------FTGDYIPGTETHMAPEVVL 177
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 358 GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQP---LKFPEGSISFAAKdLIRGLLTKDPKKR 427
Cdd:cd13991 178 GKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPpplREIPPSCAPLTAQ-AIQAGLRKEPVHR 249
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
114-261 1.19e-07

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: 53.54  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd07869   7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTP--FTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 194 CSGgDLHILRQKQPGKHFSElAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07869  85 VHT-DLCQYMDKHPGGLHPE-NVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA 150
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
113-261 1.70e-07

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: 52.69  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCF----FAMKVMDKGMLIGRKKLVRAQT----------EREILGLLDHPFLPTLY 178
Cdd:cd05095   6 LLTFKEKLGEGQFGEVHLCEAEGMEKFmdkdFALEVSENQPVLVAVKMLRADAnknarndflkEIKIMSRLKDPNIIRLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 179 SHFETEKFSCLLMEFCSGGDLH--ILRQKQPGK----------HFSELaaRFYASEVLLALEYLHMMGVVYRDLKPENVM 246
Cdd:cd05095  86 AVCITDDPLCMITEYMENGDLNqfLSRQQPEGQlalpsnaltvSYSDL--RFMAAQIASGMKYLSSLNFVHRDLATRNCL 163
                       170
                ....*....|....*
gi 15242554 247 VREDGHIMLSDFDLS 261
Cdd:cd05095 164 VGKNYTIKIADFGMS 178
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
114-268 1.77e-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: 52.72  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd06634  17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 194 CSGGDLHILR-QKQPGKHFsELAARFYASevLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqSFVSP 268
Cdd:cd06634  97 CLGSASDLLEvHKKPLQEV-EIAAITHGA--LQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA--SIMAP 167
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
117-261 1.83e-07

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: 52.44  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVM-----DKGmligrkklVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:cd07839   5 LEKIGEGTYGTVFKAKNRETHEIVALKRVrldddDEG--------VPSSALREIclLKELKHKNIVRLYDVLHSDKKLTL 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 190 LMEFCSGgDLHilrqkqpgKHFSEL-------AARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07839  77 VFEYCDQ-DLK--------KYFDSCngdidpeIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLA 146
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
155-261 2.13e-07

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: 52.57  E-value: 2.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 155 KLVRAQTEREILGLLDHPFLPTLYSHFETEkfsclLMefcsGGDLHILRQKQP-GKHFselaARFYASEVLLALEYLHMM 233
Cdd:cd07856  61 KLLKHLRHENIISLSDIFISPLEDIYFVTE-----LL----GTDLHRLLTSRPlEKQF----IQYFLYQILRGLKYVHSA 127
                        90       100
                ....*....|....*....|....*...
gi 15242554 234 GVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07856 128 GVIHRDLKPSNILVNENCDLKICDFGLA 155
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
161-381 2.14e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 53.07  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  161 TEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGgDLHILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDL 240
Cdd:PHA03212 132 TEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILA--IERSVLRAIQYLHENRIIHRDI 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  241 KPENVMVREDGHIMLSDFdlslqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkak 320
Cdd:PHA03212 209 KAENIFINHPGDVCLGDF-------------------------------------------------------------- 226
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554  321 tekaGSDSLPMLIaepTAARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGK 381
Cdd:PHA03212 227 ----GAACFPVDI---NANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
117-261 3.72e-07

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: 51.89  E-value: 3.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVMDkgMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd07870   5 LEKLGEGSYATVYKGISRINGQLVALKVIS--MKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 197 GDLHILRQKQPGKHFSELaaRFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07870  83 DLAQYMIQHPGGLHPYNV--RLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLA 145
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
116-261 4.04e-07

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 51.29  E-value: 4.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMgCFFAMKVMDKGMLiGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd05059   8 FLKELGSGQFGVVHLGKWRGK-IDVAIKMIKEGSM-SEDDFIE---EAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMA 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 196 GGDLHILRQKQPGKHFSELAARFyASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05059  83 NGCLLNYLRERRGKFQTEQLLEM-CKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLA 147
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
114-432 4.70e-07

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: 51.38  E-value: 4.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELR-EMGCFF--AMKVMdKGMLIGRKKLVRAQTEREILGLLDHPFLPTL----YSHFETEKF 186
Cdd:cd05035   1 LKLGKILGEGEFGSVMEAQLKqDDGSQLkvAVKTM-KVDIHTYSEIEEFLSEAACMKDFDHPNVMRLigvcFTASDLNKP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SC--LLMEFCSGGDLHIL----RQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:cd05035  80 PSpmVILPFMKHGDLHSYllysRLGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 261 SLQSFVSPTLIQStsqpscHIAsyciqppcidpscKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaar 340
Cdd:cd05035 160 SRKIYSGDYYRQG------RIS-------------KMPV----------------------------------------- 179
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 341 smsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNREtLFNVV--GQPLKFPEGSISfAAKDLIR 417
Cdd:cd05035 180 --------KWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHE-IYDYLrnGNRLKQPEDCLD-EVYFLMY 249
                       330
                ....*....|....*
gi 15242554 418 GLLTKDPKKRLGFKK 432
Cdd:cd05035 250 FCWTVDPKDRPTFTK 264
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
115-393 4.73e-07

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: 51.10  E-value: 4.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLA---ELREMgcffAMKVMDKGMLiGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd05112   7 TFVQEIGSGQFGLVHLGywlNKDKV----AIKTIREGAM-SEEDFIE---EAEVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqSFVSPTli 271
Cdd:cd05112  79 EFMEHGCLSDYLRTQRGL-FSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMT--RFVLDD-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 QSTSQpschiasyciqppcidPSCKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgthEYL 351
Cdd:cd05112 154 QYTSS----------------TGTKFPV-------------------------------------------------KWS 168
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL 393
Cdd:cd05112 169 SPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVV 211
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
114-431 5.33e-07

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: 50.90  E-value: 5.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMgCFFAMKVMDKGMLIGRKKLvraQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd05148   8 FTLERKLGSGYFGEVWEGLWKNR-VRVAIKILKSDDLLKQQDF---QKEVQALKRLRHKHLISLFAVCSVGEPVYIITEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspTLIQs 273
Cdd:cd05148  84 MEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLA-------RLIK- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciQPPCIDPSCKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvgthEYLAP 353
Cdd:cd05148 156 -------------EDVYLSSDKKIPY-------------------------------------------------KWTAP 173
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVVG-----QPLKFPEgsisfAAKDLIRGLLTKDPKKR 427
Cdd:cd05148 174 EAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAgyrmpCPAKCPQ-----EIYKIMLECWAAEPEDR 248

                ....
gi 15242554 428 LGFK 431
Cdd:cd05148 249 PSFK 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
118-392 5.35e-07

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: 50.91  E-value: 5.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIG-RKKLVRaqtEREILGLLDHPFLPTLYShFETEKFSCLL-MEFCS 195
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDlKRKFLQ---EARILKQYDHPNIVKLIG-VCVQKQPIMIvMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGD-LHILRQKQPG------KHFSELAARfyasevllALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSfvsp 268
Cdd:cd05041  77 GGSlLTFLRKKGARltvkqlLQMCLDAAA--------GMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREE---- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpscHIASYCIQppcidpscklpvaciqpscfkprflnnkprkaktekAGSDSLPMliaeptaarsmsfvgth 348
Cdd:cd05041 145 -----------EDGEYTVS------------------------------------DGLKQIPI----------------- 160
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRET 392
Cdd:cd05041 161 KWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQT 205
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
116-407 6.30e-07

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: 50.79  E-value: 6.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmligRKKLVRAQTEREILGLLDHPFLpTLYSHFETEKFSCLLMEFCS 195
Cdd:cd14150   4 MLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPT----PEQLQAFKNEMQVLRKTRHVNI-LLFMGFMTRPNFAIITQWCE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDLHilrqkqpgKHFSELAARF-------YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd14150  79 GSSLY--------RHLHVTETRFdtmqlidVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLA------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSDSLpmliAEPTaarsmsfvGTH 348
Cdd:cd14150 144 -------------------------------------------------TVKTRWSGSQQV----EQPS--------GSI 162
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 349 EYLAPEIIR---GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS 407
Cdd:cd14150 163 LWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPDLS 224
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
346-428 6.62e-07

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: 50.87  E-value: 6.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 346 GTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNREtLFNVVGQP-LKFPE-GSISFAAKDLIRGLLTK 422
Cdd:cd13974 195 GSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQE-LFRKIKAAeYTIPEdGRVSENTVCLIRKLLVL 273

                ....*.
gi 15242554 423 DPKKRL 428
Cdd:cd13974 274 NPQKRL 279
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
113-261 7.89e-07

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: 50.66  E-value: 7.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGcffamkvMDKGMLIGRKKLVRA--------QTEREILGLLDHPFLPTL--YSHFE 182
Cdd:cd05081   5 HLKYISQLGKGNFGSVELCRYDPLG-------DNTGALVAVKQLQHSgpdqqrdfQREIQILKALHSDFIVKYrgVSYGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 183 TEKFSCLLMEFCSGGDLHILRQKqpgkHFSELAAR---FYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd05081  78 GRRSLRLVMEYLPSGCLRDFLQR----HRARLDASrllLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFG 153

                ..
gi 15242554 260 LS 261
Cdd:cd05081 154 LA 155
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
118-431 8.52e-07

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 50.30  E-value: 8.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYlaelreMGCF-----FAMKVMDKGMLIGRKKLVRAQtereILGLLDHPFLPTLYSHFETEKFScLLME 192
Cdd:cd14203   1 VKLGQGCFGEVW------MGTWngttkVAIKTLKPGTMSPEAFLEEAQ----IMKKLRHDKLVQLYAVVSEEPIY-IVTE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspTLIQ 272
Cdd:cd14203  70 FMSKGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA-------RLIE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 273 STSQPSCHIASYciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslPMLIAEPTAARSMSFVgtheyla 352
Cdd:cd14203 143 DNEYTARQGAKF---------------------------------------------PIKWTAPEAALYGRFT------- 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 353 peiIRGDghgssvdWWTFGIFLYELLT-GKTPFKGNGNRETLFNV-VGQPLKFPEGSISfAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd14203 171 ---IKSD-------VWSFGILLTELVTkGRVPYPGMNNREVLEQVeRGYRMPCPPGCPE-SLHELMCQCWRKDPEERPTF 239

                .
gi 15242554 431 K 431
Cdd:cd14203 240 E 240
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
120-263 9.59e-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: 50.00  E-value: 9.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGCFfAMKVMDKGMLIGRKklVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGD- 198
Cdd:cd05085   4 LGKGNFGEVYKGTLKDKTPV-AVKTCKEDLPQELK--IKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDf 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 199 LHILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQ 263
Cdd:cd05085  81 LSFLRKKKDELKTKQLVK--FSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ 143
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
190-442 1.06e-06

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: 50.77  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEfcsgGDLHILRQKQpgkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspt 269
Cdd:cd07849  89 LME----TDLYKLIKTQ---HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLA-------- 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liQSTSQPSCHiasyciqppcidpscklpvaciqpscfkPRFLnnkprkakTEkagsdslpmliaeptaarsmsFVGTHE 349
Cdd:cd07849 154 --RIADPEHDH----------------------------TGFL--------TE---------------------YVATRW 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEI-IRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQP-------------------LKFPEG 406
Cdd:cd07849 175 YRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLnliLGILGTPsqedlnciislkarnyiksLPFKPK 254
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15242554 407 sISFA---------AKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd07849 255 -VPWNklfpnadpkALDLLDKMLTFNPHKRI----TVEEALAHPY 294
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
350-442 1.24e-06

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: 49.49  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIrGDGHGSS---VDWWTFGIFLYELLTGKTPFKgNGNRETLFNVVGQ-PLKFPEGsISFAAKDLIRGLLTKDPK 425
Cdd:cd14024 152 YVGPEIL-SSRRSYSgkaADVWSLGVCLYTMLLGRYPFQ-DTEPAALFAKIRRgAFSLPAW-LSPGARCLVSCMLRRSPA 228
                        90
                ....*....|....*..
gi 15242554 426 KRLgfkkGATEIKQHPF 442
Cdd:cd14024 229 ERL----KASEILLHPW 241
pknD PRK13184
serine/threonine-protein kinase PknD;
111-385 1.24e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 51.31  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmLIGRKKL-VRAQTEREILGLLDHPFLPTLYSHFETEKFSCL 189
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRED-LSENPLLkKRFLREAKIAADLIHPGIVPVYSICSDGDPVYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  190 LMEFCSGGDL-HILR---QKQ--PGKHFSELAARFYAS---EVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:PRK13184  80 TMPYIEGYTLkSLLKsvwQKEslSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  261 SLQsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGSDSLPMliaEPTAAR 340
Cdd:PRK13184 160 AIF-----------------------------------------------------KKLEEEDLLDIDVDE---RNICYS 183
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15242554  341 SMS----FVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFK 385
Cdd:PRK13184 184 SMTipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR 232
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
114-431 1.51e-06

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 49.68  E-value: 1.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMgCFFAMKVMDKGMLIGRKKLVRAQtereILGLLDHPFLPTLYSHFETEKFScLLMEF 193
Cdd:cd05069  14 LRLDVKLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMMPEAFLQEAQ----IMKKLRHDKLVPLYAVVSEEPIY-IVTEF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 194 CSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspTLIQS 273
Cdd:cd05069  88 MGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA-------RLIED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 TSQpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakTEKAGSdSLPMLIAEPTAARSMSFVgtheylap 353
Cdd:cd05069 161 NEY--------------------------------------------TARQGA-KFPIKWTAPEAALYGRFT-------- 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 eiIRGdghgssvDWWTFGIFLYELLT-GKTPFKGNGNRETLFNV-VGQPLKFPEGSISfAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd05069 188 --IKS-------DVWSFGILLTELVTkGRVPYPGMVNREVLEQVeRGYRMPCPQGCPE-SLHELMKLCWKKDPDERPTFE 257
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
177-439 1.54e-06

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: 49.67  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 177 LYSHFETEKFSCLLMEFCSGGDL----HILRQKQPGKHFSELAarfyaSEVLLALEYLHMMGVVYRDLKPENVMVREDGH 252
Cdd:cd14151  68 LFMGYSTKPQLAIVTQWCEGSSLyhhlHIIETKFEMIKLIDIA-----RQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 253 IMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSDSLPML 332
Cdd:cd14151 143 VKIGDFGLA--------------------------------------------------------TVKSRWSGSHQFEQL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 333 iaeptaarsmsfVGTHEYLAPEIIR---GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGS-- 407
Cdd:cd14151 167 ------------SGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSkv 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15242554 408 ---ISFAAKDLIRGLLTKDPKKRLGFKKGATEIKQ 439
Cdd:cd14151 235 rsnCPKAMKRLMAECLKKKRDERPLFPQILASIEL 269
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
116-432 1.58e-06

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: 49.65  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLaelremGCFFAMKVMDKGMLIGRKKLVRAQTEREILGLL---------DHPFLPTLYSHFETEKF 186
Cdd:cd05032  10 LIRELGQGSFGMVYE------GLAKGVVKGEPETRVAIKTVNENASMRERIEFLneasvmkefNCHHVVRLLGVVSTGQP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGGDLH-ILRQKQPGKHFSEL-----AARFY--ASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd05032  84 TLVVMELMAKGDLKsYLRSRRPEAENNPGlgpptLQKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNkprkakTE---KAGSDSLPMliae 335
Cdd:cd05032 164 GMT------------------------------------------------RDIYE------TDyyrKGGKGLLPV---- 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 336 ptaaRSMsfvgtheylAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL-FNVVGQPLKFPEGSISFAAk 413
Cdd:cd05032 186 ----RWM---------APESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLkFVIDGGHLDLPENCPDKLL- 251
                       330
                ....*....|....*....
gi 15242554 414 DLIRGLLTKDPKKRLGFKK 432
Cdd:cd05032 252 ELMRMCWQYNPKMRPTFLE 270
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
114-443 1.64e-06

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: 49.98  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREM--GCFFAMKVM--DKGMLIGrkklVRAQTEREILGL--LDHPFLPTLYSHF--ETEK 185
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRKNGkdGKEYAIKKFkgDKEQYTG----ISQSACREIALLreLKHENVVSLVEVFleHADK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLMEFCSGGDLHILRQkqpgkHFSELAARFYASEV-------LLALEYLHMMGVVYRDLKPENVMV----REDGHIM 254
Cdd:cd07842  78 SVYLLFDYAEHDLWQIIKF-----HRQAKRVSIPPSMVksllwqiLNGIHYLHSNWVLHRDLKPANILVmgegPERGVVK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 255 LSDFDLSlQSFVSPtliqstsqpschiasyciqppcidpscklpvaciqpscFKPRFLNNKPrkaktekagsdslpmlia 334
Cdd:cd07842 153 IGDLGLA-RLFNAP--------------------------------------LKPLADLDPV------------------ 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 335 eptaarsmsfVGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNR------------ETLFNVVGQP- 400
Cdd:cd07842 176 ----------VVTIWYRAPELLLGARHyTKAIDIWAIGCIFAELLTLEPIFKGREAKikksnpfqrdqlERIFEVLGTPt 245
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 401 -------LKFPE----GSISFAAK---------------------DLIRGLLTKDPKKRLgfkkGATEIKQHPFF 443
Cdd:cd07842 246 ekdwpdiKKMPEydtlKSDTKASTypnsllakwmhkhkkpdsqgfDLLRKLLEYDPTKRI----TAEEALEHPYF 316
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
118-248 1.96e-06

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 49.66  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAE---LREMGCFFAMKVMDKG----MLIGRKKLvraqtEREILGLLDHPFLPTLYSH-FETEkfSCL 189
Cdd:cd13981   6 KELGEGGYASVYLAKdddEQSDGSLVALKVEKPPsiweFYICDQLH-----SRLKNSRLRESISGAHSAHlFQDE--SIL 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 190 LMEFCSGG---DLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVR 248
Cdd:cd13981  79 VMDYSSQGtllDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLR 140
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
111-442 2.00e-06

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: 49.42  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAelremgcffamKVMDKGMLIGRKKlVRAQTERE-----------ILGLLDHPFLPTLYS 179
Cdd:cd07864   6 VDKFDIIGIIGEGTYGQVYKA-----------KDKDTGELVALKK-VRLDNEKEgfpitaireikILRQLNHRSVVNLKE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 180 ---------HFETEKFSC-LLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVRE 249
Cdd:cd07864  74 ivtdkqdalDFKKDKGAFyLVFEYMDHDLMGLLESGL--VHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 250 DGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTEKagsdsl 329
Cdd:cd07864 152 KGQIKLADFGLA------------------------------------------------RLYNSEESRPYTNK------ 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 330 pmliaeptaarsmsfVGTHEYLAPEIIRGDG-HGSSVDWWTFGIFLYELLTGKTPFKGN---GNRETLFNVVGQP----- 400
Cdd:cd07864 178 ---------------VITLWYRPPELLLGEErYGPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRLCGSPcpavw 242
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 401 ---LKFP---------------EGSISF---AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd07864 243 pdvIKLPyfntmkpkkqyrrrlREEFSFiptPALDLLDHMLTLDPSKRC----TAEQALNSPW 301
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
159-393 2.14e-06

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: 49.53  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 159 AQTEREILGLL------DHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHM 232
Cdd:cd14135  44 GLKELEILKKLndadpdDKKHCIRLLRHFEHKNHLCLVFESLSMNLREVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKK 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 233 MGVVYRDLKPENVMVREDgHIMLSDFDLSLQSFVSptliqstsqpSCHIASYCIQppcidpscklpvaciqpscfkpRFl 312
Cdd:cd14135 124 CNILHADIKPDNILVNEK-KNTLKLCDFGSASDIG----------ENEITPYLVS----------------------RF- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 313 nnkprkaktekagsdslpmliaeptaarsmsfvgtheYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRET 392
Cdd:cd14135 170 -------------------------------------YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHM 212

                .
gi 15242554 393 L 393
Cdd:cd14135 213 L 213
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
162-430 2.87e-06

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: 48.81  E-value: 2.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLYSHFETEKFsCLLMEFCSGGDLHILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLK 241
Cdd:cd05116  46 EANVMQQLDNPYIVRMIGICEAESW-MLVMEMAELGPLNKFLQKN--RHVTEKNITELVHQVSMGMKYLEESNFVHRDLA 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 242 PENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfKPRFLNNKPRKAKT 321
Cdd:cd05116 123 ARNVLLVTQHYAKISDFGLS----------------------------------------------KALRADENYYKAQT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 322 ekagSDSLPMliaeptaarsmsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKG-NGNRETLFNVVGQ 399
Cdd:cd05116 157 ----HGKWPV-----------------KWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGmKGNEVTQMIEKGE 215
                       250       260       270
                ....*....|....*....|....*....|.
gi 15242554 400 PLKFPEGSiSFAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd05116 216 RMECPAGC-PPEMYDLMKLCWTYDVDERPGF 245
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
113-443 3.00e-06

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: 48.76  E-value: 3.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREmgcfFAMKVMDKGMLIGRKKLV------RAQTEREILGLL--DHPFLPTLYShFETE 184
Cdd:cd14019   2 KYRIIEKIGEGTFSSVYKAEDKL----HDLYDRNKGRLVALKHIYptsspsRILNELECLERLggSNNVSGLITA-FRNE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDLHILRQKQPGKHFselaaRFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHIMLSDFDLSlq 263
Cdd:cd14019  77 DQVVAVLPYIEHDDFRDFYRKMSLTDI-----RIYLRNLFKALKHVHSFGIIHRDVKPGNFLYnRETGKGVLVDFGLA-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 sfvsptliQSTSQPschiasyciqppcidpscklpvaciqpscfkprflnnKPRKAktekagsdslpmliaePTAarsms 343
Cdd:cd14019 150 --------QREEDR-------------------------------------PEQRA----------------PRA----- 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 fvGTHEYLAPEII-RGDGHGSSVDWWTFGIFLYELLTGKTP-FKGNGNRETLFNVVgqplkfpegSI--SFAAKDLIRGL 419
Cdd:cd14019 164 --GTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRFPfFFSSDDIDALAEIA---------TIfgSDEAYDLLDKL 232
                       330       340
                ....*....|....*....|....
gi 15242554 420 LTKDPKKRlgfkKGATEIKQHPFF 443
Cdd:cd14019 233 LELDPSKR----ITAEEALKHPFF 252
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
117-444 3.79e-06

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: 48.68  E-value: 3.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREI--LGLLDH-PFLPTLYS--HFETEKFSCLLM 191
Cdd:cd07837   6 LEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEGVPSTALREVslLQMLSQsIYIVRLLDveHVEENGKPLLYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 --EFCSGG-----DLHilrQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHIMLSDFDLSlQ 263
Cdd:cd07837  83 vfEYLDTDlkkfiDSY---GRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADLGLG-R 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 SFVSPtliqstsqpschIASYciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsms 343
Cdd:cd07837 159 AFTIP------------IKSY----------------------------------------------------------- 167
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 fvgTHE-----YLAPEIIRGDGHGS-SVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK------------ 402
Cdd:cd07837 168 ---THEivtlwYRAPEVLLGSTHYStPVDMWSVGCIFAEMSRKQPLFPGDSELQQLlhiFRLLGTPNEevwpgvsklrdw 244
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15242554 403 --FPE----------GSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFN 444
Cdd:cd07837 245 heYPQwkpqdlsravPDLEPEGVDLLTKMLAYDPAKRI----SAKAALQHPYFD 294
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
115-393 4.21e-06

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: 48.50  E-value: 4.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELREmgcffAMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd05072  10 KLVKKLGAGQFGEVWMGYYNN-----STKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqst 274
Cdd:cd05072  85 AKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLA------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 275 sqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKprkaktekagsdslpmliaEPTAARSMSFvgTHEYLAPE 354
Cdd:cd05072 152 -----------------------------------RVIEDN-------------------EYTAREGAKF--PIKWTAPE 175
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15242554 355 IIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL 393
Cdd:cd05072 176 AINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVM 215
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
165-442 4.48e-06

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: 48.97  E-value: 4.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 165 ILGLLD--HPFLPTLYSHFE--TEkfsclLMEfcsgGDLH-ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRD 239
Cdd:cd07853  61 VLSALDilQPPHIDPFEEIYvvTE-----LMQ----SDLHkIIVSPQP---LSSDHVKVFLYQILRGLKYLHSAGILHRD 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 240 LKPENVMVREDGHIMLSDFDLslqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkA 319
Cdd:cd07853 129 IKPGNLLVNSNCVLKICDFGL----------------------------------------------------------A 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 320 KTEkagsdslpmliaEPTAARSMSF-VGTHEYLAPEIIRGDGH-GSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---F 394
Cdd:cd07853 151 RVE------------EPDESKHMTQeVVTQYYRAPEILMGSRHyTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLdliT 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 395 NVVGQP--------------------LKFPEGSISF--------AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPF 442
Cdd:cd07853 219 DLLGTPsleamrsacegarahilrgpHKPPSLPVLYtlssqathEAVHLLCRMLVFDPDKRI----SAADALAHPY 290
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
213-442 5.29e-06

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: 48.04  E-value: 5.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 213 ELAARFYaSEVLLALEYLHMMGVVYRDLKPENVMvredghIMLSDFDLSLQSFVSPTLIQSTSQpschiasyciqppcid 292
Cdd:cd14100 106 ELARSFF-RQVLEAVRHCHNCGVLHRDIKDENIL------IDLNTGELKLIDFGSGALLKDTVY---------------- 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 293 pscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYLAPEIIRGDG-HGSSVDWWTFG 371
Cdd:cd14100 163 -------------------------------------------------TDFDGTRVYSPPEWIRFHRyHGRSAAVWSLG 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 372 IFLYELLTGKTPFKGNGnretlfNVVGQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFKkgatEIKQHPF 442
Cdd:cd14100 194 ILLYDMVCGDIPFEHDE------EIIRGQVFFRQ-RVSSECQHLIKWCLALRPSDRPSFE----DIQNHPW 253
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
114-386 5.63e-06

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: 48.59  E-value: 5.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKvmdkgMLIGRKKLVR-AQTEREILGLL-----DHPF-LPTLYSHFETEKF 186
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALK-----MVRNEKRFHRqAAEEIRILEHLkkqdkDNTMnVIHMLESFTFRNH 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 SCLLMEFCSGgDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH--IMLSDFDlslqs 264
Cdd:cd14224 142 ICMTFELLSM-NLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG----- 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcidpscklpvaciqPSCFKPRflnnkprkaktekagsdslpmliaeptaaRSMSF 344
Cdd:cd14224 216 ---------------------------------------SSCYEHQ-----------------------------RIYTY 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15242554 345 VGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG 386
Cdd:cd14224 228 IQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPG 269
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
116-440 5.86e-06

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: 48.10  E-value: 5.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGmligRKKLVRAQTEREILGLLDHPFLpTLYSHFETEKFSCLLMEFCS 195
Cdd:cd14149  16 LSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQFQAFRNEVAVLRKTRHVNI-LLFMGYMTKDNLAIVTQWCE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDLHilrqkqpgKHFSELAARF-------YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd14149  91 GSSLY--------KHLHVQETKFqmfqlidIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSDSlpmlIAEPTaarsmsfvGTH 348
Cdd:cd14149 156 -------------------------------------------------TVKSRWSGSQQ----VEQPT--------GSI 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIR---GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLKFPEGSISF-----AAKDLIRGLL 420
Cdd:cd14149 175 LWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYkncpkAMKRLVADCI 254
                       330       340
                ....*....|....*....|..
gi 15242554 421 TKDPKKRLGFKK--GATEIKQH 440
Cdd:cd14149 255 KKVKEERPLFPQilSSIELLQH 276
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
123-440 6.15e-06

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: 47.70  E-value: 6.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 123 GDIGSVYLAELRE----MGCffamkvmdkgmligrkKLVRAQ----TEREILGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd13995  15 GAFGKVYLAQDTKtkkrMAC----------------KLIPVEqfkpSDVEIQACFRHENIAELYGALLWEETVHLFMEAG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGD-LHILRQKQPGKHFSELaarFYASEVLLALEYLHMMGVVYRDLKPENVmVREDGHIMLSDFDLSLQsfvsptliqs 273
Cdd:cd13995  79 EGGSvLEKLESCGPMREFEII---WVTKHVLKGLDFLHSKNIIHHDIKPSNI-VFMSTKAVLVDFGLSVQ---------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 274 tsqpschiasyciqppcidpscklpvacIQPSCFKPRFLNnkprkaktekagsdslpmliaeptaarsmsfvGTHEYLAP 353
Cdd:cd13995 145 ----------------------------MTEDVYVPKDLR--------------------------------GTEIYMSP 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 354 EIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRET----LFNVVGQ--PLKFPEGSISFAAKDLIRGLLTKDPKKR 427
Cdd:cd13995 165 EVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQapPLEDIAQDCSPAMRELLEAALERNPNHR 244
                       330
                ....*....|...
gi 15242554 428 LgfkkGATEIKQH 440
Cdd:cd13995 245 S----SAAELLKH 253
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
114-247 7.16e-06

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: 47.92  E-value: 7.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMdKGMligRKKLVRaqteREILGLL---DHPFLPTLYSHF--ETEKFSC 188
Cdd:cd14132  20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL-KPV---KKKKIK----REIKILQnlrGGPNIVKLLDVVkdPQSKTPS 91
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 189 LLMEFCSGGDLHILRQKqpgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMV 247
Cdd:cd14132  92 LIFEYVNNTDFKTLYPT-----LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI 145
PTZ00284 PTZ00284
protein kinase; Provisional
343-457 7.60e-06

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 48.42  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  343 SFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRE--------------------------TLFNV 396
Cdd:PTZ00284 304 AIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEhlhlmektlgrlpsewagrcgteearLLYNS 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  397 VGQ--PLKFPEGSISFAAK-------------DLIRGLLTKDPKKRLGFKKGAT---------EIKQHPffnnvNWALIR 452
Cdd:PTZ00284 384 AGQlrPCTDPKHLARIARArpvrevirddllcDLIYGLLHYDRQKRLNARQMTThpyvlkyypECRQHP-----NYPDNR 458

                 ....*
gi 15242554  453 STTPP 457
Cdd:PTZ00284 459 SMLRP 463
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
113-261 7.64e-06

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 47.57  E-value: 7.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELRemGCF-FAMKVMDKGMLIGRKKLVRAQTEREilglLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd05113   5 DLTFLKELGTGQFGVVKYGKWR--GQYdVAIKMIKEGSMSEDEFIEEAKVMMN----LSHEKLVQLYGVCTKQRPIFIIT 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 192 EFCSGGDL-HILRQKQPGKHFSELAARFYasEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05113  79 EYMANGCLlNYLREMRKRFQTQQLLEMCK--DVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLS 147
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
209-464 8.44e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 48.11  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  209 KHFSE-------LAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIM-LSDFDlslqsfvsptliqstsqpsch 280
Cdd:PTZ00036 158 KHYARnnhalplFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLkLCDFG--------------------- 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  281 iasyciqppcidpscklpvaciqpscfkprflnnkprKAKTEKAGSdslpmliaeptaaRSMSFVGTHEYLAPEIIRGD- 359
Cdd:PTZ00036 217 -------------------------------------SAKNLLAGQ-------------RSVSYICSRFYRAPELMLGAt 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  360 GHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK--------------------------FPEGSISf 410
Cdd:PTZ00036 247 NYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLvriIQVLGTPTEdqlkemnpnyadikfpdvkpkdlkkvFPKGTPD- 325
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15242554  411 AAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFNNVNWALIRsttppeIPKPID 464
Cdd:PTZ00036 326 DAINFISQFLKYEPLKRL----NPIEALADPFFDDLRDPCIK------LPKYID 369
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
108-261 8.68e-06

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: 47.62  E-value: 8.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 108 DLGLGHFRLLKKLGCGDIGSVYLAEL---REMGCF-FAMKVMDKGMLIGRKKLVRAQT----------EREILGLLDHPF 173
Cdd:cd05096   1 KFPRGHLLFKEKLGEGQFGEVHLCEVvnpQDLPTLqFPFNVRKGRPLLVAVKILRPDAnknarndflkEVKILSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 174 LPTLYSHFETEKFSCLLMEFCSGGDL-------HILRQKQPGKHFSELAARF----------YASEVLLALEYLHMMGVV 236
Cdd:cd05096  81 IIRLLGVCVDEDPLCMITEYMENGDLnqflsshHLDDKEENGNDAVPPAHCLpaisyssllhVALQIASGMKYLSSLNFV 160
                       170       180
                ....*....|....*....|....*
gi 15242554 237 YRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05096 161 HRDLATRNCLVGENLTIKIADFGMS 185
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
162-277 9.39e-06

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: 47.14  E-value: 9.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLY-------SHFetekfsCLLMEFCSGGDLHILRQKQpgKHFSELAARF-YASEVLLALEYLHMM 233
Cdd:cd14064  41 EVSILCRLNHPCVIQFVgaclddpSQF------AIVTQYVSGGSLFSLLHEQ--KRVIDLQSKLiIAVDVAKGMEYLHNL 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15242554 234 G--VVYRDLKPENVMVREDGHIMLSDFDLS--LQSFVSPTLiqsTSQP 277
Cdd:cd14064 113 TqpIIHRDLNSHNILLYEDGHAVVADFGESrfLQSLDEDNM---TKQP 157
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
217-427 1.01e-05

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: 47.30  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 217 RFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDlslqsfvsptliqstsqpschiasyciqppcidpsck 296
Cdd:cd07848 103 RSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFG------------------------------------- 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 297 lpvaciqpscfkprFLNNkprkaktekagsdslpmlIAEPTAARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYE 376
Cdd:cd07848 146 --------------FARN------------------LSEGSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGE 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 377 LLTGKTPFKGNGNRETLFNV--VGQPL-----------------KFP------------EGSISFAAKDLIRGLLTKDPK 425
Cdd:cd07848 194 LSDGQPLFPGESEIDQLFTIqkVLGPLpaeqmklfysnprfhglRFPavnhpqslerryLGILSGVLLDLMKNLLKLNPT 273

                ..
gi 15242554 426 KR 427
Cdd:cd07848 274 DR 275
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
105-390 1.16e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 47.77  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  105 KNEDLGLGHFRLLKKLGCGDIGSVYLAELR----EMGCFFAMKVMDKGMLIGRK---KLVRA------QTEREILGL--L 169
Cdd:PHA03210 141 KHDDEFLAHFRVIDDLPAGAFGKIFICALRasteEAEARRGVNSTNQGKPKCERliaKRVKAgsraaiQLENEILALgrL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  170 DHPFLPTL--------YSHFETEKFSCLLMEFCSGGDLH-----ILRQkqpgkhfselaARFYASEVLLALEYLHMMGVV 236
Cdd:PHA03210 221 NHENILKIeeilrseaNTYMITQKYDFDLYSFMYDEAFDwkdrpLLKQ-----------TRAIMKQLLCAVEYIHDKKLI 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  237 YRDLKPENVMVREDGHIMLSDFdlslqsfvsptliqSTSQPschiasyciqppcidpscklpvaciqpscFKprflnnKP 316
Cdd:PHA03210 290 HRDIKLENIFLNCDGKIVLGDF--------------GTAMP-----------------------------FE------KE 320
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554  317 RKaktekagsdslpmliaeptaARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGK-TPFKGNGNR 390
Cdd:PHA03210 321 RE--------------------AFDYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDfCPIGDGGGK 375
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
111-425 1.33e-05

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: 47.33  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLiGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEK----F 186
Cdd:cd07876  20 LKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQ-NQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKsleeF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 S--CLLMEFCSGGDLHILRQKQPGKHFSELaarFYasEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqs 264
Cdd:cd07876  99 QdvYLVMELMDANLCQVIHMELDHERMSYL---LY--QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA--- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEkagsdslpmLIAEPtaarsmsF 344
Cdd:cd07876 171 ----------------------------------------------------RTACTN---------FMMTP-------Y 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETlFNVVGQPLKFPEGSISFAAKDLIRGLLTKDP 424
Cdd:cd07876 183 VVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQ-WNKVIEQLGTPSAEFMNRLQPTVRNYVENRP 261

                .
gi 15242554 425 K 425
Cdd:cd07876 262 Q 262
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
113-261 1.53e-05

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: 46.55  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLaelremgCFFAMKVMDKGMLIGRKKLVRAQTER--------EILGLLDHP----FLPTLYSh 180
Cdd:cd14205   5 HLKFLQQLGKGNFGSVEM-------CRYDPLQDNTGEVVAVKKLQHSTEEHlrdfereiEILKSLQHDnivkYKGVCYS- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 181 fETEKFSCLLMEFCSGGDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:cd14205  77 -AGRRNLRLIMEYLPYGSLRDYLQKHKER-IDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGL 154

                .
gi 15242554 261 S 261
Cdd:cd14205 155 T 155
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
117-261 1.61e-05

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: 46.61  E-value: 1.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmligrkklVRAQTE--------RE--ILGLLDHPFLPTLYSHFETEKF 186
Cdd:cd07844   5 LDKLGEGSYATVYKGRSKLTGQLVALKE------------IRLEHEegapftaiREasLLKDLKHANIVTLHDIIHTKKT 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242554 187 SCLLMEFCSGgDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07844  73 LTLVFEYLDT-DLKQYMDDCGGG-LSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA 145
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
117-263 1.68e-05

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 46.62  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELREMGCF----FAMKVMDKGMLIGRKKLV--RAQTEREILGLLDHPFLPTLYSHFETEKFS-CL 189
Cdd:cd14001   4 MKKLGYGTGVNVYLMKRSPRGGSsrspWAVKKINSKCDKGQRSLYqeRLKEEAKILKSLNHPNIVGFRAFTKSEDGSlCL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFC--SGGDL-----HILRQKQPGKHFSELAArfyasEVLLALEYLHM-MGVVYRDLKPENVMVREDGHIM-LSDFDL 260
Cdd:cd14001  84 AMEYGgkSLNDLieeryEAGLGPFPAATILKVAL-----SIARALEYLHNeKKILHGDIKSGNVLIKGDFESVkLCDFGV 158

                ...
gi 15242554 261 SLQ 263
Cdd:cd14001 159 SLP 161
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
159-261 1.80e-05

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: 46.52  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 159 AQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGdlhiLRQKQP--GKHFSELAARFYASEVLLALEYLHMMGVV 236
Cdd:cd07872  51 AIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKD----LKQYMDdcGNIMSMHNVKIFLYQILRGLAYCHRRKVL 126
                        90       100
                ....*....|....*....|....*
gi 15242554 237 YRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd07872 127 HRDLKPQNLLINERGELKLADFGLA 151
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
109-431 2.02e-05

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: 46.13  E-value: 2.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 109 LGLGHFRLLKKLGCGDIGSVYLAELRemGCFFAMKVMdkgmligrKKLVRAQT---EREILGLLDHPFLPTLYSHFETEK 185
Cdd:cd05082   3 LNMKELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCI--------KNDATAQAflaEASVMTQLRHSNLVQLLGVIVEEK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLM-EFCSGGDL-HILRQKQPGKHFSELAARFyASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQ 263
Cdd:cd05082  73 GGLYIVtEYMAKGSLvDYLRSRGRSVLGGDCLLKF-SLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 SfvspTLIQSTSqpschiasyciqppcidpscKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsms 343
Cdd:cd05082 152 A----SSTQDTG--------------------KLPV-------------------------------------------- 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 fvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKgngnRETLFNVV-----GQPLKFPEGSISfAAKDLIR 417
Cdd:cd05082 164 -----KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYP----RIPLKDVVprvekGYKMDAPDGCPP-AVYDVMK 233
                       330
                ....*....|....
gi 15242554 418 GLLTKDPKKRLGFK 431
Cdd:cd05082 234 NCWHLDAAMRPSFL 247
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
222-460 2.09e-05

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: 46.58  E-value: 2.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 222 EVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvac 301
Cdd:cd07875 134 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA---------------------------------------- 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 302 iqpscfkprflnnkpRKAKTEkagsdslpmLIAEPtaarsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGK 381
Cdd:cd07875 174 ---------------RTAGTS---------FMMTP-------YVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGG 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 382 TPFKGNGNRETLFNVV---GQP---------------------------------LKFPEGS-----ISFAAKDLIRGLL 420
Cdd:cd07875 223 VLFPGTDHIDQWNKVIeqlGTPcpefmkklqptvrtyvenrpkyagysfeklfpdVLFPADSehnklKASQARDLLSKML 302
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15242554 421 TKDPKKRLgfkkGATEIKQHPFFNNVNWALIRSTTPPEIP 460
Cdd:cd07875 303 VIDASKRI----SVDEALQHPYINVWYDPSEAEAPPPKIP 338
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
116-261 2.43e-05

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 46.15  E-value: 2.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMGcfFAMKVMDKGMLIG---RKKLVRAQTEREILGLLDHP----FLPTLYSHFETEKFSC 188
Cdd:cd05075   4 LGKTLGEGEFGSVMEGQLNQDD--SVLKVAVKTMKIAictRSEMEDFLSEAVCMKEFDHPnvmrLIGVCLQNTESEGYPS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 --LLMEFCSGGDLH--ILRQK---QPGKHFSELAARFYAsEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05075  82 pvVILPFMKHGDLHsfLLYSRlgdCPVYLPTQMLVKFMT-DIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLS 160
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
189-430 2.92e-05

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: 45.80  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLH--ILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVrEDGHIMLSDFDLslqsfv 266
Cdd:cd14063  73 IVTSLCKGRTLYslIHERKEK---FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGL------ 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 sptliqstsqpschiasyciqppcidpscklpvaciqpscFKPRFLNNKPRKAKTEKAGSDSLPmliaeptaarsmsfvg 346
Cdd:cd14063 143 ----------------------------------------FSLSGLLQPGRREDTLVIPNGWLC---------------- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 347 theYLAPEIIRGDGHGSSV----------DWWTFGIFLYELLTGKTPFKGNGNRETLFNV-VGQPLKFPEGSISFAAKDL 415
Cdd:cd14063 167 ---YLAPEIIRALSPDLDFeeslpftkasDVYAFGTVWYELLAGRWPFKEQPAESIIWQVgCGKKQSLSQLDIGREVKDI 243
                       250
                ....*....|....*
gi 15242554 416 IRGLLTKDPKKRLGF 430
Cdd:cd14063 244 LMQCWAYDPEKRPTF 258
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
222-387 3.01e-05

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: 46.25  E-value: 3.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 222 EVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLslqsfvsptliqstsqpschiasyciqppcidpscklpvac 301
Cdd:cd07850 110 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL----------------------------------------- 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 302 iqpscfkprflnnkprkAKTekAGSDSLpmliaeptaarsMS-FVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTG 380
Cdd:cd07850 149 -----------------ART--AGTSFM------------MTpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRG 197

                ....*..
gi 15242554 381 KTPFKGN 387
Cdd:cd07850 198 TVLFPGT 204
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
111-427 3.44e-05

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: 45.58  E-value: 3.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVYLAELREMGCFFAMK-VMDKGmlIGRKKLVRAQTEREILGLLDHPFLpTLYSHFETEKFSCL 189
Cdd:cd14049   5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKkILIKK--VTKRDCMKVLREVKVLAGLQHPNI-VGYHTAWMEHVQLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 L---MEFC--SGGDLHILRQKQPgkHFSELAARFYA-----------SEVLLALEYLHMMGVVYRDLKPENVMVR-EDGH 252
Cdd:cd14049  82 LyiqMQLCelSLWDWIVERNKRP--CEEEFKSAPYTpvdvdvttkilQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 253 IMLSDFDLslqsfvsptliqstsqpschiasyciqppcidpSCKLPVACIQPScfkprfLNNKPRKAKTEKAGsdslpml 332
Cdd:cd14049 160 VRIGDFGL---------------------------------ACPDILQDGNDS------TTMSRLNGLTHTSG------- 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 333 iaeptaarsmsfVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLtgkTPFKGNGNR-ETLFNVVGQplKFPEgsiSFA 411
Cdd:cd14049 194 ------------VGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPFGTEMERaEVLTQLRNG--QIPK---SLC 253
                       330       340
                ....*....|....*....|.
gi 15242554 412 AK-----DLIRGLLTKDPKKR 427
Cdd:cd14049 254 KRwpvqaKYIKLLTSTEPSER 274
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
160-256 3.57e-05

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: 45.70  E-value: 3.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 160 QTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRD 239
Cdd:cd08227  47 QGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRS 126
                        90
                ....*....|....*..
gi 15242554 240 LKPENVMVREDGHIMLS 256
Cdd:cd08227 127 VKASHILISVDGKVYLS 143
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
114-442 3.77e-05

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: 45.23  E-value: 3.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKL---VRAQTEREILGLL----DHPFLPTLYSHFET-EK 185
Cdd:cd14101   2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLpgvNPVPNEVALLQSVgggpGHRGVIRLLDWFEIpEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLMEFCSGGDL-HILRQKQPgkhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVR-EDGHIMLSDFdlslq 263
Cdd:cd14101  82 FLLVLERPQHCQDLfDYITERGA---LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDF----- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 264 sfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekaGSDSLpmLIAEPTAarsmS 343
Cdd:cd14101 154 -------------------------------------------------------------GSGAT--LKDSMYT----D 166
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 344 FVGTHEYLAPE-IIRGDGHGSSVDWWTFGIFLYELLTGKTPFKgngnRETlfNVVGQPLKFPEgSISFAAKDLIRGLLTK 422
Cdd:cd14101 167 FDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPFE----RDT--DILKAKPSFNK-RVSNDCRSLIRSCLAY 239
                       330       340
                ....*....|....*....|
gi 15242554 423 DPKKRLGFKkgatEIKQHPF 442
Cdd:cd14101 240 NPSDRPSLE----QILLHPW 255
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
120-384 3.91e-05

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: 45.18  E-value: 3.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAelremgcffamkVMDKGMLIGRKKLVRA---------QTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd14664   1 IGRGGAGTVYKG------------VMPNGTLVAVKRLKGEgtqggdhgfQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDL-HILRQKQPGKHFSELAARF-YASEVLLALEYLH---MMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsf 265
Cdd:cd14664  69 YEYMPNGSLgELLHSRPESQPPLDWETRQrIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLA---- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 266 vspTLIQstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaePTAARSMSFV 345
Cdd:cd14664 145 ---KLMD---------------------------------------------------------------DKDSHVMSSV 158
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15242554 346 -GTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPF 384
Cdd:cd14664 159 aGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
120-378 4.62e-05

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: 45.17  E-value: 4.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMGcffamKVMDKGMLI---GRKKLVRaqtEREILGLLDHP----FLPTLYShfetEKFSCLLME 192
Cdd:cd14065   1 LGKGFFGEVYKVTHRETG-----KVMVMKELKrfdEQRSFLK---EVKLMRRLSHPnilrFIGVCVK----DNKLNFITE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 193 FCSGGDLHILrQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDG---HIMLSDFDLSlqsfvspt 269
Cdd:cd14065  69 YVNGGTLEEL-LKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANrgrNAVVADFGLA-------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 270 liqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEKAGsdslpmliaEPTAARSMSFVGTHE 349
Cdd:cd14065 140 -----------------------------------------------REMPDEKTK---------KPDRKKRLTVVGSPY 163
                       250       260
                ....*....|....*....|....*....
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELL 378
Cdd:cd14065 164 WMAPEMLRGESYDEKVDVFSFGIVLCEII 192
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
113-261 4.71e-05

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: 45.35  E-value: 4.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREMGCFFAM---KVMDKGMLIGRKKLVRAQT---------EREILGLLDHPFLPTLYSH 180
Cdd:cd05097   6 QLRLKEKLGEGQFGEVHLCEAEGLAEFLGEgapEFDGQPVLVAVKMLRADVTktarndflkEIKIMSRLKNPNIIRLLGV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 181 FETEKFSCLLMEFCSGGDLH-ILRQKQ-----------PGKHFSELAarFYASEVLLALEYLHMMGVVYRDLKPENVMVR 248
Cdd:cd05097  86 CVSDDPLCMITEYMENGDLNqFLSQREiestfthanniPSVSIANLL--YMAVQIASGMKYLASLNFVHRDLATRNCLVG 163
                       170
                ....*....|...
gi 15242554 249 EDGHIMLSDFDLS 261
Cdd:cd05097 164 NHYTIKIADFGMS 176
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
118-263 5.33e-05

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: 44.92  E-value: 5.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSGG 197
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKA--KFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 198 D-LHILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQ 263
Cdd:cd05084  80 DfLTFLRTEGPRLKVKELIR--MVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE 144
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
115-396 5.40e-05

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 45.09  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAeLREMGCFFAMKVMDKGMLIGRKKLVRAQtereILGLLDHPFLPTLYS--------HFETEkf 186
Cdd:cd05068  11 KLLRKLGSGQFGEVWEG-LWNNTTPVAVKTLKPGTMDPEDFLREAQ----IMKKLRHPKLIQLYAvctleepiYIITE-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 sclLMefCSGGDLHILRQKQPGKHFSELAArfYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfv 266
Cdd:cd05068  84 ---LM--KHGSLLEYLQGKGRSLQLPQLID--MAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLA----- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 267 spTLIQSTSQPSCHIASyciqppcidpscKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsmsfvg 346
Cdd:cd05068 152 --RVIKVEDEYEAREGA------------KFPI----------------------------------------------- 170
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 347 thEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNV 396
Cdd:cd05068 171 --KWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQV 219
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
114-276 5.52e-05

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: 45.40  E-value: 5.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklvrAQTEREILGLL-----DHPFLPTLYSHFETEKFSC 188
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQ----GQIEVGILARLsnenaDEFNFVRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHILRQKQpgkhFSEL---AARFYASEVLLALEYLHMMGVVYRDLKPENVM----VREDGHIMLSDFDLS 261
Cdd:cd14229  78 LVFEMLEQNLYDFLKQNK----FSPLplkVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSA 153
                       170
                ....*....|....*
gi 15242554 262 lqSFVSPTLIQSTSQ 276
Cdd:cd14229 154 --SHVSKTVCSTYLQ 166
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
222-258 5.61e-05

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 45.45  E-value: 5.61e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15242554  222 EVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:PLN03224 317 QVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDF 353
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
163-271 5.67e-05

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: 45.16  E-value: 5.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 163 REI--LGLLDHP--------FLPT-------LYSHFEtekfsclLMEfcsgGDLHilrqkQPGKHFSELAA---RFYASE 222
Cdd:cd07859  48 REIklLRLLRHPdiveikhiMLPPsrrefkdIYVVFE-------LME----SDLH-----QVIKANDDLTPehhQFFLYQ 111
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15242554 223 VLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSLQSFV-SPTLI 271
Cdd:cd07859 112 LLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNdTPTAI 161
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
116-261 6.31e-05

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 44.47  E-value: 6.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMgcffaMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCS 195
Cdd:cd05114   8 FMKELGSGLFGVVRLGKWRAQ-----YKVAIKAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFME 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 196 GGDL-HILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05114  83 NGCLlNYLRQRR--GKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT 147
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
115-396 6.91e-05

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: 44.47  E-value: 6.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELREMG---CFFAMKVMDKGMLigRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd05066   7 KIEKVIGAGEFGEVCSGRLKLPGkreIPVAIKTLKAGYT--EKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 192 EFCSGGDLHILRQKQPGkHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptli 271
Cdd:cd05066  85 EYMENGSLDAFLRKHDG-QFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLS---------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 272 qstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTEKAGsdSLPMliaeptaarsmsfvgthEYL 351
Cdd:cd05066 154 --------------------------------------RVLEDDPEAAYTTRGG--KIPI-----------------RWT 176
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 352 APEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNV 396
Cdd:cd05066 177 APEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEMSNQDVIKAI 222
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
119-431 9.50e-05

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: 44.19  E-value: 9.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAElremgCFFAMKVMDKgMLIGRKKLVRA--------QTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05092  12 ELGEGAFGKVFLAE-----CHNLLPEQDK-MLVAVKALKEAtesarqdfQREAELLTVLQHQHIVRFYGVCTEGEPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH-ILRQKQPGKHF---SELAA---------RFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSD 257
Cdd:cd05092  86 FEYMRHGDLNrFLRSHGPDAKIldgGEGQApgqltlgqmLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGD 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 258 FDLSLQsfvsptlIQSTSQpschiasYCIqppcidpscklpvaciqpscfkprflnnkprkaktekAGSDSLPMliaept 337
Cdd:cd05092 166 FGMSRD-------IYSTDY-------YRV-------------------------------------GGRTMLPI------ 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 aarsmsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLKFPEGSISfAAKDL 415
Cdd:cd05092 189 -----------RWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITqGRELERPRTCPP-EVYAI 256
                       330
                ....*....|....*.
gi 15242554 416 IRGLLTKDPKKRLGFK 431
Cdd:cd05092 257 MQGCWQREPQQRHSIK 272
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
120-404 9.54e-05

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 44.09  E-value: 9.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 120 LGCGDIGSVYLAELREMG---CFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEFCSG 196
Cdd:cd05065  12 IGAGEFGEVCRGRLKLPGkreIFVAIKTLKSGYTEKQRR--DFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMEN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 197 GDL-HILRQKQpgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsptliqsts 275
Cdd:cd05065  90 GALdSFLRQND--GQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLS-------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 qpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPrkaktekagsdslpmliAEPTAARSMSFVGTHEYLAPEI 355
Cdd:cd05065 154 ----------------------------------RFLEDDT-----------------SDPTYTSSLGGKIPIRWTAPEA 182
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15242554 356 IRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLfNVVGQPLKFP 404
Cdd:cd05065 183 IAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDVI-NAIEQDYRLP 231
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
117-261 9.59e-05

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 44.17  E-value: 9.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 117 LKKLGCGDIGSVYLAELreMGCFFAMKVMDK------GMLIGRKKLVRAQTEREilglLDHP-FLPTLYSHFETEKFsCL 189
Cdd:cd14206   2 LQEIGNGWFGKVILGEI--FSDYTPAQVVVKelrvsaGPLEQRKFISEAQPYRS----LQHPnILQCLGLCTETIPF-LL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDL-HILRQKQPGKHFS-ELAAR------FYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd14206  75 IMEFCQLGDLkRYLRAQRKADGMTpDLPTRdlrtlqRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS 154
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
115-261 9.62e-05

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 44.29  E-value: 9.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 115 RLLKKLGCGDIGSVYLAELREMG---CFFAMKVMDKGMliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLM 191
Cdd:cd05033   7 TIEKVIGGGEFGEVCSGSLKLPGkkeIDVAIKTLKSGY--SDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVT 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 192 EFCSGGDL-HILRQKQPGKHFSELAARFYAseVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05033  85 EYMENGSLdKFLRENDGKFTVTQLVGMLRG--IASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLS 153
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
109-432 1.02e-04

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: 44.09  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 109 LGLGHFRLLKKLGCGDIGSVYLAELreMGCFFAMK----------------VMDKgmlIGRKKLVRaqtereILGLLDHP 172
Cdd:cd05083   3 LNLQKLTLGEIIGEGEFGAVLQGEY--MGQKVAVKnikcdvtaqafleetaVMTK---LQHKNLVR------LLGVILHN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 173 FLptlyshfetekfsCLLMEFCSGGDL-HILRQKqpGKHFSELAARF-YASEVLLALEYLHMMGVVYRDLKPENVMVRED 250
Cdd:cd05083  72 GL-------------YIVMELMSKGNLvNFLRSR--GRALVPVIQLLqFSLDVAEGMEYLESKKLVHRDLAARNILVSED 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 251 GHIMLSDFDLSLqsfvsptliqstsqpschiasycIQPPCIDPScKLPVaciqpscfkprflnnkprkaktekagsdslp 330
Cdd:cd05083 137 GVAKISDFGLAK-----------------------VGSMGVDNS-RLPV------------------------------- 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 331 mliaeptaarsmsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNV-VGQPLKFPEGSI 408
Cdd:cd05083 162 ------------------KWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAVeKGYRMEPPEGCP 223
                       330       340
                ....*....|....*....|....
gi 15242554 409 SfAAKDLIRGLLTKDPKKRLGFKK 432
Cdd:cd05083 224 P-DVYSIMTSCWEAEPGKRPSFKK 246
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
188-387 1.32e-04

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: 43.80  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDLH-ILRQKQPGKHFSELAARF---YASEVLLALEYLHMMGVVYRDLKPENVMV-----REDGHIMLSDF 258
Cdd:cd14067  84 CFALELAPLGSLNtVLEENHKGSSFMPLGHMLtfkIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDY 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLQSFvsptliqstsqpscHIASYCIQppcidpscklpvaciqpscfkprflnnkprkaktekagsdslpmliaepta 338
Cdd:cd14067 164 GISRQSF--------------HEGALGVE--------------------------------------------------- 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15242554 339 arsmsfvGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGN 387
Cdd:cd14067 179 -------GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGH 220
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
111-444 1.40e-04

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: 43.92  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 111 LGHFRLLKKLGCGDIGSVylaelremgCFFAMKVMDKGMLIgrKKLVR----------AQTEREILGLLDHPFLPTLYSH 180
Cdd:cd07874  16 LKRYQNLKPIGSGAQGIV---------CAAYDAVLDRNVAI--KKLSRpfqnqthakrAYRELVLMKCVNHKNIISLLNV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 181 FETEKF------SCLLMEFCSGGDLHILRQKQPGKHFSELaarFYasEVLLALEYLHMMGVVYRDLKPENVMVREDGHIM 254
Cdd:cd07874  85 FTPQKSleefqdVYLVMELMDANLCQVIQMELDHERMSYL---LY--QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 255 LSDFDLSlqsfvsptliqstsqpschiasyciqppcidpscklpvaciqpscfkprflnnkpRKAKTEkagsdslpmLIA 334
Cdd:cd07874 160 ILDFGLA-------------------------------------------------------RTAGTS---------FMM 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 335 EPtaarsmsFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQ--------------- 399
Cdd:cd07874 176 TP-------YVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQlgtpcpefmkklqpt 248
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 400 ----------------PLKFPEGSI----------SFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFN 444
Cdd:cd07874 249 vrnyvenrpkyagltfPKLFPDSLFpadsehnklkASQARDLLSKMLVIDPAKRI----SVDEALQHPYIN 315
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
119-261 1.41e-04

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 43.56  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 119 KLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKKLVRAQTEREIlgllDHPFLPTLYSHFETEKFSCLLMEFCSGGD 198
Cdd:cd05052  13 KLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEI----KHPNLVQLLGVCTREPPFYIITEFMPYGN 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242554 199 L-HILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05052  89 LlDYLRECNREE-LNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLS 151
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
189-260 1.66e-04

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 43.42  E-value: 1.66e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242554 189 LLMEFCSGGDLHILrQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVrEDGHIMLSDFDL 260
Cdd:cd14152  73 IITSFCKGRTLYSF-VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGL 142
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
222-258 1.73e-04

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 43.58  E-value: 1.73e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15242554 222 EVLLALEYLHMMGVVYRDLKPENVMVRE-DGHIMLSDF 258
Cdd:cd14013 128 QILVALRKLHSTGIVHRDVKPQNIIVSEgDGQFKIIDL 165
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
217-258 1.77e-04

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: 43.40  E-value: 1.77e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15242554 217 RFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd13980 100 KWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDF 141
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
112-393 1.90e-04

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 43.42  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMG---CFFAMKVMDKGMLigRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSC 188
Cdd:cd05063   5 SHITKQKVIGAGEFGEVFRGILKMPGrkeVAVAIKTLKPGYT--EKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 189 LLMEFCSGGDLHILRQKQPGKhFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvsp 268
Cdd:cd05063  83 IITEYMENGALDKYLRDHDGE-FSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLS------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 269 tliqstsqpschiasyciqppcidpscklpvaciqpscfkpRFLNNKPRKAKTEKAGsdSLPMliaeptaarsmsfvgth 348
Cdd:cd05063 155 -----------------------------------------RVLEDDPEGTYTTSGG--KIPI----------------- 174
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL 393
Cdd:cd05063 175 RWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVM 220
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
116-261 1.93e-04

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: 43.17  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMGCffamkVMDKGMLIGRKKLVRAQTEREILGLLdhpflptlySHFETEKF--------- 186
Cdd:cd05053  16 LGKPLGEGAFGQVVKAEAVGLDN-----KPNEVVTVAVKMLKDDATEKDLSDLV---------SEMEMMKMigkhkniin 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 187 ---SC-------LLMEFCSGGDLH-ILRQKQP-GKHFSELAARF------------YASEVLLALEYLHMMGVVYRDLKP 242
Cdd:cd05053  82 llgACtqdgplyVVVEYASKGNLReFLRARRPpGEEASPDDPRVpeeqltqkdlvsFAYQVARGMEYLASKKCIHRDLAA 161
                       170
                ....*....|....*....
gi 15242554 243 ENVMVREDGHIMLSDFDLS 261
Cdd:cd05053 162 RNVLVTEDNVMKIADFGLA 180
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
116-256 2.57e-04

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: 43.32  E-value: 2.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCG--DIGSVYLAELREMGCFFAMKVMDKGMlIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEF 193
Cdd:cd08226   2 LQVELGKGfcNLTSVYLARHTPTGTLVTVKITNLDN-CSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPF 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242554 194 CS-GGDLHILRQKQPgKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLS 256
Cdd:cd08226  81 MAyGSARGLLKTYFP-EGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLS 143
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
116-431 2.64e-04

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 42.75  E-value: 2.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREmGCFFAMKVMDKGMLIGRKKLVRAQtereILGLLDHPFLPTLYSHFETEKFScLLMEFCS 195
Cdd:cd05070  13 LIKRLGNGQFGEVWMGTWNG-NTKVAIKTLKPGTMSPESFLEEAQ----IMKKLKHDKLVQLYAVVSEEPIY-IVTEYMS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 196 GGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLSlqsfvspTLIQSTS 275
Cdd:cd05070  87 KGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLA-------RLIEDNE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 276 QpschiasyciqppcidpscklpvaciqpscfkprflnnkprkakTEKAGSdSLPMLIAEPTAARSMSFVgtheylapei 355
Cdd:cd05070 160 Y--------------------------------------------TARQGA-KFPIKWTAPEAALYGRFT---------- 184
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 356 IRGDghgssvdWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLKFPEgSISFAAKDLIRGLLTKDPKKRLGFK 431
Cdd:cd05070 185 IKSD-------VWSFGILLTELVTkGRVPYPGMNNREVLEQVErGYRMPCPQ-DCPISLHELMIHCWKKDPEERPTFE 254
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
114-386 2.78e-04

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: 43.15  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklvrAQTEREILGLL------DHPFLPTlYSHFETEKFS 187
Cdd:cd14227  17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQ----GQIEVSILARLstesadDYNFVRA-YECFQHKNHT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 188 CLLMEFCSGGDLHILRQKQpgkhFSELAARF---YASEVLLALEYLHMMGVVYRDLKPENVMVredghimlsdfdlslqs 264
Cdd:cd14227  92 CLVFEMLEQNLYDFLKQNK----FSPLPLKYirpILQQVATALMKLKSLGLIHADLKPENIML----------------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 265 fvsptliqstsqpschiasyciqppcIDPScklpvaciqpscfkprflnNKPRKAKTEKAGSDSlpmliaEPTAARSMSF 344
Cdd:cd14227 151 --------------------------VDPS-------------------RQPYRVKVIDFGSAS------HVSKAVCSTY 179
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15242554 345 VGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKG 386
Cdd:cd14227 180 LQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPG 221
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
114-261 2.80e-04

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 42.80  E-value: 2.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVmdKGMligRKKLVRAQTEREILGLLDHPF-LPTLYSHFETEKFSCLLME 192
Cdd:cd14126   2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKL--EPM---KSRAPQLHLEYRFYKLLGQAEgLPQVYYFGPCGKYNAMVLE 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 193 FC--SGGDLHILrqkqPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGH-----IMLSDFDLS 261
Cdd:cd14126  77 LLgpSLEDLFDL----CDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTkkqhvIHIIDFGLA 148
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
112-261 2.82e-04

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: 42.79  E-value: 2.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVY----LAELREMGCFFAMKVMDKGMliGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKFs 187
Cdd:cd05057   7 TELEKGKVLGSGAFGTVYkgvwIPEGEKVKIPVAIKVLREET--GPKANEEILDEAYVMASVDHPHLVRLLGICLSSQV- 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 188 CLLMEFCSGGDL-HILRQkqpgkHFSELAARF---YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05057  84 QLITQLMPLGCLlDYVRN-----HRDNIGSQLllnWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLA 156
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
121-277 3.15e-04

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: 42.81  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 121 GCGDIGSVYLAELreMGCFFAMKVMDKGmliGRKKLvraQTEREILG--LLDHP----FLPTLYSHFETEKFSCLLMEFC 194
Cdd:cd13998   4 GKGRFGEVWKASL--KNEPVAVKIFSSR---DKQSW---FREKEIYRtpMLKHEnilqFIAADERDTALRTELWLVTAFH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 195 SGGDL------HILrQKQPGKHFSELAARfyasevllALEYLHM---------MGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd13998  76 PNGSL*dylslHTI-DWVSLCRLALSVAR--------GLAHLHSeipgctqgkPAIAHRDLKSKNILVKNDGTCCIADFG 146
                       170
                ....*....|....*...
gi 15242554 260 LSLqsfvspTLIQSTSQP 277
Cdd:cd13998 147 LAV------RLSPSTGEE 158
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
118-261 3.20e-04

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 42.33  E-value: 3.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 118 KKLGCGDIGSVYLAE-LREMGCFF--AMKVMDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYSHFETEKfscLLM--E 192
Cdd:cd05040   1 EKLGDGSFGVVRRGEwTTPSGKVIqvAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSP---LMMvtE 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 193 FCSGGDLhILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05040  78 LAPLGSL-LDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLM 145
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
168-258 3.90e-04

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 42.10  E-value: 3.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 168 LLDHPFL--PTLYSHFETEKfsCLLMEFCSGGDL-HILRQKQPGKHFSELAARfyasevlLALEYLHMM---GVVYRDLK 241
Cdd:cd05121 127 LKDSPDVyvPKVYPELSTRR--VLVMEYIDGVKLtDLEALRAAGIDRKELARR-------LVDAYLKQIfedGFFHADPH 197
                        90
                ....*....|....*..
gi 15242554 242 PENVMVREDGHIMLSDF 258
Cdd:cd05121 198 PGNILVLPDGRIALLDF 214
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
340-378 3.95e-04

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: 42.12  E-value: 3.95e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 15242554 340 RSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELL 378
Cdd:cd14156 152 RKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
146-263 4.25e-04

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 42.23  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 146 DKGMLIGRKKLVRAQTEREILglldhpflpTLYSHFeTEKFS------CLLMEFCSGGDLHILRQKQPGKHfSELAARFY 219
Cdd:cd14020  47 DYGFAKERAALEQLQGHRNIV---------TLYGVF-TNHYSanvpsrCLLLELLDVSVSELLLRSSNQGC-SMWMIQHC 115
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15242554 220 ASEVLLALEYLHMMGVVYRDLKPENVM-VREDGHIMLSDFDLSLQ 263
Cdd:cd14020 116 ARDVLEALAFLHHEGYVHADLKPRNILwSAEDECFKLIDFGLSFK 160
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
114-430 4.33e-04

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 42.21  E-value: 4.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELR-EMGCFFAMKV-MDKGMLIGRKKLVRAQTEREILGLLDHPFLPTLYS---HFETEK--- 185
Cdd:cd05074  11 FTLGRMLGKGEFGSVREAQLKsEDGSFQKVAVkMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGvslRSRAKGrlp 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 186 FSCLLMEFCSGGDLH--ILRQKQPGKHFS---ELAARFYAsEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDL 260
Cdd:cd05074  91 IPMVILPFMKHGDLHtfLLMSRIGEEPFTlplQTLVRFMI-DIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 261 SLQSFVSPTLIQSTSQpschiasyciqppcidpscKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaar 340
Cdd:cd05074 170 SKKIYSGDYYRQGCAS-------------------KLPV----------------------------------------- 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 341 smsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL-FNVVGQPLKFPEGSISfAAKDLIRG 418
Cdd:cd05074 190 --------KWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYnYLIKGNRLKQPPDCLE-DVYELMCQ 260
                       330
                ....*....|..
gi 15242554 419 LLTKDPKKRLGF 430
Cdd:cd05074 261 CWSPEPKCRPSF 272
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
116-431 4.62e-04

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 42.07  E-value: 4.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREM-----GCFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05049   9 LKRELGEGAFGKVFLGECYNLepeqdKMLVAVKTLKDASSPDARK--DFEREAELLTNLQHENIVKFYGVCTEGDPLLMV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH-ILRQKQPGKHF--SELAARF---------YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd05049  87 FEYMEHGDLNkFLRSHGPDAAFlaSEDSAPGeltlsqllhIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 259 DLSLQsfvsptlIQSTSQpschiasYCIqppcidpscklpvaciqpscfkprflnnkprkaktekAGSDSLPMliaepta 338
Cdd:cd05049 167 GMSRD-------IYSTDY-------YRV-------------------------------------GGHTMLPI------- 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 339 aRSMSfvgtheylaPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETL-FNVVGQPLKFPEGSISfAAKDLI 416
Cdd:cd05049 189 -RWMP---------PESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEVIeCITQGRLLQRPRTCPS-EVYAVM 257
                       330
                ....*....|....*
gi 15242554 417 RGLLTKDPKKRLGFK 431
Cdd:cd05049 258 LGCWKREPQQRLNIK 272
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
189-258 4.86e-04

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: 42.11  E-value: 4.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242554 189 LLMEFCSGGDLHILRQKQPGKHFS--ELAARFYasEVLLALEYLHMMG--VVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd14036  83 LLTELCKGQLVDFVKKVEAPGPFSpdTVLKIFY--QTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDF 154
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
190-261 4.87e-04

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: 42.16  E-value: 4.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 190 LMEFCSGGDLH---ILRQKQPGKHFSelaarfYASEVLLALEYLHMMGVVYRDLKPENVMV---REDGHIMLSDFDLS 261
Cdd:cd13977 113 VMEFCDGGDMNeylLSRRPDRQTNTS------FMLQLSSALAFLHRNQIVHRDLKPDNILIshkRGEPILKVADFGLS 184
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
112-430 4.92e-04

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 42.13  E-value: 4.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAelREMG-------CFFAMKVMDKGMLIGRKKlvRAQTEREILGLLDHPFLPTLYSHFETE 184
Cdd:cd05050   5 NNIEYVRDIGQGAFGRVFQA--RAPGllpyepfTMVAVKMLKEEASADMQA--DFQREAALMAEFDHPNIVKLLGVCAVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 185 KFSCLLMEFCSGGDLH-ILRQKQPGKHFS----ELAARFY---------------ASEVLLALEYLHMMGVVYRDLKPEN 244
Cdd:cd05050  81 KPMCLLFEYMAYGDLNeFLRHRSPRAQCSlshsTSSARKCglnplplscteqlciAKQVAAGMAYLSERKFVHRDLATRN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 245 VMVREDGHIMLSDFDLSLQSFVsptliqstsqpschiASYCiqppcidpscklpvaciqpscfkprflnnkprKAktekA 324
Cdd:cd05050 161 CLVGENMVVKIADFGLSRNIYS---------------ADYY--------------------------------KA----S 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 325 GSDSLPMliaeptaarsmsfvgthEYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNRETLFNVV-GQPLK 402
Cdd:cd05050 190 ENDAIPI-----------------RWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAHEEVIYYVRdGNVLS 252
                       330       340
                ....*....|....*....|....*...
gi 15242554 403 FPEGSISfAAKDLIRGLLTKDPKKRLGF 430
Cdd:cd05050 253 CPDNCPL-ELYNLMRLCWSKLPSDRPSF 279
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
154-443 5.00e-04

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: 42.02  E-value: 5.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 154 KKLVRAQTER-----EILGLLDHPFLPTLYSHFET----EKFSCLLMEFCSGGDLHILRQKqpGKHFSELAARFYASEVL 224
Cdd:cd14031  46 RKLTKAEQQRfkeeaEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMTSGTLKTYLKR--FKVMKPKVLRSWCRQIL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 225 LALEYLHMMG--VVYRDLKPENVMVR-EDGHIMLSDFDLSlqsfvspTLIQSTSqpschiasyciqppcidpscklpvac 301
Cdd:cd14031 124 KGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA-------TLMRTSF-------------------------- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 302 iqpscfkprflnnkprkaktekagsdslpmliaeptaarSMSFVGTHEYLAPEIIRgDGHGSSVDWWTFGIFLYELLTGK 381
Cdd:cd14031 171 ---------------------------------------AKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSE 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 382 TPFKGNGNRETLFNVVG---QPLKF-----PEgsisfaAKDLIRGLLTKDPKKRLGFKkgatEIKQHPFF 443
Cdd:cd14031 211 YPYSECQNAAQIYRKVTsgiKPASFnkvtdPE------VKEIIEGCIRQNKSERLSIK----DLLNHAFF 270
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
162-258 5.18e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 42.57  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  162 EREILGLLDHP-FLPTLYSHfETEKFSCLLM-EFCSggDLHILRQKQPgKHFSELAARFYASEVLLALEYLHMMGVVYRD 239
Cdd:PHA03211 210 EARLLRRLSHPaVLALLDVR-VVGGLTCLVLpKYRS--DLYTYLGARL-RPLGLAQVTAVARQLLSAIDYIHGEGIIHRD 285
                         90
                 ....*....|....*....
gi 15242554  240 LKPENVMVREDGHIMLSDF 258
Cdd:PHA03211 286 IKTENVLVNGPEDICLGDF 304
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
162-261 5.22e-04

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 42.02  E-value: 5.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 162 EREILGLLDHPFLPTLYShFETEKFSCLLMEFCSGGDL-HILRQKQPGKHFSELAarFYASEVLLALEYLHMMGVVYRDL 240
Cdd:cd05056  57 EAYIMRQFDHPHIVKLIG-VITENPVWIVMELAPLGELrSYLQVNKYSLDLASLI--LYAYQLSTALAYLESKRFVHRDI 133
                        90       100
                ....*....|....*....|.
gi 15242554 241 KPENVMVREDGHIMLSDFDLS 261
Cdd:cd05056 134 AARNVLVSSPDCVKLGDFGLS 154
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
223-405 5.25e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.52  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  223 VLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFdlslqsfvsptliqstsqpschiasyciqppciDPSCKLPVACI 302
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDF---------------------------------GAACKLDAHPD 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  303 QPSCFkprflnnkprkaktekagsdslpmliaeptaarsmSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKT 382
Cdd:PHA03207 241 TPQCY-----------------------------------GWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNV 285
                        170       180       190
                 ....*....|....*....|....*....|
gi 15242554  383 PFKG---NGNRETLFNVVG----QPLKFPE 405
Cdd:PHA03207 286 TLFGkqvKSSSSQLRSIIRcmqvHPLEFPQ 315
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
112-380 5.37e-04

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: 42.18  E-value: 5.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 112 GHFRLLKKLGCGDIGSVYLAELREMGCFFAMKV-----------MDKGMLIGRKKLV--RAQTEREILGLLDHpflptlY 178
Cdd:cd14136  10 GRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVvksaqhyteaaLDEIKLLKCVREAdpKDPGREHVVQLLDD------F 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 179 SHF-ETEKFSCLLMEFcsGGD--LHILRQ-----------KQPGKHfselaarfyaseVLLALEYLH-MMGVVYRDLKPE 243
Cdd:cd14136  84 KHTgPNGTHVCMVFEV--LGPnlLKLIKRynyrgiplplvKKIARQ------------VLQGLDYLHtKCGIIHTDIKPE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 244 NVMVredghimlsdfdlslqsfvsptliqSTSQPSCHIASyciqppcidpsckLPVACIqpscfkprflnnkprkakTEK 323
Cdd:cd14136 150 NVLL-------------------------CISKIEVKIAD-------------LGNACW------------------TDK 173
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242554 324 AGSDSlpmliaeptaarsmsfVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTG 380
Cdd:cd14136 174 HFTED----------------IQTRQYRSPEVILGAGYGTPADIWSTACMAFELATG 214
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
366-396 6.33e-04

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


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 41.50  E-value: 6.33e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 15242554 366 DWWTFGIFLYELLT-GKTPFKGNGNRETLFNV 396
Cdd:cd05034 175 DVWSFGILLYEIVTyGRVPYPGMTNREVLEQV 206
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
114-261 8.82e-04

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 41.21  E-value: 8.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMgCFFAMKVMDKGMLIGRKKLVRAQTEREilglLDHPFLPTLYSHFETEKFScLLMEF 193
Cdd:cd05071  11 LRLEVKLGQGCFGEVWMGTWNGT-TRVAIKTLKPGTMSPEAFLQEAQVMKK----LRHEKLVQLYAVVSEEPIY-IVTEY 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 194 CSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05071  85 MSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLA 152
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
350-430 9.93e-04

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


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 40.93  E-value: 9.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 350 YLAPEIIR---GDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVGQPLK--FPEGSISFAAKdLIRGLLTKDP 424
Cdd:cd14057 157 WMAPEALQkkpEDINRRSADMWSFAILLWELVTREVPFADLSNMEIGMKIALEGLRvtIPPGISPHMCK-LMKICMNEDP 235

                ....*.
gi 15242554 425 KKRLGF 430
Cdd:cd14057 236 GKRPKF 241
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
349-439 1.04e-03

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 41.10  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 349 EYLAPEIIRGDGHGSSVDWWTFGIFLYELLT-GKTPFKGNGNrETLFNVV--GQPLKFPEgSISFAAKDLIRGLLTKDPK 425
Cdd:cd05045 194 KWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAP-ERLFNLLktGYRMERPE-NCSEEMYNLMLTCWKQEPD 271
                        90
                ....*....|....
gi 15242554 426 KRLGFKKGATEIKQ 439
Cdd:cd05045 272 KRPTFADISKELEK 285
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
160-263 1.04e-03

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: 41.19  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 160 QTEREI--LGLLDHPFLPTLYSHFE-------TEKFscLLMEFCSGGDL-HILRQkqpgkHFSELA-ARFYASEVLLALE 228
Cdd:cd14054  35 QNEKDIyeLPLMEHSNILRFIGADErptadgrMEYL--LVLEYAPKGSLcSYLRE-----NTLDWMsSCRMALSLTRGLA 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15242554 229 YLHMM---------GVVYRDLKPENVMVREDGHIMLSDFDLSLQ 263
Cdd:cd14054 108 YLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMV 151
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
337-394 1.19e-03

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: 40.96  E-value: 1.19e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 337 TAARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLF 394
Cdd:cd14159 158 TLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTKY 215
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
217-443 1.25e-03

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: 41.15  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 217 RFYASEVLLALEYLHMMGVVYRDLKPENVMvredghIMLSDFDLSLQSfvsptliqstsqpschiasyciqppcidpsck 296
Cdd:cd14214 120 RHMAYQLCHALKFLHENQLTHTDLKPENIL------FVNSEFDTLYNE-------------------------------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 297 lpvaciQPSCFKPRFLNNKPRKAKTEKAGSDSlpmliaeptaARSMSFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYE 376
Cdd:cd14214 162 ------SKSCEEKSVKNTSIRVADFGSATFDH----------EHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFE 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 377 LLTGKTPFKGNGNRETLF---NVVGqPLK------------FPEGSISFAAK---------------------------- 413
Cdd:cd14214 226 YYRGFTLFQTHENREHLVmmeKILG-PIPshmihrtrkqkyFYKGSLVWDENssdgryvsenckplmsymlgdslehtql 304
                       250       260       270
                ....*....|....*....|....*....|.
gi 15242554 414 -DLIRGLLTKDPKKRLGFKkgatEIKQHPFF 443
Cdd:cd14214 305 fDLLRRMLEFDPALRITLK----EALLHPFF 331
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
114-258 1.33e-03

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: 40.84  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVMDKGMLIGRKklvrAQTEREILGLL------DHPFLPTlYSHFETEKFS 187
Cdd:cd14228  17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQ----GQIEVSILSRLssenadEYNFVRS-YECFQHKNHT 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242554 188 CLLMEFCSGGDLHILRQKQpgkhFSELAARFYA---SEVLLALEYLHMMGVVYRDLKPENVM----VREDGHIMLSDF 258
Cdd:cd14228  92 CLVFEMLEQNLYDFLKQNK----FSPLPLKYIRpilQQVATALMKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDF 165
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
213-385 1.60e-03

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: 40.32  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 213 ELAARFYAsEVLLALEYLHMMGVVYRDLKPENVMVRedghimLSDFDLSLQSFVSPTLIQSTSQpschiasyciqppcid 292
Cdd:cd14102 105 DTARGFFR-QVLEAVRHCYSCGVVHRDIKDENLLVD------LRTGELKLIDFGSGALLKDTVY---------------- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 293 pscklpvaciqpscfkprflnnkprkaktekagsdslpmliaeptaarsMSFVGTHEYLAPEIIRGDG-HGSSVDWWTFG 371
Cdd:cd14102 162 -------------------------------------------------TDFDGTRVYSPPEWIRYHRyHGRSATVWSLG 192
                       170
                ....*....|....
gi 15242554 372 IFLYELLTGKTPFK 385
Cdd:cd14102 193 VLLYDMVCGDIPFE 206
Keratin_B2_2 pfam13885
Keratin, high sulfur B2 protein;
267-309 1.85e-03

Keratin, high sulfur B2 protein;


Pssm-ID: 464017 [Multi-domain]  Cd Length: 45  Bit Score: 36.21  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15242554   267 SPTLIQSTS-QPSCHIASYCiQPPCIDPSCKLPVACiQPSCFKP 309
Cdd:pfam13885   3 QPSCCQPSCcQPSCCQPSCC-QPSCCQPSCCRPSCC-RSSCCQP 44
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
114-258 1.90e-03

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: 40.31  E-value: 1.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYLAELREMGCFFAMKVmdkgmlIGRKK--LVRAQTEREILGLLDHPFLPT-------LYSHFETE 184
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKV------LKNKPayFRQAMLEIAILTLLNTKYDPEdkhhivrLLDHFMHH 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242554 185 KFSCLLMEfCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENV-MVRED-GHIMLSDF 258
Cdd:cd14212  75 GHLCIVFE-LLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENIlLVNLDsPEIKLIDF 149
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
113-261 1.92e-03

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 40.40  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 113 HFRLLKKLGCGDIGSVYLAELREM-----GCFFAMKVMDKGMLIGRKKL-------VRAQTERE--ILGLLDHPFLPTLY 178
Cdd:cd05051   6 KLEFVEKLGEGQFGEVHLCEANGLsdltsDDFIGNDNKDEPVLVAVKMLrpdasknAREDFLKEvkIMSQLKDPNIVRLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 179 SHFETEKFSCLLMEFCSGGDLH-ILRQKQP--------GKHFSELAARFY-ASEVLLALEYLHMMGVVYRDLKPENVMVR 248
Cdd:cd05051  86 GVCTRDEPLCMIVEYMENGDLNqFLQKHEAetqgasatNSKTLSYGTLLYmATQIASGMKYLESLNFVHRDLATRNCLVG 165
                       170
                ....*....|...
gi 15242554 249 EDGHIMLSDFDLS 261
Cdd:cd05051 166 PNYTIKIADFGMS 178
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
114-261 2.23e-03

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 40.05  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVY----LAELREMGCFFAMKVMDKgmLIGRKKLVRAQTEREILGLLDHPFLptlyshfetekfsCL 189
Cdd:cd05110   9 LKRVKVLGSGAFGTVYkgiwVPEGETVKIPVAIKILNE--TTGPKANVEFMDEALIMASMDHPHL-------------VR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 190 LMEFCSGGDLHILRQKQPG--------KHFSELAARF---YASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDF 258
Cdd:cd05110  74 LLGVCLSPTIQLVTQLMPHgclldyvhEHKDNIGSQLllnWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDF 153

                ...
gi 15242554 259 DLS 261
Cdd:cd05110 154 GLA 156
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
336-427 2.50e-03

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: 39.78  E-value: 2.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 336 PTAARSMSFVGTHEYLAPEIIRGDgHGSSVDWWTFGIFLYELLTG--KTP--FKGNGNRETLFNVV---GQPLKFPegSI 408
Cdd:cd13975 151 PEAMMSGSIVGTPIHMAPELFSGK-YDNSVDVYAFGILFWYLCAGhvKLPeaFEQCASKDHLWNNVrkgVRPERLP--VF 227
                        90
                ....*....|....*....
gi 15242554 409 SFAAKDLIRGLLTKDPKKR 427
Cdd:cd13975 228 DEECWNLMEACWSGDPSQR 246
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
188-264 3.47e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 38.40  E-value: 3.47e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242554 188 CLLMEFCSGGDLH--ILRQKQPGKHFSELAArfyasevLLALeyLHMMGVVYRDLKPENVMVREDGhIMLSDFDLSLQS 264
Cdd:COG3642  32 DLVMEYIEGETLAdlLEEGELPPELLRELGR-------LLAR--LHRAGIVHGDLTTSNILVDDGG-VYLIDFGLARYS 100
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
116-261 3.76e-03

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: 39.25  E-value: 3.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMG-----CFFAMKVMDKGMLIGRKKLVRaqtEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05093   9 LKRELGEGAFGKVFLAECYNLCpeqdkILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH-ILRQKQP-------GKHFSELAAR---FYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFD 259
Cdd:cd05093  86 FEYMKHGDLNkFLRAHGPdavlmaeGNRPAELTQSqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 165

                ..
gi 15242554 260 LS 261
Cdd:cd05093 166 MS 167
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
117-446 3.98e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 39.42  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  117 LKKLGCGDIGSVYLAELREMGCFFAMKvmdKGMLIGRKKLVRAQTEREI--LGLLDHPFLPTLYSHFETEKFSCLLMEFC 194
Cdd:PLN00009   7 VEKIGEGTYGVVYKARDRVTNETIALK---KIRLEQEDEGVPSTAIREIslLKEMQHGNIVRLQDVVHSEKRLYLVFEYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  195 sggDLHILRQKQPGKHFSE--LAARFYASEVLLALEYLHMMGVVYRDLKPENVMV-REDGHIMLSDFDLSlQSFvsptli 271
Cdd:PLN00009  84 ---DLDLKKHMDSSPDFAKnpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIdRRTNALKLADFGLA-RAF------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  272 qstsqpschiasyciqppcidpscKLPVaciqpscfkprflnnkprkaktekagsdslpmliaeptaaRSMsfvgTHE-- 349
Cdd:PLN00009 154 ------------------------GIPV----------------------------------------RTF----THEvv 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554  350 ---YLAPEIIRGDGHGSS-VDWWTFGIFLYELLTGKTPFKGNGNRETL---FNVVGQPLK---------------FPE-- 405
Cdd:PLN00009 166 tlwYRAPEILLGSRHYSTpVDIWSVGCIFAEMVNQKPLFPGDSEIDELfkiFRILGTPNEetwpgvtslpdyksaFPKwp 245
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 15242554  406 --------GSISFAAKDLIRGLLTKDPKKRLgfkkGATEIKQHPFFNNV 446
Cdd:PLN00009 246 pkdlatvvPTLEPAGVDLLSKMLRLDPSKRI----TARAALEHEYFKDL 290
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
338-443 4.02e-03

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: 39.26  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 338 AARSMSFVGTHEYLAPEIIRgDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETLFNVVG---QPLKFPEGSISfAAKD 414
Cdd:cd14030 183 ASFAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTsgvKPASFDKVAIP-EVKE 260
                        90       100
                ....*....|....*....|....*....
gi 15242554 415 LIRGLLTKDPKKRLGFKkgatEIKQHPFF 443
Cdd:cd14030 261 IIEGCIRQNKDERYAIK----DLLNHAFF 285
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
343-393 4.42e-03

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: 39.23  E-value: 4.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242554 343 SFVGTHEYLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL 393
Cdd:cd14215 191 TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHL 241
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
345-384 4.54e-03

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: 39.02  E-value: 4.54e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15242554 345 VGTHEYLAPEIIRGDGHGSSvDWWTFGIFLYELLTGKTPF 384
Cdd:cd14158 180 VGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPV 218
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
184-244 4.80e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 38.85  E-value: 4.80e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242554 184 EKFSCLLMEFcSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPEN 244
Cdd:cd14130  68 EKFNYVVMQL-QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 127
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
351-428 4.93e-03

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: 39.01  E-value: 4.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 351 LAPEIIRG-DGHGSSVDW-----WTFGIFLYELLTGKTPFKGNGNrETLFNVVGQPLKFPE--GSISFAAKDLIRGLLTK 422
Cdd:cd14018 215 MAPEVSTAvPGPGVVINYskadaWAVGAIAYEIFGLSNPFYGLGD-TMLESRSYQESQLPAlpSAVPPDVRQVVKDLLQR 293

                ....*.
gi 15242554 423 DPKKRL 428
Cdd:cd14018 294 DPNKRV 299
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
114-261 5.29e-03

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 38.71  E-value: 5.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 114 FRLLKKLGCGDIGSVYlaelreMGCF-----FAMKVMDKGMLIGRKKLVRAQTEREilglLDHPFLPTLYSHFETEKFSc 188
Cdd:cd05067   9 LKLVERLGAGQFGEVW------MGYYnghtkVAIKSLKQGSMSPDAFLAEANLMKQ----LQHQRLVRLYAVVTQEPIY- 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242554 189 LLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLSDFDLS 261
Cdd:cd05067  78 IITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLA 150
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
116-261 5.80e-03

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 38.84  E-value: 5.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 116 LLKKLGCGDIGSVYLAELREMG-----CFFAMKVMDKGMLIGRKKLvraQTEREILGLLDHPFLPTLYSHFETEKFSCLL 190
Cdd:cd05094   9 LKRELGEGAFGKVFLAECYNLSptkdkMLVAVKTLKDPTLAARKDF---QREAELLTNLQHDHIVKFYGVCGDGDPLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 191 MEFCSGGDLH-----------ILRQKQPGKHFSELAAR---FYASEVLLALEYLHMMGVVYRDLKPENVMVREDGHIMLS 256
Cdd:cd05094  86 FEYMKHGDLNkflrahgpdamILVDGQPRQAKGELGLSqmlHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 165

                ....*
gi 15242554 257 DFDLS 261
Cdd:cd05094 166 DFGMS 170
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
160-255 6.35e-03

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 38.66  E-value: 6.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 160 QTEREILGLLDHP-FLPTLYSHFETEkFSCLLMEFCSGGDLHILRQKQPGKHFSELAARFYASEVLL-ALEYLHMMGVVY 237
Cdd:cd14157  40 QTEVQICFRCCHPnILPLLGFCVESD-CHCLIYPYMPNGSLQDRLQQQGGSHPLPWEQRLSISLGLLkAVQHLHNFGILH 118
                        90       100
                ....*....|....*....|...
gi 15242554 238 RDLKPENVMVRED-----GHIML 255
Cdd:cd14157 119 GNIKSSNVLLDGNllpklGHSGL 141
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
350-393 6.36e-03

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: 38.92  E-value: 6.36e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15242554 350 YLAPEIIRGDGHGSSVDWWTFGIFLYELLTGKTPFKGNGNRETL 393
Cdd:cd14225 211 YRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQL 254
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
159-283 8.15e-03

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: 38.28  E-value: 8.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242554 159 AQTEREILGLLDHPFLPTLYSHFETEKFSCLLMEfcsggDLH--ILRQKQPGKHFSELAARFYASEVLLALEYLHMMGVV 236
Cdd:cd14112  47 AVREFESLRTLQHENVQRLIAAFKPSNFAYLVME-----KLQedVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIA 121
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15242554 237 YRDLKPENVMVREDGHIMLSDFDLSLQSFVSPtLIQSTSQPSCHIAS 283
Cdd:cd14112 122 HLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSK-LGKVPVDGDTDWAS 167
 
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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