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Conserved domains on  [gi|14042947|ref|NP_114417|]
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testis-specific serine/threonine-protein kinase 1 [Homo sapiens]

Protein Classification

testis-specific serine/threonine-protein kinase( domain architecture ID 10197676)

testis-specific serine/threonine-protein kinase (TSSK) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
10-272 0e+00

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: 550.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIV 89
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFETSDGKVYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRM 169
Cdd:cd14165  81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd14165 161 VLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSECKDLI 240
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14165 241 YRLLQPDVSQRLCIDEVLSHPWL 263
 
Name Accession Description Interval E-value
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
10-272 0e+00

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: 550.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIV 89
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFETSDGKVYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRM 169
Cdd:cd14165  81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd14165 161 VLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSECKDLI 240
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14165 241 YRLLQPDVSQRLCIDEVLSHPWL 263
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-272 2.96e-90

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 271.33  E-value: 2.96e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFED-EDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrDDSGRMal 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL--DPGEKL-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    172 sKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPR-SKHLTGECKDLI 249
Cdd:smart00220 154 -TTFVGTPEYMAPEVLLGKGYGKAV-DIWSLGVILYELLTGKPPFpGDDQLLELFKKIGKPKPPFPPpEWDISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 14042947    250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
18-272 2.10e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 178.21  E-value: 2.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAVQGD 97
Cdd:pfam00069   7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNIL-REIKILKKLNHPNIVRLYDAFED-KDNLYLVLEYVEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDvvhrdlkcdnllldkdfniklsdfsfskrclrddsgrmalskTFCG 177
Cdd:pfam00069  85 LFDLLSEKGAFSEREAKFIMKQILEGLESGSSLT------------------------------------------TFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY---DDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYHMLQ 254
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKV-DVWSLGCILYELLTGKPPFpgiNGNEIYELIIDQPYAFPELP--SNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 14042947   255 PDVNRRLHIDEILSHCWM 272
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
18-367 2.21e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.59  E-value: 2.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKA-PADFLEKFLpREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELaVQG 96
Cdd:COG0515  15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAaDPEARERFR-REARALARLNHPNIVRVYDVGE-EDGRPYLVMEY-VEG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 -DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclRDDSGRMALSKTF 175
Cdd:COG0515  92 eSLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIAR---ALGGATLTQTGTV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKvYDIWSLGVILYIMVCGSMPYD-DSNIKKMLRIQKEHRVNFPR-SKHLTGECKDLIYHML 253
Cdd:COG0515 169 VGTPGYMAPEQARGEPVDPR-SDVYSLGVTLYELLTGRPPFDgDSPAELLRAHLREPPPPPSElRPDLPPALDAIVLRAL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 254 QPDVNRRLH-----IDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQPQAQPETKP 328
Cdd:COG0515 248 AKDPEERYQsaaelAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAA 327
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 14042947 329 EGTAMQMSRQSEILGFPSKPSTMETEEGPPQQPPETRAQ 367
Cdd:COG0515 328 AAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAA 366
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
3-261 3.05e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 136.87  E-value: 3.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    3 DAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETS 82
Cdd:PTZ00263  11 DTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   83 HgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcL 162
Cdd:PTZ00263  91 N-RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-V 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  163 RDDsgrmalSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQkEHRVNFPRskHL 241
Cdd:PTZ00263 169 PDR------TFTLCGTPEYLAPEVIQSKGHG-KAVDWWTMGVLLYEFIAGYPPfFDDTPFRIYEKIL-AGRLKFPN--WF 238
                        250       260
                 ....*....|....*....|
gi 14042947  242 TGECKDLIYHMLQPDVNRRL 261
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-219 6.56e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 102.95  E-value: 6.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKII------DrkkapADFLEKFLpREIEILAMLNHCSIIKTYEIFETsHGK 85
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLrpdlarD-----PEFVARFR-REAQSAASLSHPNIVSVYDVGED-GGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   86 VYIVMELaVQG-DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrd 164
Cdd:NF033483  82 PYIVMEY-VDGrTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR----- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947  165 dsgrmALSKT-------FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD-DS 219
Cdd:NF033483 156 -----ALSSTtmtqtnsVLGTVHYLSPEQARGGTVDARS-DIYSLGIVLYEMLTGRPPFDgDS 212
 
Name Accession Description Interval E-value
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
10-272 0e+00

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: 550.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIV 89
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFETSDGKVYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRM 169
Cdd:cd14165  81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd14165 161 VLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSECKDLI 240
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14165 241 YRLLQPDVSQRLCIDEVLSHPWL 263
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
11-272 1.19e-167

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: 468.20  E-value: 1.19e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSER--LKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYI 88
Cdd:cd14080   1 GYRLGKTIGEGSYSKVKLAEYTKsgLKEKVACKIIDKKKAPKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGS-KVFI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgR 168
Cdd:cd14080  80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDD--G 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSK-HLTGECKD 247
Cdd:cd14080 158 DVLSKTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSVkKLSPECKD 237
                       250       260
                ....*....|....*....|....*
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14080 238 LIDQLLEPDPTKRATIEEILNHPWL 262
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-271 9.65e-130

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: 371.85  E-value: 9.65e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEK-IKREIEIMKLLNHPNIIKLYEVIETEN-KIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmaL 171
Cdd:cd14003  80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGS-----L 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKehRVNFPRSKHLTGECKDLIYH 251
Cdd:cd14003 155 LKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKIL--KGKYPIPSHLSPDARDLIRR 232
                       250       260
                ....*....|....*....|
gi 14042947 252 MLQPDVNRRLHIDEILSHCW 271
Cdd:cd14003 233 MLVVDPSKRITIEEILNHPW 252
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
11-271 4.56e-129

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: 370.47  E-value: 4.56e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVM 90
Cdd:cd14162   1 GYIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTS-RVYIIM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMA 170
Cdd:cd14162  80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGKPK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRiQKEHRVNFPRSKHLTGECKDLIY 250
Cdd:cd14162 160 LSETYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLK-QVQRRVVFPKNPTVSEECKDLIL 238
                       250       260
                ....*....|....*....|.
gi 14042947 251 HMLQPdVNRRLHIDEILSHCW 271
Cdd:cd14162 239 RMLSP-VKKRITIEEIKRDPW 258
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
11-272 7.29e-97

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: 288.43  E-value: 7.29e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVM 90
Cdd:cd14163   1 GYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADGKIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLdKDFNIKLSDFSFSKRCLRddsGRMA 170
Cdd:cd14163  81 ELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPK---GGRE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLrIQKEHRVNFPRSKHLTGECKDLIY 250
Cdd:cd14163 157 LSQTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKML-CQQQKGVSLPGHLGVSRTCQDLLK 235
                       250       260
                ....*....|....*....|..
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14163 236 RLLEPDMVLRPSIEEVSWHPWL 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-272 2.96e-90

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 271.33  E-value: 2.96e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFED-EDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrDDSGRMal 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL--DPGEKL-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    172 sKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPR-SKHLTGECKDLI 249
Cdd:smart00220 154 -TTFVGTPEYMAPEVLLGKGYGKAV-DIWSLGVILYELLTGKPPFpGDDQLLELFKKIGKPKPPFPPpEWDISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 14042947    250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
11-272 4.54e-89

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: 268.65  E-value: 4.54e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVM 90
Cdd:cd14164   1 GYTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEVANGRLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ElAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD-FNIKLSDFSFSkrclRDDSGRM 169
Cdd:cd14164  81 E-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADdRKIKIADFGFA----RFVEDYP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIkKMLRIQKEHrVNFPRSKHLTGECKDLI 249
Cdd:cd14164 156 ELSTTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNV-RRLRLQQRG-VLYPSGVALEEPCRALI 233
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14164 234 RTLLQFNPSTRPSIQQVAGNSWL 256
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-271 5.44e-87

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: 263.18  E-value: 5.44e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLR-REIEILKRLDHPNIVKLYEVFEDD-KNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRcLRDDSgr 168
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEGE-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 maLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR-IQK-EHRVNFPRSKHLTGECK 246
Cdd:cd05117 157 --KLKTVCGTPYYVAPEVLKGKGYGKKC-DIWSLGVILYILLCGYPPFYGETEQELFEkILKgKYSFDSPEWKNVSEEAK 233
                       250       260
                ....*....|....*....|....*
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd05117 234 DLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
18-272 1.76e-81

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: 249.23  E-value: 1.76e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14071   8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKK-IYREVQIMKMLNHPHIIKLYQVMETKD-MLYLVTEYASNGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmaLSKTFCG 177
Cdd:cd14071  86 IFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGE-----LLKTWCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQ-PKVyDIWSLGVILYIMVCGSMPYDDSNIkKMLR---IQKEHRVNFprskHLTGECKDLIYHML 253
Cdd:cd14071 161 SPPYAAPEVFEGKEYEgPQL-DIWSLGVVLYVLVCGALPFDGSTL-QTLRdrvLSGRFRIPF----FMSTDCEHLIRRML 234
                       250
                ....*....|....*....
gi 14042947 254 QPDVNRRLHIDEILSHCWM 272
Cdd:cd14071 235 VLDPSKRLTIEQIKKHKWM 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
10-272 2.86e-81

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: 248.72  E-value: 2.86e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKK-APADFLEKfLPREIEILAMLNHCSIIKTYEIFETSHgKVYI 88
Cdd:cd14079   2 GNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKiKSLDMEEK-IRREIQILKLFRHPHIIRLYEVIETPT-DIFM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDdsGR 168
Cdd:cd14079  80 VMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSN-IMRD--GE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MAlsKTFCGSPAYAAPEVLQGIPYQ-PKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRiqKEHRVNFPRSKHLTGECKD 247
Cdd:cd14079 157 FL--KTSCGSPNYAAPEVISGKLYAgPEV-DVWSCGVILYALLCGSLPFDDEHIPNLFK--KIKSGIYTIPSHLSPGARD 231
                       250       260
                ....*....|....*....|....*
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14079 232 LIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
12-272 1.09e-75

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: 234.46  E-value: 1.09e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENK-KYLYLVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrddSGRMAl 171
Cdd:cd14081  82 YVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQP---EGSLL- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 sKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKDLIYH 251
Cdd:cd14081 158 -ETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPH--FISPDAQDLLRR 234
                       250       260
                ....*....|....*....|.
gi 14042947 252 MLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14081 235 MLEVNPEKRITIEEIKKHPWF 255
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
17-271 1.93e-75

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: 233.82  E-value: 1.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKII--DRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAV 94
Cdd:cd14073   8 TLGKGTYGKVKLAIERATGREVAIKSIkkDKIEDEQDMVR--IRREIEIMSSLNHPHIIRIYEVFE-NKDKIVIVMEYAS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmaLSKT 174
Cdd:cd14073  85 GGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDK-----LLQT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQ-PKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKhltGECKDLIYHML 253
Cdd:cd14073 160 FCGSPLYASPEIVNGTPYQgPEV-DCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQP---SDASGLIRWML 235
                       250
                ....*....|....*...
gi 14042947 254 QPDVNRRLHIDEILSHCW 271
Cdd:cd14073 236 TVNPKRRATIEDIANHWW 253
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-271 9.24e-75

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: 231.91  E-value: 9.24e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKT-KIFFVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrCLRDDSGRMAL 171
Cdd:cd14663  81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLS--ALSEQFRQDGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRiqKEHRVNFPRSKHLTGECKDLIYH 251
Cdd:cd14663 159 LHTTCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYR--KIMKGEFEYPRWFSPGAKSLIKR 236
                       250       260
                ....*....|....*....|
gi 14042947 252 MLQPDVNRRLHIDEILSHCW 271
Cdd:cd14663 237 ILDPNPSTRITVEQIMASPW 256
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
14-273 2.72e-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: 217.73  E-value: 2.72e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELA 93
Cdd:cd14007   4 IGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFED-KKRIYLILEYA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrDDSGRMalsk 173
Cdd:cd14007  83 PNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHA--PSNRRK---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKML-RIQKEHrVNFPrsKHLTGECKDLIYHM 252
Cdd:cd14007 157 TFCGTLDYLPPEMVEGKEYDYKV-DIWSLGVLCYELLVGKPPFESKSHQETYkRIQNVD-IKFP--SSVSPEAKDLISKL 232
                       250       260
                ....*....|....*....|.
gi 14042947 253 LQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14007 233 LQKDPSKRLSLEQVLNHPWIK 253
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
12-272 8.85e-69

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: 216.62  E-value: 8.85e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQK-LFREVRIMKILNHPNIVKLFEVIETEK-TLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrDDSGRMAL 171
Cdd:cd14072  80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSN----EFTPGNKL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SkTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKmLR---IQKEHRVNFprskHLTGECKDL 248
Cdd:cd14072 156 D-TFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKE-LRervLRGKYRIPF----YMSTDCENL 229
                       250       260
                ....*....|....*....|....
gi 14042947 249 IYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14072 230 LKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
12-272 1.36e-68

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: 216.27  E-value: 1.36e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKK-APADFLEKFLpREIEILAMLNHCSIIKTYEIFETSHgKVYIVM 90
Cdd:cd14099   3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSlTKPKQREKLK-SEIKIHRSLKHPNIVKFHDCFEDEE-NVYILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRma 170
Cdd:cd14099  81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERK-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 lsKTFCGSPAYAAPEVLQGIP-YQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd14099 159 --KTLCGTPNYIAPEVLEKKKgHSFEV-DIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLSISDEAKDLI 235
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14099 236 RSMLQPDPTKRPSLDEILSHPFF 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
12-272 1.43e-67

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: 213.35  E-value: 1.43e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADfLEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVME 91
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQK-TQRLLSREISSMEKLHHPNIIRLYEVVET-LSKLHLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmal 171
Cdd:cd14075  82 YASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLN--- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 skTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYH 251
Cdd:cd14075 159 --TFCGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIP--SYVSEPCQELIRG 234
                       250       260
                ....*....|....*....|.
gi 14042947 252 MLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14075 235 ILQPVPSDRYSIDEIKNSEWL 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
18-272 1.67e-67

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: 213.57  E-value: 1.67e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKK------------APADFLEKFLpREIEILAMLNHCSIIKTYEIFET-SHG 84
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRlrkrregkndrgKIKNALDDVR-REIAIMKKLDHPNIVRLYEVIDDpESD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVQGDLLELI--KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCl 162
Cdd:cd14008  80 KLYLVLEYCEGGPVMELDsgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMF- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 rdDSGRMALSKTfCGSPAYAAPEVLQGI--PYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKH 240
Cdd:cd14008 159 --EDGNDTLQKT-AGTPAFLAPELCDGDskTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPE 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14008 236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
12-272 1.87e-67

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: 213.40  E-value: 1.87e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflekfLPR---EIEILAMLNHCSIIKTYEIFETSHgKVYI 88
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDD-----LPRvktEIEALKNLSHQHICRLYHVIETDN-KIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFskrCLRDDSGR 168
Cdd:cd14078  79 VLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGL---CAKPKGGM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRiqKEHRVNFPRSKHLTGECKDL 248
Cdd:cd14078 156 DHHLETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYR--KIQSGKYEEPEWLSPSSKLL 233
                       250       260
                ....*....|....*....|....
gi 14042947 249 IYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14078 234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-272 4.47e-65

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: 207.27  E-value: 4.47e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKApADFLEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVME 91
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL-DDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDT-QTKLYLILE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL-DKDFNIKLSDFSFSKRCLrddSGRM 169
Cdd:cd14074  83 LGDGGDMYDYImKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQ---PGEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 AlsKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLI 249
Cdd:cd14074 160 L--ETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVP--AHVSPECKDLI 235
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14074 236 RRMLIRDPKKRASLEEIENHPWL 258
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
18-271 1.30e-64

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: 205.92  E-value: 1.30e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQEN-LESEIAILKSIKHPNIVRLYDVQKTED-FIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN---IKLSDFSFSkRCLRDDSgrmaLSKT 174
Cdd:cd14009  79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFA-RSLQPAS----MAET 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR-IQKEHRV-NFPRSKHLTGECKDLIYHM 252
Cdd:cd14009 154 LCGSPLYMAPEILQFQKYDAKA-DLWSVGAILFEMLVGKPPFRGSNHVQLLRnIERSDAViPFPIAAQLSPDCKDLLRRL 232
                       250
                ....*....|....*....
gi 14042947 253 LQPDVNRRLHIDEILSHCW 271
Cdd:cd14009 233 LRRDPAERISFEEFFAHPF 251
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
18-272 6.58e-63

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: 201.72  E-value: 6.58e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAySERLKFNVAIKII--DRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQ 95
Cdd:cd14161  11 LGKGTYGRVKKA-RDSSGRLVAIKSIrkDRIKDEQDLLH--IRREIEIMSSLNHPHIISVYEVFENS-SKIVIVMEYASR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDdsgrmALSKTF 175
Cdd:cd14161  87 GDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQD-----KFLQTY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMlrIQKEHRVNFPRSKHLTGECkDLIYHMLQP 255
Cdd:cd14161 162 CGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKIL--VKQISSGAYREPTKPSDAC-GLIRWLLMV 238
                       250
                ....*....|....*..
gi 14042947 256 DVNRRLHIDEILSHCWM 272
Cdd:cd14161 239 NPERRATLEDVASHWWV 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
9-272 8.76e-63

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: 201.85  E-value: 8.76e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLP-----REIEILAMLNHCSIIKTYEIFETSH 83
Cdd:cd14084   5 RKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREINKprnieTEIEILKKLSHPCIIKIEDFFDAED 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  84 gKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKr 160
Cdd:cd14084  85 -DYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSK- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 clrdDSGRMALSKTFCGSPAYAAPEVLQ---GIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQ-KEHRVNF- 235
Cdd:cd14084 163 ----ILGETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAV-DCWSLGVILFICLSGYPPFSEEYTQMSLKEQiLSGKYTFi 237
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 14042947 236 -PRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14084 238 pKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-269 3.31e-62

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: 198.26  E-value: 3.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApaDFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQGD 97
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLNHPNIVKLYDVFETENF-LYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrDDSGRMALSKTFC 176
Cdd:cd00180  78 LKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDL--DSDDSLLKTTGGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMvcgsmpyddsnikkmlriqkehrvnfprskhltGECKDLIYHMLQPD 256
Cdd:cd00180 156 TPPYYAPPELLGGRYYGPKV-DIWSLGVILYEL---------------------------------EELKDLIRRMLQYD 201
                       250
                ....*....|...
gi 14042947 257 VNRRLHIDEILSH 269
Cdd:cd00180 202 PKKRPSAKELLEH 214
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-260 1.78e-59

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: 192.80  E-value: 1.78e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAP-ADFLEKFLpREIEILAMLNHCSIIKTYEIFETsHGKVYIV 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEdEEFRERFL-REARALARLSHPNIVRVYDVGED-DGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclRDDSGRM 169
Cdd:cd14014  79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR---ALGDSGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTFCGSPAYAAPEVLQGIPYQPKvYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKD 247
Cdd:cd14014 156 TQTGSVLGTPAYMAPEQARGGPVDPR-SDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnPDVPPALDA 234
                       250
                ....*....|...
gi 14042947 248 LIYHMLQPDVNRR 260
Cdd:cd14014 235 IILRALAKDPEER 247
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
18-269 2.44e-59

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 192.29  E-value: 2.44e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAK---VKSAYSERLkfnVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAV 94
Cdd:cd08215   8 IGKGSFGSaylVRRKSDGKL---YVLKEIDLSNMSEKEREEAL-NEVKLLSKLKHPNIVKYYESFEE-NGKLCIVMEYAD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALH----EDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDDsgrMA 170
Cdd:cd08215  83 GGDLAQKIKKQKKKGqpfpEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK-VLEST---TD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKK-MLRIQKEHRVNFPrsKHLTGECKDLI 249
Cdd:cd08215 159 LAKTVVGTPYYLSPELCENKPYNYKS-DIWALGCVLYELCTLKHPFEANNLPAlVYKIVKGQYPPIP--SQYSSELRDLV 235
                       250       260
                ....*....|....*....|
gi 14042947 250 YHMLQPDVNRRLHIDEILSH 269
Cdd:cd08215 236 NSMLQKDPEKRPSANEILSS 255
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-271 2.11e-58

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: 189.89  E-value: 2.11e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd14083  11 LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGK--EDSLENEIAVLRKIKHPNIVQLLDIYE-SKSHLYLVMELVTGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL---LDKDFNIKLSDFSFSKrclRDDSGRMAlskT 174
Cdd:cd14083  88 LFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK---MEDSGVMS---T 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQK-EHRVNFPRSKHLTGECKDLIYHM 252
Cdd:cd14083 162 ACGTPGYVAPEVLAQKPYGKAV-DCWSIGVISYILLCGYPPfYDENDSKLFAQILKaEYEFDSPYWDDISDSAKDFIRHL 240
                       250
                ....*....|....*....
gi 14042947 253 LQPDVNRRLHIDEILSHCW 271
Cdd:cd14083 241 MEKDPNKRYTCEQALEHPW 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
18-272 2.42e-58

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: 190.21  E-value: 2.42e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYS--ERLKFNVAIKIIDRKKAPA---DFLEKFLpREIEILAMLNHCSIIKTYEIFETSHGKVYIVMEL 92
Cdd:cd13994   1 IGKGATSVVRIVTKknPRSGVLYAVKEYRRRDDESkrkDYVKRLT-SEYIISSKLHHPNIVKVLDLCQDLHGKWCLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDDSGRMA-L 171
Cdd:cd13994  80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAE-VFGMPAEKESpM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPY-----DDSNIKK-MLRIQKEHRVNFPRSKHLTGEC 245
Cdd:cd13994 159 SAGLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWrsakkSDSAYKAyEKSGDFTNGPYEPIENLLPSEC 238
                       250       260
                ....*....|....*....|....*..
gi 14042947 246 KDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd13994 239 RRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
12-272 6.97e-58

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: 188.81  E-value: 6.97e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRkkAPADFL--------------EKFLPREIEILAMLNHCSIIKTYE 77
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPR--ASNAGLkkerekrlekeisrDIRTIREAALSSLLNHPHICRLRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  78 IFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSF 157
Cdd:cd14077  81 FLRTPN-HYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 158 SKRCLRDDsgrmaLSKTFCGSPAYAAPEVLQGIPYQ-PKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFP 236
Cdd:cd14077 160 SNLYDPRR-----LLRTFCGSLYFAAPELLQAQPYTgPEV-DVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYP 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 14042947 237 rsKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14077 234 --SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-272 4.15e-57

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: 186.18  E-value: 4.15e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV---KSAYSERLkfnVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAV 94
Cdd:cd05123   1 LGKGSFGKVllvRKKDTGKL---YAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQT-EEKLYLVLDYVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrDDSGRMALSKT 174
Cdd:cd05123  77 GGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAK----ELSSDGDRTYT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKDLIYHMLQ 254
Cdd:cd05123 153 FCGTPEYLAPEVLLGKGYGKAV-DWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPE--YVSPEAKSLISGLLQ 229
                       250       260
                ....*....|....*....|.
gi 14042947 255 PDVNRRLH---IDEILSHCWM 272
Cdd:cd05123 230 KDPTKRLGsggAEEIKAHPFF 250
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
11-271 7.17e-56

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: 183.69  E-value: 7.17e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETSHGKvYIVM 90
Cdd:cd14069   2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPEN-IKKEVCIQKMLSHKNVVRFYGHRREGEFQ-YLFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRma 170
Cdd:cd14069  80 EYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKER-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYD---DSNIKKMLRIQKEHRVNFPRSKhLTGECKD 247
Cdd:cd14069 158 LLNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDqpsDSCQEYSDWKENKKTYLTPWKK-IDTAALS 236
                       250       260
                ....*....|....*....|....
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14069 237 LLRKILTENPNKRITIEDIKKHPW 260
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
12-272 1.20e-55

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: 183.09  E-value: 1.20e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD-FLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVM 90
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsYVTKNLRREGRIQQMIRHPNITQLLDILETEN-SYYLVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDDSGRMA 170
Cdd:cd14070  83 ELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSN-CAGILGYSDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSkTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY--DDSNIKKMLRIQKEHRVNfPRSKHLTGECKDL 248
Cdd:cd14070 162 FS-TQCGSPAYAAPELLARKKYGPKV-DVWSIGVNMYAMLTGTLPFtvEPFSLRALHQKMVDKEMN-PLPTDLSPGAISF 238
                       250       260
                ....*....|....*....|....
gi 14042947 249 IYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14070 239 LRSLLEPDPLKRPNIKQALANRWL 262
Pkinase pfam00069
Protein kinase domain;
18-272 2.10e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 178.21  E-value: 2.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAVQGD 97
Cdd:pfam00069   7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNIL-REIKILKKLNHPNIVRLYDAFED-KDNLYLVLEYVEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDvvhrdlkcdnllldkdfniklsdfsfskrclrddsgrmalskTFCG 177
Cdd:pfam00069  85 LFDLLSEKGAFSEREAKFIMKQILEGLESGSSLT------------------------------------------TFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY---DDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYHMLQ 254
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKV-DVWSLGCILYELLTGKPPFpgiNGNEIYELIIDQPYAFPELP--SNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 14042947   255 PDVNRRLHIDEILSHCWM 272
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-272 1.59e-53

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: 177.53  E-value: 1.59e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGK--ETSIENEIAVLHKIKHPNIVALDDIYE-SGGHLYLIMQLVSGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL---LDKDFNIKLSDFSFSKrclRDDSGrmALSKT 174
Cdd:cd14167  88 LFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK---IEGSG--SVMST 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNFPRSKHLTGECKDLIYHM 252
Cdd:cd14167 163 ACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDAKLFEqiLKAEYEFDSPYWDDISDSAKDFIQHL 241
                       250       260
                ....*....|....*....|
gi 14042947 253 LQPDVNRRLHIDEILSHCWM 272
Cdd:cd14167 242 MEKDPEKRFTCEQALQHPWI 261
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
12-272 3.32e-53

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: 176.91  E-value: 3.32e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVK-----SAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKV 86
Cdd:cd14076   3 YILGRTLGEGEFGKVKlgwplPKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKK-YI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDS 166
Cdd:cd14076  82 GIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRMalsKTFCGSPAYAAPE-VLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDD-------SNIKKMLRIQKEHRVNFPrs 238
Cdd:cd14076 162 DLM---STSCGSPCYAAPElVVSDSMYAGRKADIWSCGVILYAMLAGYLPFDDdphnpngDNVPRLYRYICNTPLIFP-- 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 239 KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14076 237 EYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
21-271 1.11e-52

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: 175.48  E-value: 1.11e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  21 GSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLE 100
Cdd:cd05579   4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKK-NLYLVMEYLPGGDLYS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 101 LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAL--------- 171
Cdd:cd05579  83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKLSIqkksngape 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 --SKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd05579 163 keDRRIVGTPDYLAPEILLGQGHGKTV-DWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDPEVSDEAKDLI 241
                       250       260
                ....*....|....*....|....*
gi 14042947 250 YHMLQPDVNRRL---HIDEILSHCW 271
Cdd:cd05579 242 SKLLTPDPEKRLgakGIEEIKNHPF 266
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
18-272 3.71e-52

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: 173.73  E-value: 3.71e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEK-----FLPREIEILAMLN---HCSIIKTYEIFETShGKVYIV 89
Cdd:cd14004   8 MGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRdrklgTVPLEIHILDTLNkrsHPNIVKLLDFFEDD-EFYYLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQG-DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsGR 168
Cdd:cd14004  87 MEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDF-----------GS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSK-----TFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYddSNIKKMLriQKEHRVNFPRSKhltg 243
Cdd:cd14004 156 AAYIKsgpfdTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPF--YNIEEIL--EADLRIPYAVSE---- 227
                       250       260
                ....*....|....*....|....*....
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14004 228 DLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
12-271 1.11e-51

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: 172.51  E-value: 1.11e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGK--EHMIENEVAILRRVKHPNIVQLIEEYDTD-TELYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRCLRDDSg 167
Cdd:cd14095  79 LVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATEVKEPLF- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmalskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY--DDSNIKKMLRIQKEHRVNF--PRSKHLTG 243
Cdd:cd14095 158 ------TVCGTPTYVAPEILAETGYGLKV-DIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEFEFlsPYWDNISD 230
                       250       260
                ....*....|....*....|....*...
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14095 231 SAKDLISRMLVVDPEKRYSAGQVLDHPW 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
18-269 6.74e-51

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: 170.46  E-value: 6.74e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAVQGD 97
Cdd:cd05122   8 IGKGGFGVVYKARHKKTGQIVAIKKINLESKEK---KESILNEIAILKKCKHPNIVKYYGSYLK-KDELWIVMEFCSGGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGA-LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmalSKTFC 176
Cdd:cd05122  84 LKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKT-----RNTFV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNI-KKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQP 255
Cdd:cd05122 159 GTPYWMAPEVIQGKPYGFKA-DIWSLGITAIEMAEGKPPYSELPPmKALFLIATNGPPGLRNPKKWSKEFKDFLKKCLQK 237
                       250
                ....*....|....
gi 14042947 256 DVNRRLHIDEILSH 269
Cdd:cd05122 238 DPEKRPTAEQLLKH 251
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
18-271 1.05e-50

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: 170.01  E-value: 1.05e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKtYEIFETSHGKVYIVMELAVQGD 97
Cdd:cd06606   8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALE-REIRILSSLKHPNIVR-YLGTERTENTLNIFLEYVPGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRclRDDSGRMALSKTFCG 177
Cdd:cd06606  86 LASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKR--LAEIATGEGTKSLRG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddSNIKK----MLRI-QKEHRVNFPrsKHLTGECKDLIYHM 252
Cdd:cd06606 164 TPYWMAPEVIRGEGYGRAA-DIWSLGCTVIEMATGKPPW--SELGNpvaaLFKIgSSGEPPPIP--EHLSEEAKDFLRKC 238
                       250
                ....*....|....*....
gi 14042947 253 LQPDVNRRLHIDEILSHCW 271
Cdd:cd06606 239 LQRDPKKRPTADELLQHPF 257
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-301 1.08e-50

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: 171.71  E-value: 1.08e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflekflpREIEILAML-NHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd14092  14 LGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTS--------REVQLLRLCqGHPNIVKLHEVFQDEL-HTYLVMELLRGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSkrCLRDDSGRMalsK 173
Cdd:cd14092  85 ELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFA--RLKPENQPL---K 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKvY----DIWSLGVILYIMVCGSMP-----YDDSNIKKMLRIqKEHRVNF--PRSKHLT 242
Cdd:cd14092 160 TPCFTLPYAAPEVLKQALSTQG-YdescDLWSLGVILYTMLSGQVPfqspsRNESAAEIMKRI-KSGDFSFdgEEWKNVS 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCWMQpkargspsvainkeGESSRGTEPLWTPE 301
Cdd:cd14092 238 SEAKSLIQGLLTVDPSKRLTMSELRNHPWLQ--------------GSSSPSSTPLMTPG 282
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
18-367 2.21e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.59  E-value: 2.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKA-PADFLEKFLpREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELaVQG 96
Cdd:COG0515  15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAaDPEARERFR-REARALARLNHPNIVRVYDVGE-EDGRPYLVMEY-VEG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 -DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclRDDSGRMALSKTF 175
Cdd:COG0515  92 eSLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIAR---ALGGATLTQTGTV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKvYDIWSLGVILYIMVCGSMPYD-DSNIKKMLRIQKEHRVNFPR-SKHLTGECKDLIYHML 253
Cdd:COG0515 169 VGTPGYMAPEQARGEPVDPR-SDVYSLGVTLYELLTGRPPFDgDSPAELLRAHLREPPPPPSElRPDLPPALDAIVLRAL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 254 QPDVNRRLH-----IDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQPQAQPETKP 328
Cdd:COG0515 248 AKDPEERYQsaaelAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAA 327
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 14042947 329 EGTAMQMSRQSEILGFPSKPSTMETEEGPPQQPPETRAQ 367
Cdd:COG0515 328 AAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAA 366
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-277 2.12e-48

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: 165.29  E-value: 2.12e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd14086   3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQK-LEREARICRLLKHPNIVRLHDSISEE-GFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRCLRDDSGR 168
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MAlsktFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSK--HLTGECK 246
Cdd:cd14086 161 FG----FAGTPGYLSPEVLRKDPYGKPV-DIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEwdTVTPEAK 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCWMQPKAR 277
Cdd:cd14086 236 DLINQMLTVNPAKRITAAEALKHPWICQRDR 266
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
18-271 2.84e-48

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: 164.45  E-value: 2.84e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKK---------------------APADFLEKfLPREIEILAMLNHCSIIKTY 76
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKllkqagffrrppprrkpgalgKPLDPLDR-VYREIAILKKLDHPNVVKLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  77 EIF-ETSHGKVYIVMELAVQGDLLElIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF 155
Cdd:cd14118  81 EVLdDPNEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 156 SFSKRCLRDDSgrmALSKTfCGSPAYAAPEVLQG--IPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRV 233
Cdd:cd14118 160 GVSNEFEGDDA---LLSST-AGTPAFMAPEALSEsrKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPV 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 14042947 234 NFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14118 236 VFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
18-269 3.81e-48

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: 163.23  E-value: 3.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERL-KFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEiFETSHGKVYIVMELAVQG 96
Cdd:cd14121   3 LGSGTYATVYKAYRKSGaREVVAVKCVSKSSLNKASTENLL-TEIELLKKLKHPHIVELKD-FQWDEEHIYLIMEYCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN--IKLSDFSFSKRCLRDDSGRmalskT 174
Cdd:cd14121  81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNpvLKLADFGFAQHLKPNDEAH-----S 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKM-LRIQKEHRVNFPRSKHLTGECKDLIYHML 253
Cdd:cd14121 156 LRGSPLYMAPEMILKKKYDARV-DLWSVGVILYECLFGRAPFASRSFEELeEKIRSSKPIEIPTRPELSADCRDLLLRLL 234
                       250
                ....*....|....*.
gi 14042947 254 QPDVNRRLHIDEILSH 269
Cdd:cd14121 235 QRDPDRRISFEEFFAH 250
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
12-272 9.81e-48

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: 162.72  E-value: 9.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLeKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAV-KLLEREVDILKHVNHAHIIHLEEVFETPK-RMYLVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD-------FNIKLSDFSFSkrcLRD 164
Cdd:cd14097  81 LCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLS---VQK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLT 242
Cdd:cd14097 158 YGLGEDMLQETCGTPIYMAPEVISAHGYSQQC-DIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSvwQSVS 236
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14097 237 DAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
18-272 1.32e-47

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: 162.52  E-value: 1.32e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDR------KKAPADFLEKFLpREIEILAMLN-HCSIIKTYEIFETShGKVYIVM 90
Cdd:cd14093  11 LGRGVSSTVRRCIEKETGQEFAVKIIDItgekssENEAEELREATR-REIEILRQVSgHPNIIELHDVFESP-TFIFLVF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRma 170
Cdd:cd14093  89 ELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLR-- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 lskTFCGSPAYAAPEVLQ-----GIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNF--PRSKHLTG 243
Cdd:cd14093 167 ---ELCGTPGYLAPEVLKcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFgsPEWDDISD 243
                       250       260
                ....*....|....*....|....*....
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14093 244 TAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-272 2.01e-47

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: 162.47  E-value: 2.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPAdFLEKFLPREIEILAMLNHCSIIKTYEIFE-TSHgkVYIVMELAVQG 96
Cdd:cd14166  11 LGSGAFSEVYLVKQRSTGKLYALKCI--KKSPL-SRDSSLENEIAVLKRIKHENIVTLEDIYEsTTH--YYLVMQLVSGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKrclRDDSGRMAlsk 173
Cdd:cd14166  86 ELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK---MEQNGIMS--- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNF--PRSKHLTGECKDLIYH 251
Cdd:cd14166 160 TACGTPGYVAPEVLAQKPYS-KAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFesPFWDDISESAKDFIRH 238
                       250       260
                ....*....|....*....|.
gi 14042947 252 MLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14166 239 LLEKNPSKRYTCEKALSHPWI 259
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-272 1.38e-46

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: 160.06  E-value: 1.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAY---SERLkfnVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYI 88
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQergSQRL---VALKCIPKKALRGK--EAMVENEIAVLRRINHENIVSLEDIYESP-THLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD---KDFNIKLSDFSFSKrclRDD 165
Cdd:cd14169  79 AMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK---IEA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRMAlskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNFPRSKHLTG 243
Cdd:cd14169 156 QGMLS---TACGTPGYVAPELLEQKPYGKAV-DVWAIGVISYILLCGYPPFYDENDSELFNqiLKAEYEFDSPYWDDISE 231
                       250       260
                ....*....|....*....|....*....
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14169 232 SAKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
19-269 2.61e-46

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: 158.57  E-value: 2.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVksaYSERLKFN---VAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAvQ 95
Cdd:cd14002  10 GEGSFGKV---YKGRRKYTgqvVALKFIPKRGKSEKELRN-LRQEIEILRKLNHPNIIEMLDSFET-KKEFVVVTEYA-Q 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrdDSGRMALSkTF 175
Cdd:cd14002  84 GELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAM---SCNTLVLT-SI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYHMLQP 255
Cdd:cd14002 160 KGTPLYMAPELVQEQPYDHTA-DLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWP--SNMSPEFKSFLQGLLNK 236
                       250
                ....*....|....
gi 14042947 256 DVNRRLHIDEILSH 269
Cdd:cd14002 237 DPSKRLSWPDLLEH 250
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
18-272 2.86e-46

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: 158.57  E-value: 2.86e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY-SERLKfNVAIKIIDRKKapadfLEKF------LPREIEILAMLNHCSIIKTYEIFETSH-GKVYIV 89
Cdd:cd14119   1 LGEGSYGKVKEVLdTETLC-RRAVKILKKRK-----LRRIpngeanVKREIQILRRLNHRNVIKLVDVLYNEEkQKLYMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVqGDLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR-CLRDDS 166
Cdd:cd14119  75 MEYCV-GGLQEMLDSAPDkrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAlDLFAED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRMalsKTFCGSPAYAAPEVLQGIPY--QPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGE 244
Cdd:cd14119 154 DTC---TTSQGSPAFQPPEIANGQDSfsGFKV-DIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPD--DVDPD 227
                       250       260
                ....*....|....*....|....*...
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14119 228 LQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
12-269 5.13e-46

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: 158.53  E-value: 5.13e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDR------KKAPADFLEKflpreiEILAMLNHCSIIKTYEIFETSHgK 85
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKrhiikeKKVKYVTIEK------EVLSRLAHPGIVKLYYTFQDES-K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDD 165
Cdd:cd05581  76 LYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRMALSK-------------TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN----IKKMLRIQ 228
Cdd:cd05581 156 SPESTKGDadsqiaynqaraaSFVGTAEYVSPELLNEKPAGKSS-DLWALGCIIYQMLTGKPPFRGSNeyltFQKIVKLE 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14042947 229 KEHRVNFPRskhltgECKDLIYHMLQPDVNRRLHI------DEILSH 269
Cdd:cd05581 235 YEFPENFPP------DAKDLIQKLLVLDPSKRLGVnenggyDELKAH 275
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
18-272 8.41e-46

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: 157.31  E-value: 8.41e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKflprEIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCES----ELNVLRRVRHTNIIQLIEVFETKE-RVYMVMELATGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRCLRDDSGRMalsKT 174
Cdd:cd14087  84 LFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGPNCLM---KT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR-IQKEHRVNFPRS-KHLTGECKDLIYHM 252
Cdd:cd14087 161 TCGTPEYIAPEILLRKPYTQSV-DMWAVGVIAYILLSGTMPFDDDNRTRLYRqILRAKYSYSGEPwPSVSNLAKDFIDRL 239
                       250       260
                ....*....|....*....|
gi 14042947 253 LQPDVNRRLHIDEILSHCWM 272
Cdd:cd14087 240 LTVNPGERLSATQALKHPWI 259
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
17-271 1.02e-45

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: 157.24  E-value: 1.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKIIDRKKApadfLEKFLPREIEILAMLNHCSIIKTYEIFET-SHgkVYIVMELAVQ 95
Cdd:cd14662   7 DIGSGNFGVARLMRNKETKELVAVKYIERGLK----IDENVQREIINHRSLRHPNIIRFKEVVLTpTH--LAIVMEYAAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF--NIKLSDFSFSKRCLRDDSgrmalSK 173
Cdd:cd14662  81 GELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQ-----PK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNF--PRSKHLTGECKDLI 249
Cdd:cd14662 156 STVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRktIQRIMSVQYkiPDYVRVSQDCRHLL 235
                       250       260
                ....*....|....*....|..
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14662 236 SRIFVANPAKRITIPEIKNHPW 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
18-271 1.36e-45

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: 156.87  E-value: 1.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYsERLKFNV-AIKIIDRKK-APADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQ 95
Cdd:cd14098   8 LGSGTFAEVKKAV-EVETGKMrAIKQIVKRKvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQ-HIYLVMEYVEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRclrddSGRMALSK 173
Cdd:cd14098  86 GDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAKV-----IHTGTFLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIP------YQPKVyDIWSLGVILYIMVCGSMPYD-DSNIKKMLRIQKEHRVNFP-RSKHLTGEC 245
Cdd:cd14098 161 TFCGTMAYLAPEILMSKEqnlqggYSNLV-DMWSVGCLVYVMLTGALPFDgSSQLPVEKRIRKGRYTQPPlVDFNISEEA 239
                       250       260
                ....*....|....*....|....*.
gi 14042947 246 KDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14098 240 IDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
11-281 1.38e-44

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: 155.10  E-value: 1.38e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRkkapadflEKFLPR-EIEILAML-NHCSIIKTYEIFETShGKVYI 88
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDK--------SKRDPSeEIEILLRYgQHPNIITLRDVYDDG-NSVYL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL-DKDFN---IKLSDFSFSKRcLRD 164
Cdd:cd14091  72 VTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQ-LRA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGrmaLSKTFCGSPAYAAPEVL--QGipYQpKVYDIWSLGVILYIMVCGSMPY----DDSNIKKMLRIQkEHRVNF--P 236
Cdd:cd14091 151 ENG---LLMTPCYTANFVAPEVLkkQG--YD-AACDIWSLGVLLYTMLAGYTPFasgpNDTPEVILARIG-SGKIDLsgG 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 14042947 237 RSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPS 281
Cdd:cd14091 224 NWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQR 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-268 2.50e-44

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: 153.08  E-value: 2.50e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAyserlKFN---VAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAV 94
Cdd:cd13999   1 IGSGSFGEVYKG-----KWRgtdVAIKKLKVEDDNDELLKEFR-REVSILSKLRHPNIVQFIGAC-LSPPPLCIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrclRDDSGRMALSK 173
Cdd:cd13999  74 GGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLS----RIKNSTTEKMT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHRVNfPRSKHLTGECKDLIYHM 252
Cdd:cd13999 150 GVVGTPRWMAPEVLRGEPYTEKA-DVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKGLRP-PIPPDCPPELSKLIKRC 227
                       250
                ....*....|....*.
gi 14042947 253 LQPDVNRRLHIDEILS 268
Cdd:cd13999 228 WNEDPEKRPSFSEIVK 243
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-271 2.77e-44

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: 153.22  E-value: 2.77e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRkkapADFLEKFLPREIEILAMLNHCSIIKTYEIFET-SHgkVYIVM 90
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIER----GEKIDENVQREIINHRSLRHPNIVRFKEVILTpTH--LAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF--NIKLSDFSFSKRCLRDDSgr 168
Cdd:cd14665  76 EYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQ-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 malSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNF--PRSKHLTGE 244
Cdd:cd14665 154 ---PKSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRktIQRILSVQYsiPDYVHISPE 230
                       250       260
                ....*....|....*....|....*..
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14665 231 CRHLISRIFVADPATRITIPEIRNHEW 257
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
18-269 6.45e-44

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: 152.52  E-value: 6.45e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLKFNVAIKIIDRKK--APADFLEKflprEIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAV 94
Cdd:cd14120   1 IGHGAFAVVfKGRHRKKPDLPVAIKCITKKNlsKSQNLLGK----EIKILKELSHENVVALLDCQETSSS-VYLVMEYCN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDK---------DFNIKLSDFSFSkRCLRDd 165
Cdd:cd14120  76 GGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgrkpspnDIRLKIADFGFA-RFLQD- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 sGRMAlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN---IKKMLRIQKEHRVNFPR--SKH 240
Cdd:cd14120 154 -GMMA--ATLCGSPMYMAPEVIMSLQYDAKA-DLWSIGTIVYQCLTGKAPFQAQTpqeLKAFYEKNANLRPNIPSgtSPA 229
                       250       260
                ....*....|....*....|....*....
gi 14042947 241 LtgecKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14120 230 L----KDLLLGLLKRNPKDRIDFEDFFSH 254
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-272 1.26e-43

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: 151.62  E-value: 1.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKK----APADFLEKfLPREIEILAMLNHCS---IIKTYEIFETSHG 84
Cdd:cd14005   2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewAMINGPVP-VPLEIALLLKASKPGvpgVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVyIVMELA--VQgDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD-FNIKLSDFSFSKRc 161
Cdd:cd14005  81 FL-LIMERPepCQ-DLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFGCGAL- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 162 LRDdsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPY--DDSNIKKmlriqkehRVNFPRsk 239
Cdd:cd14005 158 LKD-----SVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFenDEQILRG--------NVLFRP-- 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14005 223 RLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
17-271 1.79e-43

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: 152.35  E-value: 1.79e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05580   8 TLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDR-NLYMVMEYVPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDdsgrmaLSKTFC 176
Cdd:cd05580  87 ELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR-VKD------RTYTLC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNikKMLRIQK--EHRVNFPrsKHLTGECKDLIYHMLQ 254
Cdd:cd05580 160 GTPEYLAPEIILSKGHG-KAVDWWALGILIYEMLAGYPPFFDEN--PMKIYEKilEGKIRFP--SFFDPDAKDLIKRLLV 234
                       250       260
                ....*....|....*....|..
gi 14042947 255 PDVNRRL-----HIDEILSHCW 271
Cdd:cd05580 235 VDLTKRLgnlknGVEDIKNHPW 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
12-272 5.92e-43

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: 149.68  E-value: 5.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKtYEIFETSHGKVYIVME 91
Cdd:cd06627   2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKS-VMGEIDLLKKLNHPNIVK-YIGSVKTKDSLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSGRMAL 171
Cdd:cd06627  80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATK-LNEVEKDENS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SktfCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPrsKHLTGECKDLIY 250
Cdd:cd06627 159 V---VGTPYWMAPEVIEMSGVTTAS-DIWSVGCTVIELLTGNPPYYDLQpMAALFRIVQDDHPPLP--ENISPELRDFLL 232
                       250       260
                ....*....|....*....|..
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06627 233 QCFQKDPTLRPSAKELLKHPWL 254
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
18-271 6.99e-43

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: 149.75  E-value: 6.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII-DRKKAPadflekflpREIEILAMLNHC-SIIKTYEIFETSHGKV---YIVMEL 92
Cdd:cd14089   9 LGLGINGKVLECFHKKTGEKFALKVLrDNPKAR---------REVELHWRASGCpHIVRIIDVYENTYQGRkclLVVMEC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL-DKDFN--IKLSDFSFSKRCLRDDSg 167
Cdd:cd14089  80 MEGGELFSRIQERAdsAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsSKGPNaiLKLTDFGFAKETTTKKS- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmalSKTFCGSPAYAAPEVLqgipyQPKVY----DIWSLGVILYIMVCGSMPYDDSN-------IKKMLRiQKEHRVNFP 236
Cdd:cd14089 159 ----LQTPCYTPYYVAPEVL-----GPEKYdkscDMWSLGVIMYILLCGYPPFYSNHglaispgMKKRIR-NGQYEFPNP 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 14042947 237 RSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14089 229 EWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-276 8.36e-43

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: 150.75  E-value: 8.36e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIdrkKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVME 91
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKL---KKTVD--KKIVRTEIGVLLRLSHPNIIKLKEIFET-PTEISLVLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL---LDKDFNIKLSDFSFSKrcLRDDSGR 168
Cdd:cd14085  79 LVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSK--IVDQQVT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MalsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLR--IQKEHRVNFPRSKHLTGEC 245
Cdd:cd14085 157 M---KTVCGTPGYCAPEILRGCAYGPEV-DMWSVGVITYILLCGFEPfYDERGDQYMFKriLNCDYDFVSPWWDDVSLNA 232
                       250       260       270
                ....*....|....*....|....*....|.
gi 14042947 246 KDLIYHMLQPDVNRRLHIDEILSHCWMQPKA 276
Cdd:cd14085 233 KDLVKKLIVLDPKKRLTTQQALQHPWVTGKA 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
12-271 1.69e-42

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: 148.64  E-value: 1.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd14184   3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGK--EHLIENEVSILRRVKHPNIIMLIEEMDTP-AELYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRClrddSG 167
Cdd:cd14184  80 LVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV----EG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMAlskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQ-KEHRVNFPRS--KHLTG 243
Cdd:cd14184 156 PLY---TVCGTPTYVAPEIIAETGYGLKV-DIWAAGVITYILLCGFPPFrSENNLQEDLFDQiLLGKLEFPSPywDNITD 231
                       250       260
                ....*....|....*....|....*...
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14184 232 SAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
12-271 1.18e-41

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: 146.63  E-value: 1.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGK--EDMIESEILIIKSLSHPNIVKLFEVYETE-KEIYLILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRCLRDdsg 167
Cdd:cd14185  79 YVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGP--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmalSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY--DDSNIKKMLRIQKEHRVNF--PRSKHLTG 243
Cdd:cd14185 156 ----IFTVCGTPTYVAPEILSEKGYGLEV-DMWAAGVILYILLCGFPPFrsPERDQEELFQIIQLGHYEFlpPYWDNISE 230
                       250       260
                ....*....|....*....|....*...
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14185 231 AAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
11-272 1.56e-41

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: 147.20  E-value: 1.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKV-KSAYSERLKFNVAIKIIdRKKAPADFLEKFLPR-----EIEILAMLNHCSIIKTYEIFETSHg 84
Cdd:cd14096   2 NYRLINKIGEGAFSNVyKAVPLRNTGKPVAIKVV-RKADLSSDNLKGSSRanilkEVQIMKRLSHPNIVKLLDFQESDE- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDK-DFN-------------- 149
Cdd:cd14096  80 YYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPiPFIpsivklrkadddet 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 150 ------------------IKLSDFSFSKRcLRDDSgrmalSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC 211
Cdd:cd14096 160 kvdegefipgvggggigiVKLADFGLSKQ-VWDSN-----TKTPCGTVGYTAPEVVKDERYSKKV-DMWALGCVLYTLLC 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 212 GSMPYDDSNIKKMLriQKEHRVNF----PRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14096 233 GFPPFYDESIETLT--EKISRGDYtflsPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
18-261 3.59e-41

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: 146.98  E-value: 3.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK------IIDRKKAPADFLEKflpreiEILAMLNHCS-IIKTYEIFETSHgKVYIVM 90
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKvlkkevIIEDDDVECTMTEK------RVLALANRHPfLTGLHACFQTED-RLYFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALheDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgr 168
Cdd:cd05570  76 EYVNGGDLMFHIQRARRF--TEERARFYaaEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGN-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 maLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKDL 248
Cdd:cd05570 152 --TTSTFCGTPDYIAPEILREQDYGFSV-DWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPR--WLSREAVSI 226
                       250
                ....*....|...
gi 14042947 249 IYHMLQPDVNRRL 261
Cdd:cd05570 227 LKGLLTKDPARRL 239
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-273 5.40e-41

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: 145.49  E-value: 5.40e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKK--APADFLEKFLPR---------------------EIEILAMLN 68
Cdd:cd14199   4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmRQAGFPRRPPPRgaraapegctqprgpiervyqEIAILKKLD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  69 HCSIIKTYEIFET-SHGKVYIVMELAVQGDLLElIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD 147
Cdd:cd14199  84 HPNVVKLVEVLDDpSEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGED 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 148 FNIKLSDFSFSKRClrddSGRMALSKTFCGSPAYAAPEVLQGIP--YQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKML 225
Cdd:cd14199 163 GHIKIADFGVSNEF----EGSDALLTNTVGTPAFMAPETLSETRkiFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 226 RIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14199 239 SKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
18-272 7.15e-41

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: 144.23  E-value: 7.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14186   9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSN-YVYLVLEMCHNGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRG-ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMalskTFC 176
Cdd:cd14186  88 MSRYLKNRKkPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF----TMC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLriQKEHRVNFPRSKHLTGECKDLIYHMLQPD 256
Cdd:cd14186 164 GTPNYISPEIATRSAHGLES-DVWSLGCMFYTLLVGRPPFDTDTVKNTL--NKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                       250
                ....*....|....*.
gi 14042947 257 VNRRLHIDEILSHCWM 272
Cdd:cd14186 241 PADRLSLSSVLDHPFM 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
18-271 1.18e-40

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: 144.09  E-value: 1.18e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADfLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMElAVQGD 97
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTK-QESQLRNEVAILQQLSHPGVVNLECMFETPE-RVFVVME-KLHGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELI--KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN---IKLSDFSFSkRCLRDDSGRmals 172
Cdd:cd14082  88 MLEMIlsSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFA-RIIGEKSFR---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPY-DDSNIKKmlRIQKEHRVnFPRS--KHLTGECKDLI 249
Cdd:cd14082 163 RSVVGTPAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFnEDEDIND--QIQNAAFM-YPPNpwKEISPDAIDLI 238
                       250       260
                ....*....|....*....|..
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14082 239 NNLLQVKMRKRYSVDKSLSHPW 260
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
18-269 1.28e-40

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: 143.62  E-value: 1.28e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAP-ADFLekflpREIEILAMLNHC-SIIKTYEI-FETSHGKVYiVMELAV 94
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKlKDFL-----REYNISLELSVHpHIIKTYDVaFETEDYYVF-AQEYAP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDN-LLLDKDFN-IKLSDFSFSKRclrddsgRMALS 172
Cdd:cd13987  75 YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDKDCRrVKLCDFGLTRR-------VGSTV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQP----KVYDIWSLGVILYIMVCGSMPY-----DDSNIKKMLRIQKEHRVNFPRS-KHLT 242
Cdd:cd13987 148 KRVSGTIPYTAPEVCEAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFPWekadsDDQFYEEFVRWQKRKNTAVPSQwRRFT 227
                       250       260
                ....*....|....*....|....*..
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd13987 228 PKALRMFKKLLAPEPERRCSIKEVFKY 254
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
12-271 2.73e-40

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: 143.71  E-value: 2.73e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDrkKAPADFLEKFLpREIEILAML-NHCSIIKTYEIFETSHgKVYIVM 90
Cdd:cd14090   4 KLTGELLGEGAYASVQTCINLYTGKEYAVKIIE--KHPGHSRSRVF-REVETLHQCqGHPNILQLIEYFEDDE-RFYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL---LDKDFNIKLSDFSFSKRClRDDSG 167
Cdd:cd14090  80 EKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGI-KLSST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMALSKT-----FCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPY-----DD---------SNIKKM 224
Cdd:cd14090 159 SMTPVTTpelltPVGSAEYMAPEVVDAFVGEALSYdkrcDLWSLGVILYIMLCGYPPFygrcgEDcgwdrgeacQDCQEL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 225 L--RIQkEHRVNFPRS--KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14090 239 LfhSIQ-EGEYEFPEKewSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
14-272 3.29e-40

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: 142.79  E-value: 3.29e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELA 93
Cdd:cd14116   9 IGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDA-TRVYLILEYA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrcLRDDSGRMAlsk 173
Cdd:cd14116  88 PLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS---VHAPSSRRT--- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRiqKEHRVNFPRSKHLTGECKDLIYHML 253
Cdd:cd14116 162 TLCGTLDYLPPEMIEGRMHDEKV-DLWSLGVLCYEFLVGKPPFEANTYQETYK--RISRVEFTFPDFVTEGARDLISRLL 238
                       250
                ....*....|....*....
gi 14042947 254 QPDVNRRLHIDEILSHCWM 272
Cdd:cd14116 239 KHNPSQRPMLREVLEHPWI 257
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
18-273 6.16e-40

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: 142.46  E-value: 6.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEiFETSHGKVYIVMELAVQG 96
Cdd:cd14202  10 IGHGAFAVVfKGRHKEKHDLEVAVKCINKKNLAKS--QTLLGKEIKILKELKHENIVALYD-FQEIANSVYLVMEYCNGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD---------KDFNIKLSDFSFSkRCLRDDSg 167
Cdd:cd14202  87 DLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFA-RYLQNNM- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmaLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRV---NFPR--SKHLt 242
Cdd:cd14202 165 ---MAATLCGSPMYMAPEVIMSQHYDAKA-DLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSlspNIPRetSSHL- 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 14042947 243 gecKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14202 240 ---RQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
18-271 8.06e-40

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: 144.35  E-value: 8.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKapaDFLEK----FLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd05573   9 IGRGAFGEVWLVRDKDTGQVYAMKIL-RKS---DMLKReqiaHVRAERDILADADSPWIVRLHYAFQDED-HLYLVMEYM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR------------- 160
Cdd:cd05573  84 PGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKmnksgdresylnd 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 ------------CLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLRI 227
Cdd:cd05573 164 svntlfqdnvlaRRRPHKQRRVRAYSAVGTPDYIAPEVLRGTGYGPEC-DWWSLGVILYEMLYGFPPfYSDSLVETYSKI 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 228 --QKEHRVnFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd05573 243 mnWKESLV-FPDDPDVSPEAIDLIRRLLCDPEDRLGSAEEIKAHPF 287
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
18-271 1.43e-39

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: 140.48  E-value: 1.43e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII---DRKKAPADflekflpREIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAV 94
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIpkrDKKKEAVL-------REISILNQLQHPRIIQLHEAYESPTELV-LILELCS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD--KDFNIKLSDFSFSKRCLRDDsgrmaLS 172
Cdd:cd14006  73 GGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGE-----EL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQPkVYDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQK-EHRVNFPRSKHLTGECKDLIY 250
Cdd:cd14006 148 KEIFGTPEFVAPEIVNGEPVSL-ATDMWSIGVLTYVLLSGLSPfLGEDDQETLANISAcRVDFSEEYFSSVSQEAKDFIR 226
                       250       260
                ....*....|....*....|.
gi 14042947 251 HMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14006 227 KLLVKEPRKRPTAQEALQHPW 247
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
12-272 6.12e-39

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: 140.08  E-value: 6.12e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKK------------------APADFLEKFLP-----REIEILAMLN 68
Cdd:cd14200   2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygfprrppprgskaAQGEQAKPLAPlervyQEIAILKKLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  69 HCSIIKTYEIFET-SHGKVYIVMELAVQGDLLElIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD 147
Cdd:cd14200  82 HVNIVKLIEVLDDpAEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 148 FNIKLSDFSFSKRCLRDDSgrmALSKTfCGSPAYAAPEVL--QGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKML 225
Cdd:cd14200 161 GHVKIADFGVSNQFEGNDA---LLSST-AGTPAFMAPETLsdSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALH 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14042947 226 RIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14200 237 NKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
18-273 1.38e-38

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: 138.51  E-value: 1.38e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIF-ETSHgkVYIVMELAVQG 96
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFkDKKY--LYMLMEYCLGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrdDSGRMAlsKTFC 176
Cdd:cd05572  79 ELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKL---GSGRKT--WTFC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY---DDSNIKKMLRIQKE-HRVNFPrsKHLTGECKDLIYHM 252
Cdd:cd05572 154 GTPEYVAPEIILNKGYDFSV-DYWSLGILLYELLTGRPPFggdDEDPMKIYNIILKGiDKIEFP--KYIDKNAKNLIKQL 230
                       250       260
                ....*....|....*....|....*.
gi 14042947 253 LQPDVNRRL-----HIDEILSHCWMQ 273
Cdd:cd05572 231 LRRNPEERLgylkgGIRDIKKHKWFE 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-271 2.92e-38

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: 137.37  E-value: 2.92e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEkflpREIEILAMLN----HCSIIKTYEIFETSHGK-VYIVMEL 92
Cdd:cd05118   7 IGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAAL----REIKLLKHLNdvegHPNIVKLLDVFEHRGGNhLCLVFEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLELIKTRGALHEDEARKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFSFSkRCLRDDsgrma 170
Cdd:cd05118  83 -MGMNLYELIKDYPRGLPLDLIKSYlYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLA-RSFTSP----- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPAYAAPEV-LQGIPYQPKVyDIWSLGVILYIMVCGS-MPYDDSNIKKMLRIQKehrvnfprskhLTG--ECK 246
Cdd:cd05118 156 PYTPYVATRWYRAPEVlLGAKPYGSSI-DIWSLGCILAELLTGRpLFPGDSEVDQLAKIVR-----------LLGtpEAL 223
                       250       260
                ....*....|....*....|....*
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd05118 224 DLLSKMLKYDPAKRITASQALAHPY 248
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
9-268 3.35e-38

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: 137.76  E-value: 3.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYI 88
Cdd:cd14187   6 RRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFE-DNDFVYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGR 168
Cdd:cd14187  85 VLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 malsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKM-LRIQKEHrvnFPRSKHLTGECKD 247
Cdd:cd14187 165 ----KTLCGTPNYIAPEVLSKKGHSFEV-DIWSIGCIMYTLLVGKPPFETSCLKETyLRIKKNE---YSIPKHINPVAAS 236
                       250       260
                ....*....|....*....|.
gi 14042947 248 LIYHMLQPDVNRRLHIDEILS 268
Cdd:cd14187 237 LIQKMLQTDPTARPTINELLN 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
18-269 3.45e-38

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 137.14  E-value: 3.45e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAysERLKFN--VAIKIID----RKKAPADFLEkflprEIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd08530   8 LGKGSYGSVYKV--KRLSDNqvYALKEVNlgslSQKEREDSVN-----EIRLLASVNHPNIIRYKEAFLDGN-RLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELI----KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRddsg 167
Cdd:cd08530  80 YAPFGDLSKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKK---- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddsNIKKM--LRiQKEHRVNFPRSKHL-TGE 244
Cdd:cd08530 156 --NLAKTQIGTPLYAAPEVWKGRPYDYKS-DIWSLGCLLYEMATFRPPF---EARTMqeLR-YKVCRGKFPPIPPVySQD 228
                       250       260
                ....*....|....*....|....*
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd08530 229 LQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
12-267 3.55e-38

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 137.16  E-value: 3.55e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVME 91
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAI-DEARVLSKLNSPYVIKYYDSF-VDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKT-RGA-LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLRDDSGRM 169
Cdd:cd08529  80 YAENGDLHSLIKSqRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK--ILSDTTNF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 AlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN----IKKMLRiQKEHRVNFPRSKHLTgec 245
Cdd:cd08529 158 A--QTIVGTPYYLSPELCEDKPYNEKS-DVWALGCVLYELCTGKHPFEAQNqgalILKIVR-GKYPPISASYSQDLS--- 230
                       250       260
                ....*....|....*....|..
gi 14042947 246 kDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd08529 231 -QLIDSCLTKDYRQRPDTTELL 251
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
10-269 1.91e-37

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: 135.52  E-value: 1.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIV 89
Cdd:cd14188   1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKE-NIYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRm 169
Cdd:cd14188  80 LEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRR- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 alsKTFCGSPAYAAPEVL--QGIPYQPkvyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECKD 247
Cdd:cd14188 159 ---RTICGTPNYLSPEVLnkQGHGCES---DIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSS--LLAPAKH 230
                       250       260
                ....*....|....*....|..
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14188 231 LIASMLSKNPEDRPSLDEIIRH 252
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
17-269 2.54e-37

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: 135.36  E-value: 2.54e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKIID------RKKapadfleKFLPREIEILAMLNHCSIIKTYE-IFETSHGKVYIV 89
Cdd:cd08217   7 TIGKGSFGTVRKVRRKSDGKILVWKEIDygkmseKEK-------QQLVSEVNILRELKHPNIVRYYDrIVDRANTTLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIK----TRGALHEDEARKKFHQLSLAIKYCHDLD-----VVHRDLKCDNLLLDKDFNIKLSDFSFSkR 160
Cdd:cd08217  80 MEYCEGGDLAQLIKkckkENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGLA-R 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 CLRDDSgrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMlrIQKEHRVNFPR-SK 239
Cdd:cd08217 159 VLSHDS---SFAKTYVGTPYYMSPELLNEQSYDEKS-DIWSLGCLIYELCALHPPFQAANQLEL--AKKIKEGKFPRiPS 232
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd08217 233 RYSSELNEVIKSMLNVDPDKRPSVEELLQL 262
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
3-261 3.05e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 136.87  E-value: 3.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    3 DAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETS 82
Cdd:PTZ00263  11 DTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   83 HgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcL 162
Cdd:PTZ00263  91 N-RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-V 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  163 RDDsgrmalSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQkEHRVNFPRskHL 241
Cdd:PTZ00263 169 PDR------TFTLCGTPEYLAPEVIQSKGHG-KAVDWWTMGVLLYEFIAGYPPfFDDTPFRIYEKIL-AGRLKFPN--WF 238
                        250       260
                 ....*....|....*....|
gi 14042947  242 TGECKDLIYHMLQPDVNRRL 261
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRL 258
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
10-269 3.11e-37

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: 134.67  E-value: 3.11e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIV 89
Cdd:cd14189   1 RSYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAE-NIYIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRm 169
Cdd:cd14189  80 LELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRK- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 alsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECKDLI 249
Cdd:cd14189 159 ---KTICGTPNYLAPEVLLRQGHGPES-DVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPAS--LSLPARHLL 232
                       250       260
                ....*....|....*....|
gi 14042947 250 YHMLQPDVNRRLHIDEILSH 269
Cdd:cd14189 233 AGILKRNPGDRLTLDQILEH 252
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
18-273 6.15e-37

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: 134.84  E-value: 6.15e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd14209   9 LGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFK-DNSNLYMVMEYVPGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrddSGRmalSKTFCG 177
Cdd:cd14209  88 MFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV----KGR---TWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYHMLQPDV 257
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAV-DWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP--SHFSSDLKDLLRNLLQVDL 237
                       250       260
                ....*....|....*....|.
gi 14042947 258 NRRL-----HIDEILSHCWMQ 273
Cdd:cd14209 238 TKRFgnlknGVNDIKNHKWFA 258
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
18-269 1.19e-36

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: 135.13  E-value: 1.19e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAVQGD 97
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQT-HDRLCFVMEYANGGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmALSKTFCG 177
Cdd:cd05595  82 LFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDG----ATMKTFCG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECKDLIYHMLQPDV 257
Cdd:cd05595 158 TPEYLAPEVLEDNDYGRAV-DWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRT--LSPEAKSLLAGLLKKDP 234
                       250
                ....*....|....*..
gi 14042947 258 NRRL-----HIDEILSH 269
Cdd:cd05595 235 KQRLgggpsDAKEVMEH 251
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
18-269 1.61e-36

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: 132.72  E-value: 1.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIID-RKKApadflEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQG 96
Cdd:cd06614   8 IGEGASGEVYKATDRATGKEVAIKKMRlRKQN-----KELIINEILIMKECKHPNIVDYYDSYLVG-DELWVVMEYMDGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTF 175
Cdd:cd06614  82 SLTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKR----NSV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQ 254
Cdd:cd06614 158 VGTPYWMAPEVIKRKDYGPKV-DIWSLGIMCIEMAEGEPPYlEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFLNKCLV 236
                       250
                ....*....|....*
gi 14042947 255 PDVNRRLHIDEILSH 269
Cdd:cd06614 237 KDPEKRPSAEELLQH 251
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
18-273 2.14e-36

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: 133.12  E-value: 2.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIID----RKKAPADF--LEKFLPREIEILAMLN-HCSIIKTYEIFETsHGKVYIVM 90
Cdd:cd14182  11 LGRGVSSVVRRCIHKPTRQEYAVKIIDitggGSFSPEEVqeLREATLKEIDILRKVSgHPNIIQLKDTYET-NTFFFLVF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrCLRDDSGRMa 170
Cdd:cd14182  90 DLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFS--CQLDPGEKL- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 lsKTFCGSPAYAAPEVLQGI--PYQP---KVYDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNFPRSKHLTG 243
Cdd:cd14182 167 --REVCGTPGYLAPEIIECSmdDNHPgygKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRmiMSGNYQFGSPEWDDRSD 244
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14182 245 TVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
18-273 2.98e-36

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: 132.94  E-value: 2.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApaDFLEKFLPrEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESE--EELEDFMV-EIDILSECKHPNIVGLYEAY-FYENKLWILIEFCDGGA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFC 176
Cdd:cd06611  89 LDSIMlELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKR----DTFI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVL-----QGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKDLIY 250
Cdd:cd06611 165 GTPYWMAPEVVacetfKDNPYDYKA-DIWSLGITLIELAQMEPPHHELNpMRVLLKILKSEPPTLDQPSKWSSSFNDFLK 243
                       250       260
                ....*....|....*....|...
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd06611 244 SCLVKDPDDRPTAAELLKHPFVS 266
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
18-261 3.55e-36

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: 133.68  E-value: 3.55e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksayserlkFNVaiKIIDRKKAPADFLEKFLPR---------------EIEILAMLNHCSIIKTYEIFETS 82
Cdd:cd05584   4 LGKGGYGKV---------FQV--RKTTGSDKGKIFAMKVLKKasivrnqkdtahtkaERNILEAVKHPFIVDLHYAFQTG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  83 hGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCL 162
Cdd:cd05584  73 -GKLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 RDDsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPrsKHLT 242
Cdd:cd05584 152 HDG----TVTHTFCGTIEYMAPEILTRSGHGKAV-DWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLP--PYLT 224
                       250
                ....*....|....*....
gi 14042947 243 GECKDLIYHMLQPDVNRRL 261
Cdd:cd05584 225 NEARDLLKKLLKRNVSSRL 243
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
12-272 5.86e-36

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: 131.66  E-value: 5.86e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVME 91
Cdd:cd14183   8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGK--EHMIQNEVSILRRVKHPNIVLLIEEMDM-PTELYLVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRClrddSG 167
Cdd:cd14183  85 LVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVV----DG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMAlskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQK--EHRVNFPRS--KHLTG 243
Cdd:cd14183 161 PLY---TVCGTPTYVAPEIIAETGYGLKV-DIWAAGVITYILLCGFPPFRGSGDDQEVLFDQilMGQVDFPSPywDNVSD 236
                       250       260
                ....*....|....*....|....*....
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14183 237 SAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
15-269 1.15e-35

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 130.60  E-value: 1.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  15 GINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLE--KFLPREIEILAMLNHCSIIKTYEIfETSHGKVYIVMEL 92
Cdd:cd06632   5 GQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSREsvKQLEQEIALLSKLRHPNIVQYYGT-EREEDNLYIFLEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrddSGRMALS 172
Cdd:cd06632  84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVE---AFSFAKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 ktFCGSPAYAAPEVL--QGIPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHRVNfPRSKHLTGECKDLI 249
Cdd:cd06632 161 --FKGSPYWMAPEVImqKNSGYGLAV-DIWSLGCTVLEMATGKPPWSQyEGVAAIFKIGNSGELP-PIPDHLSPDAKDFI 236
                       250       260
                ....*....|....*....|
gi 14042947 250 YHMLQPDVNRRLHIDEILSH 269
Cdd:cd06632 237 RLCLQRDPEDRPTASQLLEH 256
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-272 1.52e-35

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: 131.71  E-value: 1.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14168  18 LGTGAFSEVVLAEERATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYESPN-HLYLVMQLVSGGE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRclrddSGRMALSKT 174
Cdd:cd14168  95 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKM-----EGKGDVMST 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNFPRSKHLTGECKDLIYHM 252
Cdd:cd14168 170 ACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEqiLKADYEFDSPYWDDISDSAKDFIRNL 248
                       250       260
                ....*....|....*....|
gi 14042947 253 LQPDVNRRLHIDEILSHCWM 272
Cdd:cd14168 249 MEKDPNKRYTCEQALRHPWI 268
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-301 1.75e-35

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 131.70  E-value: 1.75e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkapadfLEKFLPREIEILAMLN-HCSIIKTYEIFetsHGKV--YIVMELAV 94
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIVSKR------MEANTQREIAALKLCEgHPNIVKLHEVY---HDQLhtFLVMELLK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL-DKDFN--IKLSDFSFSKRCLRDDSgrmaL 171
Cdd:cd14179  86 GGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtDESDNseIKIIDFGFARLKPPDNQ----P 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD--------DSNIKKMLRIQK-EHRVNFPRSKHLT 242
Cdd:cd14179 162 LKTPCFTLHYAAPELLNYNGYDESC-DLWSLGVILYTMLSGQVPFQchdksltcTSAEEIMKKIKQgDFSFEGEAWKNVS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSpsvainkegessrgTEPLWTPE 301
Cdd:cd14179 241 QEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLS--------------SNPLMTPD 285
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
14-277 2.64e-35

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: 129.98  E-value: 2.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd14117  10 IGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRK-RIYLILEYA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrcLRDDSGRmalSK 173
Cdd:cd14117  89 PRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS---VHAPSLR---RR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHrVNFPRSkhLTGECKDLIYHM 252
Cdd:cd14117 163 TMCGTLDYLPPEMIEGRTHDEKV-DLWCIGVLCYELLVGMPPFESaSHTETYRRIVKVD-LKFPPF--LSDGSRDLISKL 238
                       250       260
                ....*....|....*....|....*
gi 14042947 253 LQPDVNRRLHIDEILSHCWMQPKAR 277
Cdd:cd14117 239 LRYHPSERLPLKGVMEHPWVKANSR 263
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-279 2.76e-35

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: 129.58  E-value: 2.76e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERL---KFNVAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAV 94
Cdd:cd00192   3 LGEGAFGEVYKGKLKGGdgkTVDVAVKTL-KEDASESERKDFL-KEARVMKKLGHPNVVRLLGVC-TEEEPLYLVMEYME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKF---------HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDD 165
Cdd:cd00192  80 GGDLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRMALSKTFcgsPA-YAAPEVLQGipyqpKVY----DIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRS 238
Cdd:cd00192 160 YYRKKTGGKL---PIrWMAPESLKD-----GIFtsksDVWSFGVLLWeIFTLGATPYPGlSNEEVLEYLRKGYRLPKPEN 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 14042947 239 khltgeCKDLIYhmlqpdvnrrlhidEILSHCWMQ-PKARGS 279
Cdd:cd00192 232 ------CPDELY--------------ELMLSCWQLdPEDRPT 253
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
18-269 4.42e-35

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: 129.40  E-value: 4.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFleKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd06610   9 IGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSM--DELRKEIQAMSQCNHPNVVSYYTSFVVGD-ELWLVMPLLSGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKT---RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDDSGRMALS-K 173
Cdd:cd06610  86 LLDIMKSsypRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSA-SLATGGDRTRKVrK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVL-QGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKK--MLRIQKehrvNFPR------SKHLTGE 244
Cdd:cd06610 165 TFVGTPCWMAPEVMeQVRGYDFKA-DIWSFGITAIELATGAAPYSKYPPMKvlMLTLQN----DPPSletgadYKKYSKS 239
                       250       260
                ....*....|....*....|....*
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd06610 240 FRKMISLCLQKDPSKRPTAEELLKH 264
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
18-273 5.86e-35

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: 128.86  E-value: 5.86e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQGD 97
Cdd:cd06623   9 LGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEE--FRKQLLRELKTLRSCESPYVVKCYGAFYKE-GEISIVLEYMDGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCH-DLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDdsgRMALSKTFC 176
Cdd:cd06623  86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISK-VLEN---TLDQCNTFV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYqpkVY--DIWSLGVILYIMVCGSMPYDDSNIKK----MLRIQKEHrVNFPRSKHLTGECKDLIY 250
Cdd:cd06623 162 GTVTYMSPERIQGESY---SYaaDIWSLGLTLLECALGKFPFLPPGQPSffelMQAICDGP-PPSLPAEEFSPEFRDFIS 237
                       250       260
                ....*....|....*....|...
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd06623 238 ACLQKDPKKRPSAAELLQHPFIK 260
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-267 6.52e-35

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: 128.54  E-value: 6.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFlPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd08225   8 IGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEAS-KKEVILLAKMKHPNIVTFFASFQ-ENGRLFIVMEYCDGGD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELI-KTRGAL-HEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNI-KLSDFSFSkRCLRDDsgrMALSKT 174
Cdd:cd08225  86 LMKRInRQRGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIA-RQLNDS---MELAYT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKM-LRIQKEHRVnfPRSKHLTGECKDLIYHML 253
Cdd:cd08225 162 CVGTPYYLSPEICQNRPYNNKT-DIWSLGCVLYELCTLKHPFEGNNLHQLvLKICQGYFA--PISPNFSRDLRSLISQLF 238
                       250
                ....*....|....
gi 14042947 254 QPDVNRRLHIDEIL 267
Cdd:cd08225 239 KVSPRDRPSITSIL 252
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
38-269 8.25e-35

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: 128.57  E-value: 8.25e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIDRKKAPAdflekfLPREIEILAMLNHCSIIKTYEIFETS-HgkVYIVMELAVQGDLLELIKTRGALHEDEARKK 116
Cdd:cd14010  28 VAIKCVDKSKRPE------VLNEVRLTHELKHPNVLKFYEWYETSnH--LWLVVEYCTGGDLETLLRQDGNLPESSVRKF 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 117 FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR------------CLRDDSGRMALSKTFCGSPAYAAP 184
Cdd:cd14010 100 GRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARRegeilkelfgqfSDEGNVNKVSKKQAKRGTPYYMAP 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 185 EVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTG---ECKDLIYHMLQPDVNRRL 261
Cdd:cd14010 180 ELFQGGVHS-FASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVSSKpspDFKSLLKGLLEKDPAKRL 258

                ....*...
gi 14042947 262 HIDEILSH 269
Cdd:cd14010 259 SWDELVKH 266
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
39-271 9.82e-35

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: 128.37  E-value: 9.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  39 AIKIIdrKKAPADFLEKFLPREIEILAMLNHCS---IIKTYEIFEtSHGKVYIVMELAVQGDLLELIKTRGALHEDEARK 115
Cdd:cd05611  25 AIKVL--KKSDMIAKNQVTNVKAERAIMMIQGEspyVAKLYYSFQ-SKDYLYLVMEYLNGGDCASLIKTLGGLPEDWAKQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 116 KFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrclrddsgRMAL----SKTFCGSPAYAAPEVLQGIP 191
Cdd:cd05611 102 YIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS---------RNGLekrhNKKFVGTPDYLAPETILGVG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 192 yQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKH--LTGECKDLIYHMLQPDVNRRLH---IDEI 266
Cdd:cd05611 173 -DDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKefCSPEAVDLINRLLCMDPAKRLGangYQEI 251

                ....*
gi 14042947 267 LSHCW 271
Cdd:cd05611 252 KSHPF 256
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
18-269 1.35e-34

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: 128.55  E-value: 1.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIID---RKKAPADFLEKFLP--REIEILAML-NHCSIIKTYEIFETShGKVYIVME 91
Cdd:cd14181  18 IGRGVSSVVRRCVHRHTGQEFAVKIIEvtaERLSPEQLEEVRSStlKEIHILRQVsGHPSIITLIDSYESS-TFIFLVFD 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrCLRDDSGRMal 171
Cdd:cd14181  97 LMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFS--CHLEPGEKL-- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 sKTFCGSPAYAAPEVL-----QGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNF--PRSKHLTGE 244
Cdd:cd14181 173 -RELCGTPGYLAPEILkcsmdETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssPEWDDRSST 251
                       250       260
                ....*....|....*....|....*
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14181 252 VKDLISRLLVVDPEIRLTAEQALQH 276
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
11-281 2.15e-34

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: 128.21  E-value: 2.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDR-KKAPADflekflprEIEILAML-NHCSIIKTYEIFETshGK-VY 87
Cdd:cd14178   4 GYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKsKRDPSE--------EIEILLRYgQHPNIITLKDVYDD--GKfVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFN---IKLSDFSFSKRcLR 163
Cdd:cd14178  74 LVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQ-LR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGrmaLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY----DDSNIKKMLRI-QKEHRVNFPRS 238
Cdd:cd14178 153 AENG---LLMTPCYTANFVAPEVLKRQGYDAAC-DIWSLGILLYTMLAGFTPFangpDDTPEEILARIgSGKYALSGGNW 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 14042947 239 KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPS 281
Cdd:cd14178 229 DSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSQN 271
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-273 3.39e-34

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: 126.89  E-value: 3.39e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAY--SERLKfnVAIKIIDRK------KAPADFLekfLPREIEILAML----NHCSIIKTYEIF 79
Cdd:cd14101   2 YTMGNLLGKGGFGTVYAGHriSDGLQ--VAIKQISRNrvqqwsKLPGVNP---VPNEVALLQSVgggpGHRGVIRLLDWF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  80 ETSHGkVYIVME--LAVQgDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFS 156
Cdd:cd14101  77 EIPEG-FLLVLErpQHCQ-DLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 157 fSKRCLRDdsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYD-DSNIKKMlriqkehRVNF 235
Cdd:cd14101 155 -SGATLKD-----SMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFErDTDILKA-------KPSF 221
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 14042947 236 PrsKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14101 222 N--KRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
11-275 3.42e-34

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: 127.84  E-value: 3.42e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDR-KKAPADflekflprEIEILAML-NHCSIIKTYEIFEtsHGK-VY 87
Cdd:cd14175   2 GYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKsKRDPSE--------EIEILLRYgQHPNIITLKDVYD--DGKhVY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFN---IKLSDFSFSKRcLR 163
Cdd:cd14175  72 LVTELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQ-LR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGrmaLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY----DDSNIKKMLRI-QKEHRVNFPRS 238
Cdd:cd14175 151 AENG---LLMTPCYTANFVAPEVLKRQGYDEGC-DIWSLGILLYTMLAGYTPFangpSDTPEEILTRIgSGKFTLSGGNW 226
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 14042947 239 KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPK 275
Cdd:cd14175 227 NTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQK 263
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-272 4.01e-34

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 126.70  E-value: 4.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCS-IIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd14106  16 LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEIL-HEIAVLELCKDCPrVVNLHEVYETRS-ELILILELAAGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN---IKLSDFSFSKRCLRDDSGRMALsk 173
Cdd:cd14106  94 ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVIGEGEEIREIL-- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 tfcGSPAYAAPEVLQgipYQP--KVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKeHRVNFPRS--KHLTGECKDL 248
Cdd:cd14106 172 ---GTPDYVAPEILS---YEPisLATDMWSIGVLTYVLLTGHSPFgGDDKQETFLNISQ-CNLDFPEElfKDVSPLAIDF 244
                       250       260
                ....*....|....*....|....
gi 14042947 249 IYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14106 245 IKRLLVKDPEKRLTAKECLEHPWL 268
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
18-273 4.25e-34

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: 127.05  E-value: 4.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLKFNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd14201  14 VGHGAFAVVfKGRHRKKTDWEVAIKSINKKNLSKS--QILLGKEIKILKELQHENIVALYDVQEMPN-SVFLVMEYCNGG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD---------KDFNIKLSDFSFSKRClrdDSG 167
Cdd:cd14201  91 DLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYL---QSN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMAlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYdDSNIKKMLRIQKEHRVNFPRS--KHLTGEC 245
Cdd:cd14201 168 MMA--ATLCGSPMYMAPEVIMSQHYDAKA-DLWSIGTVIYQCLVGKPPF-QANSPQDLRMFYEKNKNLQPSipRETSPYL 243
                       250       260
                ....*....|....*....|....*...
gi 14042947 246 KDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14201 244 ADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-272 8.37e-34

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: 125.87  E-value: 8.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII-DRKKAPadflekflpREIEILAMLNHCS-IIKTYEIFETSH-GK--VYIVMEL 92
Cdd:cd14172  12 LGLGVNGKVLECFHRRTGQKCALKLLyDSPKAR---------REVEHHWRASGGPhIVHILDVYENMHhGKrcLLIIMEC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKrclrDDSG 167
Cdd:cd14172  83 MEGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAK----ETTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMALsKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSN-------IKKMLRIQKEHRVNfPRSKH 240
Cdd:cd14172 159 QNAL-QTPCYTPYYVAPEVLGPEKYD-KSCDMWSLGVIMYILLCGFPPFYSNTgqaispgMKRRIRMGQYGFPN-PEWAE 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14172 236 VSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
15-271 9.27e-34

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: 125.88  E-value: 9.27e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  15 GINLGEGSYAKVKSAYSerLKFN--VAIKII-----DRKKAPAdflekfLPREIEILAMLNHCSIIKTYEIfETSHGKVY 87
Cdd:cd06626   5 GNKIGEGTFGKVYTAVN--LDTGelMAMKEIrfqdnDPKTIKE------IADEMKVLEGLDHPNLVRYYGV-EVHREEVY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCL-RDDS 166
Cdd:cd06626  76 IFMEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKnNTTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRMALSKTFCGSPAYAAPEVLQGIPYQPKV--YDIWSLGVILYIMVCGSMPYD--DSNIKKMLRIQKEHRVNFPRSKHLT 242
Cdd:cd06626 156 MAPGEVNSLVGTPAYMAPEVITGNKGEGHGraADIWSLGCVVLEMATGKRPWSelDNEWAIMYHVGMGHKPPIPDSLQLS 235
                       250       260
                ....*....|....*....|....*....
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd06626 236 PEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
17-271 1.13e-33

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: 126.06  E-value: 1.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKIIdrkkaPADFLEKFLP----REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMEL 92
Cdd:cd07829   6 KLGEGTYGVVYKAKDKKTGEIVALKKI-----RLDNEEEGIPstalREISLLKELKHPNIVKLLDVI-HTENKLYLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrclrddsgrmaL 171
Cdd:cd07829  80 -CDQDLKKYLDKRpGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFG--------------L 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFcGSPA-----------YAAPEVLQGIP-YQPKVyDIWSLGVILYIM---------------------VCG------ 212
Cdd:cd07829 145 ARAF-GIPLrtythevvtlwYRAPEILLGSKhYSTAV-DIWSVGCIFAELitgkplfpgdseidqlfkifqILGtptees 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 213 -----SMPYDDSNIKKMLRIQKEHRvnFPRskhLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07829 223 wpgvtKLPDYKPTFPKWPKNDLEKV--LPR---LDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
12-272 1.23e-33

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: 126.28  E-value: 1.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDR-KKAPADflekflprEIEILAML-NHCSIIKTYEIFETSHgKVYIV 89
Cdd:cd14177   6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKsKRDPSE--------EIEILMRYgQHPNIITLKDVYDDGR-YVYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFN---IKLSDFSFSKRcLRDD 165
Cdd:cd14177  77 TELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQ-LRGE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGrmaLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY----DDSNIKKMLRIQKEhrvNFPRS--- 238
Cdd:cd14177 156 NG---LLLTPCYTANFVAPEVLMRQGYDAAC-DIWSLGVLLYTMLAGYTPFangpNDTPEEILLRIGSG---KFSLSggn 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 14042947 239 -KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14177 229 wDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
18-273 1.47e-33

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: 125.91  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkapADFLEKFLPREIEILAMLN-HCSIIKTYEIFETShGKVYIVMELAVQG 96
Cdd:cd14174  10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKN---AGHSRSRVFREVETLYQCQgNKNILELIEFFEDD-TRFYLVFEKLRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRcLRDDSGRMALS- 172
Cdd:cd14174  86 SILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSG-VKLNSACTPITt 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 ---KTFCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPY----------DDSNI-----KKMLRIQKE 230
Cdd:cd14174 165 pelTTPCGSAEYMAPEVVEVFTDEATFYdkrcDLWSLGVILYIMLSGYPPFvghcgtdcgwDRGEVcrvcqNKLFESIQE 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 14042947 231 HRVNFPRS--KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14174 245 GKYEFPDKdwSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
60-269 1.75e-33

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: 124.85  E-value: 1.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQGDLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLDVVHRDL 137
Cdd:cd08220  49 EVKVLSMLHHPNIIEYYESFLEDKA-LMIVMEYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 138 KCDNLLLDKDFNI-KLSDFSFSKrCLRDDSgrmaLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd08220 128 KTQNILLNKKRTVvKIGDFGISK-ILSSKS----KAYTVVGTPCYISPELCEGKPYNQKS-DIWALGCVLYELASLKRAF 201
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14042947 217 DDSNIKKMlrIQKEHRVNF-PRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd08220 202 EAANLPAL--VLKIMRGTFaPISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
18-274 1.88e-33

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: 126.32  E-value: 1.88e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV---KSAYSERLkfnVAIKIIDRKKAPA-DFLEKFLPrEIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd05571   3 LGKGTFGKVilcREKATGEL---YAIKILKKEVIIAkDEVAHTLT-ENRVLQNTRHPFLTSLKYSFQTND-RLCFVMEYV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDdsGRMalSK 173
Cdd:cd05571  78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISY--GAT--TK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKDLIYHML 253
Cdd:cd05571 154 TFCGTPEYLAPEVLEDNDYGRAV-DWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPS--TLSPEAKSLLAGLL 230
                       250       260
                ....*....|....*....|....*.
gi 14042947 254 QPDVNRRL-----HIDEILSHCWMQP 274
Cdd:cd05571 231 KKDPKKRLgggprDAKEIMEHPFFAS 256
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
18-267 2.57e-33

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: 124.54  E-value: 2.57e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIID-RKKAPADFLEKflPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQG 96
Cdd:cd08218   8 IGEGSFGKALLVKSKEDGKQYVIKEINiSKMSPKEREES--RKEVAVLSKMKHPNIVQYQESFEEN-GNLYIVMDYCDGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELI-KTRGAL-HEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDsgrMALSKT 174
Cdd:cd08218  85 DLYKRInAQRGVLfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIA-RVLNST---VELART 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMlrIQKEHRVNFPR-SKHLTGECKDLIYHML 253
Cdd:cd08218 161 CIGTPYYLSPEICENKPYNNKS-DIWALGCVLYEMCTLKHAFEAGNMKNL--VLKIIRGSYPPvPSRYSYDLRSLVSQLF 237
                       250
                ....*....|....
gi 14042947 254 QPDVNRRLHIDEIL 267
Cdd:cd08218 238 KRNPRDRPSINSIL 251
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
16-271 3.53e-33

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: 124.86  E-value: 3.53e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKtyeIFETSHGK--VYIVMELA 93
Cdd:cd05612   7 KTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIR---LFWTEHDQrfLYMLMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSGrmalsk 173
Cdd:cd05612  84 PGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKK-LRDRTW------ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKDLIYHML 253
Cdd:cd05612 157 TLCGTPEYLAPEVIQSKGHNKAV-DWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPR--HLDLYAKDLIKKLL 233
                       250       260
                ....*....|....*....|...
gi 14042947 254 QPDVNRRL-----HIDEILSHCW 271
Cdd:cd05612 234 VVDRTRRLgnmknGADDVKNHRW 256
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
12-272 9.87e-33

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: 123.21  E-value: 9.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD---FLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYI 88
Cdd:cd14194   7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgVSREDIEREVSILKEIQHPNVITLHEVYENKT-DVIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDN-LLLDKDF---NIKLSDFSFSKRClrd 164
Cdd:cd14194  86 ILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKIIDFGLAHKI--- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGRMAlsKTFCGSPAYAAPEVLQgipYQP--KVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KH 240
Cdd:cd14194 163 DFGNEF--KNIFGTPEFVAPEIVN---YEPlgLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEyfSN 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14194 238 TSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
16-269 1.46e-32

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: 122.55  E-value: 1.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaVQ 95
Cdd:cd06648  13 VKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQR---RELLFNEVVIMRDYQHPNIVEMYSSYLVGD-ELWVVMEF-LE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTF 175
Cdd:cd06648  88 GGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRR----KSL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQ 254
Cdd:cd06648 164 VGTPYWMAPEVISRLPYGTEV-DIWSLGIMVIEMVDGEPPYfNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRMLV 242
                       250
                ....*....|....*
gi 14042947 255 PDVNRRLHIDEILSH 269
Cdd:cd06648 243 RDPAQRATAAELLNH 257
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
39-272 2.06e-32

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: 122.96  E-value: 2.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  39 AIKI-IDRKKApadflekflprEIEI-LAML--NHCSIIKTYEIF---------ETSHGKVYIVMELAVQGDLLELIKTR 105
Cdd:cd14171  35 ALKIlLDRPKA-----------RTEVrLHMMcsGHPNIVQIYDVYansvqfpgeSSPRARLLIVMELMEGGELFDRISQH 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 106 GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDK---DFNIKLSDFSFSKrclrDDSGRMalsKTFCGSPAYA 182
Cdd:cd14171 104 RHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDnseDAPIKLCDFGFAK----VDQGDL---MTPQFTPYYV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 183 APEVLQ----------GIPYQPKVY------DIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQKEH----RVNFPRS--K 239
Cdd:cd14171 177 APQVLEaqrrhrkersGIPTSPTPYtydkscDMWSLGVIIYIMLCGYPPfYSEHPSRTITKDMKRKimtgSYEFPEEewS 256
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14171 257 QISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
79-273 2.17e-32

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: 122.12  E-value: 2.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FETShGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05583  68 FQTD-AKLHLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLS 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KRCLRDDSGRmalSKTFCGSPAYAAPEVLQGIPY-QPKVYDIWSLGVILYIMVCGSMPY---DDSNIKKML--RIQKEHR 232
Cdd:cd05583 147 KEFLPGENDR---AYSFCGTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFtvdGERNSQSEIskRILKSHP 223
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 233 vnfPRSKHLTGECKDLIYHMLQPDVNRRL-----HIDEILSHCWMQ 273
Cdd:cd05583 224 ---PIPKTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFK 266
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
12-272 2.44e-32

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: 122.37  E-value: 2.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD---FLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYI 88
Cdd:cd14196   7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgVSREEIEREVSILRQVLHPNIITLHDVYE-NRTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDN-LLLDKDF---NIKLSDFSFSKRClrD 164
Cdd:cd14196  86 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEI--E 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGRMalsKTFCGSPAYAAPEVlqgIPYQP--KVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KH 240
Cdd:cd14196 164 DGVEF---KNIFGTPEFVAPEI---VNYEPlgLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffSH 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14196 238 TSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
18-274 2.73e-32

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: 123.26  E-value: 2.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD------FLEKflpreiEILAMLNHCS-IIKTYEIFET-SHgkVYIV 89
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDddvectMIER------RVLALASQHPfLTHLFCTFQTeSH--LFFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgRM 169
Cdd:cd05592  75 MEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGE--NK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 AlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKDLI 249
Cdd:cd05592 153 A--STFCGTPDYIAPEILKGQKYNQSV-DWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPR--WLTKEAASCL 227
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 250 YHMLQPDVNRRLHIDE-----ILSHCWMQP 274
Cdd:cd05592 228 SLLLERNPEKRLGVPEcpagdIRDHPFFKT 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
11-268 4.29e-32

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: 121.22  E-value: 4.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIID-----RKKAPADFLekflpREIEILAMLNHCSIIKTYEIFeTSHGK 85
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemmDAKARQDCL-----KEIDLLQQLNHPNIIKYLASF-IENNE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELIKTRGA----LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFskrc 161
Cdd:cd08224  75 LNIVLELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 162 lrddsGRMALSKTF-----CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFP 236
Cdd:cd08224 151 -----GRFFSSKTTaahslVGTPYYMSPERIREQGYDFKS-DIWSLGCLLYEMAALQSPFYGEKMNLYSLCKKIEKCEYP 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 237 --RSKHLTGECKDLIYHMLQPDVNRRLHIDEILS 268
Cdd:cd08224 225 plPADLYSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
18-269 7.16e-32

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: 120.81  E-value: 7.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06609   9 IGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIED--IQQEIQFLSQCDSPYITKYYGSF-LKGSKLWIIMEYCGGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKtRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSGRMalsKTFCG 177
Cdd:cd06609  86 VLDLLK-PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQ-LTSTMSKR---NTFVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSKHlTGECKDLIYHMLQPD 256
Cdd:cd06609 161 TPFWMAPEVIKQSGYDEKA-DIWSLGITAIELAKGEPPLSDlHPMRVLFLIPKNNPPSLEGNKF-SKPFKDFVELCLNKD 238
                       250
                ....*....|...
gi 14042947 257 VNRRLHIDEILSH 269
Cdd:cd06609 239 PKERPSAKELLKH 251
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
19-272 7.89e-32

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: 120.44  E-value: 7.89e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDL 98
Cdd:cd05578   9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEE-DMYMVVDLLLGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  99 LELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSgrmaLSKTFCGS 178
Cdd:cd05578  88 RYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIA-TKLTDGT----LATSTSGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 179 PAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD---DSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYHMLQP 255
Cdd:cd05578 163 KPYMAPEVFMRAGYSFAV-DWWSLGVTAYEMLRGKRPYEihsRTSIEEIRAKFETASVLYP--AGWSEEAIDLINKLLER 239
                       250
                ....*....|....*...
gi 14042947 256 DVNRRL-HIDEILSHCWM 272
Cdd:cd05578 240 DPQKRLgDLSDLKNHPYF 257
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-301 9.91e-32

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: 121.52  E-value: 9.91e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkapadfLEKFLPREIEILAML-NHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRR------MEANTQREVAALRLCqSHPNIVALHEVLHDQY-HTYLVMELLRGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN---IKLSDFSFSKrcLRDDSGRMAlsK 173
Cdd:cd14180  87 ELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFAR--LRPQGSRPL--Q 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKK--------MLRIqKEHRVNFPRS--KHLTG 243
Cdd:cd14180 163 TPCFTLQYAAPELFSNQGYD-ESCDLWSLGVILYTMLSGQVPFQSKRGKMfhnhaadiMHKI-KEGDFSLEGEawKGVSE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWMQpkargspsvainkeGESSRGTEPLWTPE 301
Cdd:cd14180 241 EAKDLVRGLLTVDPAKRLKLSELRESDWLQ--------------GGSALSSTPLMTPD 284
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
18-220 1.10e-31

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: 121.94  E-value: 1.10e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAML-NHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPD-RLFFVMEFVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELI-KTRgalHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmALSK 173
Cdd:cd05590  82 DLMFHIqKSR---RFDEARARFYaaEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNG----KTTS 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 14042947 174 TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN 220
Cdd:cd05590 155 TFCGTPDYIAPEILQEMLYGPSV-DWWAMGVLLYEMLCGHAPFEAEN 200
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
18-279 1.24e-31

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 119.94  E-value: 1.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     18 LGEGSYAKVKSAY----SERLKFNVAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELA 93
Cdd:smart00219   7 LGEGAFGEVYKGKlkgkGGKKKVEVAVKTL-KEDASEQQIEEFL-REARIMRKLDHPNVVKLLGVC-TEEEPLYIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     94 VQGDLLE-LIKTRGALHEDEaRKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAL 171
Cdd:smart00219  84 EGGDLLSyLRKNRPKLSLSD-LLSFaLQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRKRG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    172 SKtfcgSP-AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSkhltgeCKDL 248
Cdd:smart00219 163 GK----LPiRWMAPESLKEGKFTSKS-DVWSFGVLLWeIFTLGEQPYPGmSNEEVLEYLKNGYRLPQPPN------CPPE 231
                          250       260       270
                   ....*....|....*....|....*....|..
gi 14042947    249 IYhmlqpdvnrrlhidEILSHCWM-QPKARGS 279
Cdd:smart00219 232 LY--------------DLMLQCWAeDPEDRPT 249
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
18-269 1.35e-31

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: 119.68  E-value: 1.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkapADFLEkfLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06612  11 LGEGSYGSVYKAIHKETGQVVAIKVVPVE---EDLQE--IIKEISILKQCDSPYIVKYYGSY-FKNTDLWIVMEYCGAGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIK-TRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrddSGRMALSKTFC 176
Cdd:cd06612  85 VSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQL----TDTMAKRNTVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQP 255
Cdd:cd06612 161 GTPFWMAPEVIQEIGYNNKA-DIWSLGITAIEMAEGKPPYSDIHpMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVK 239
                       250
                ....*....|....
gi 14042947 256 DVNRRLHIDEILSH 269
Cdd:cd06612 240 DPEERPSAIQLLQH 253
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
18-272 1.76e-31

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: 120.52  E-value: 1.76e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkaPADFLEKFLpREIEILAMLN-HCSIIKTYEIFEtSHGKVYIVMELAVQG 96
Cdd:cd14173  10 LGEGAYARVQTCINLITNKEYAVKIIEKR--PGHSRSRVF-REVEMLYQCQgHRNVLELIEFFE-EEDKFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNI---KLSDFSF-SKRCLRDDSGRMALS 172
Cdd:cd14173  86 SILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLgSGIKLNSDCSPISTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 K--TFCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPY-----DDSN---------IKKMLRIQ-KEH 231
Cdd:cd14173 166 EllTPCGSAEYMAPEVVEAFNEEASIYdkrcDLWSLGVILYIMLSGYPPFvgrcgSDCGwdrgeacpaCQNMLFESiQEG 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 14042947 232 RVNFPRSK--HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14173 246 KYEFPEKDwaHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
39-261 1.79e-31

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: 120.80  E-value: 1.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  39 AIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTR--GALHEDEARKK 116
Cdd:cd05574  30 AMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTST-HLCFVMDYCPGGELFRLLQKQpgKRLPEEVARFY 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 117 FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRC----------LRDDSGRM---------------AL 171
Cdd:cd05574 109 AAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSsvtpppvrksLRKGSRRSsvksieketfvaepsAR 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR-IQKEhRVNFPRSKHLTGECKDLIY 250
Cdd:cd05574 189 SNSFVGTEEYIAPEVIKGDGHGSAV-DWWTLGILLYEMLYGTTPFKGSNRDETFSnILKK-ELTFPESPPVSSEAKDLIR 266
                       250
                ....*....|.
gi 14042947 251 HMLQPDVNRRL 261
Cdd:cd05574 267 KLLVKDPSKRL 277
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
39-269 2.03e-31

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: 121.26  E-value: 2.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  39 AIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELI-KTRGALHEDEARKKF 117
Cdd:cd05601  30 AMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSE-NLYLVMEYHPGGDLLSLLsRYDDIFEESMARFYL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 118 HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrdDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVY 197
Cdd:cd05601 109 AELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKL---SSDKTVTSKMPVGTPDYIAPEVLTSMNGGSKGT 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 198 -----DIWSLGVILYIMVCGSMPYDDSNIKKML-RIQKEHR-VNFPRSKHLTGECKDLIYHMLQpDVNRRLHIDEILSH 269
Cdd:cd05601 186 ygvecDWWSLGIVAYEMLYGKTPFTEDTVIKTYsNIMNFKKfLKFPEDPKVSESAVDLIKGLLT-DAKERLGYEGLCCH 263
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
38-273 2.73e-31

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: 120.80  E-value: 2.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIdRKkapADFLEK----FLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEA 113
Cdd:cd05599  29 YAMKKL-RK---SEMLEKeqvaHVRAERDILAEADNPWVVKLYYSFQDEE-NLYLIMEFLPGGDMMTLLMKKDTLTEEET 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 114 RKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFskrCLRDDSGRMALSKTfcGSPAYAAPEVLQGIPYQ 193
Cdd:cd05599 104 RFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL---CTGLKKSHLAYSTV--GTPDYIAPEVFLQKGYG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 194 PKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQ--KEHRVnFPRSKHLTGECKDLIYHMLQpDVNRRL---HIDEIL 267
Cdd:cd05599 179 KEC-DWWSLGVIMYEMLIGYPPfCSDDPQETCRKIMnwRETLV-FPPEVPISPEAKDLIERLLC-DAEHRLganGVEEIK 255

                ....*.
gi 14042947 268 SHCWMQ 273
Cdd:cd05599 256 SHPFFK 261
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
18-249 3.41e-31

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: 120.49  E-value: 3.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD------FLEK---FLPREIEILAMLNHCsiiktyeiFETSHgKVYI 88
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDddvectMVEKrvlALSGKPPFLTQLHSC--------FQTMD-RLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgr 168
Cdd:cd05616  79 VMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDG--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 mALSKTFCGSPAYAAPEVlqgIPYQP--KVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPR--SKHLTGE 244
Cdd:cd05616 156 -VTTKTFCGTPDYIAPEI---IAYQPygKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKsmSKEAVAI 231

                ....*
gi 14042947 245 CKDLI 249
Cdd:cd05616 232 CKGLM 236
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
11-216 3.47e-31

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 118.99  E-value: 3.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRK----KAPADFLEKFLPREIEILAML-NHCSIIKTYEIFETsHGK 85
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFET-EVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELIKTRGALHEDE--ARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF-NIKLSDFSFSKrcl 162
Cdd:cd13993  80 IYIVLEYCPNGDLFEAITENRIYVGKTelIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGLAT--- 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 rddsgRMALSKTF-CGSPAYAAPEVL-----QGIPYQPKVYDIWSLGVILYIMVCGSMPY 216
Cdd:cd13993 157 -----TEKISMDFgVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPW 211
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
14-269 4.26e-31

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: 118.37  E-value: 4.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    14 LGINLGEGSYAKVKSAYSERLKFN----VAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIV 89
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKGEGENtkikVAVKTL-KEGADEEEREDFL-EEASIMKKLDHPNIVKLLGVC-TQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    90 MELAVQGDLLELIKTRGALHEDEARKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGR 168
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMaLQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   169 MALSKTFCgsPAYAAPEVLQGipyqpKVY----DIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVnfPRSKHLT 242
Cdd:pfam07714 160 KRGGGKLP--IKWMAPESLKD-----GKFtsksDVWSFGVLLWeIFTLGEQPYPGmSNEEVLEFLEDGYRL--PQPENCP 230
                         250       260
                  ....*....|....*....|....*..
gi 14042947   243 GECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:pfam07714 231 DELYDLMKQCWAYDPEDRPTFSELVED 257
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
18-269 4.44e-31

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: 118.86  E-value: 4.44e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFnVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCS-IIK--TYEIFETSHgKVYIVMELAv 94
Cdd:cd14131   9 LGKGGSSKVYKVLNPKKKI-YALKRVDLEGADEQTLQSYK-NEIELLKKLKGSDrIIQlyDYEVTDEDD-YLYMVMECG- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDfNIKLSDFSFSKRCLRDDSGRMALS 172
Cdd:cd14131  85 EIDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG-RLKLIDFGIAKAIQNDTTSIVRDS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KtfCGSPAYAAPEVLQGIPYQP---KVY------DIWSLGVILYIMVCGSMPYDD--SNIKKMLRIQ-KEHRVNFPRskh 240
Cdd:cd14131 164 Q--VGTLNYMSPEAIKDTSASGegkPKSkigrpsDVWSLGCILYQMVYGKTPFQHitNPIAKLQAIIdPNHEIEFPD--- 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 LTGecKDLIYHM---LQPDVNRRLHIDEILSH 269
Cdd:cd14131 239 IPN--PDLIDVMkrcLQRDPKKRPSIPELLNH 268
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
18-268 4.45e-31

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: 118.54  E-value: 4.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKflPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd08219   8 VGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDS--RKEAVLLAKMKHPNIVAFKESFE-ADGHLYIVMEYCDGGD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIK-TRGALH-EDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfSKRCLrddSGRMALSKTF 175
Cdd:cd08219  85 LMQKIKlQRGKLFpEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLL---TSPGAYACTY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNfPRSKHLTGECKDLIYHMLQP 255
Cdd:cd08219 161 VGTPYYVPPEIWENMPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYK-PLPSHYSYELRSLIKQMFKR 238
                       250
                ....*....|...
gi 14042947 256 DVNRRLHIDEILS 268
Cdd:cd08219 239 NPRSRPSATTILS 251
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
11-272 5.99e-31

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: 120.13  E-value: 5.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDR-KKAPADflekflprEIEILAML-NHCSIIKTYEIFETshGK-VY 87
Cdd:cd14176  20 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKsKRDPTE--------EIEILLRYgQHPNIITLKDVYDD--GKyVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFN---IKLSDFSFSKRcLR 163
Cdd:cd14176  90 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQ-LR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGrmaLSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY----DDSNIKKMLRI-QKEHRVNFPRS 238
Cdd:cd14176 169 AENG---LLMTPCYTANFVAPEVLERQGYDAAC-DIWSLGVLLYTMLTGYTPFangpDDTPEEILARIgSGKFSLSGGYW 244
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 239 KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14176 245 NSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
18-269 6.34e-31

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 118.59  E-value: 6.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApaDFLEKFLPrEIEILAMLNHCSIIKTYEIFETSHgKVYIVMEL----A 93
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSE--EELEDYMV-EIDILASCDHPNIVKLLDAFYYEN-NLWILIEFcaggA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKtrgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsK 173
Cdd:cd06643  89 VDAVMLELER---PLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRR----D 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVL-----QGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKD 247
Cdd:cd06643 162 SFIGTPYWMAPEVVmcetsKDRPYDYKA-DVWSLGVTLIEMAQIEPPHHELNpMRVLLKIAKSEPPTLAQPSRWSPEFKD 240
                       250       260
                ....*....|....*....|..
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd06643 241 FLRKCLEKNVDARWTTSQLLQH 262
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
18-269 6.98e-31

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: 120.52  E-value: 6.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETsHGKVYIVMELAVQGD 97
Cdd:cd05594  33 LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQT-HDRLCFVMEYANGGE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCH-DLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmALSKTFC 176
Cdd:cd05594 112 LFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG----ATMKTFC 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECKDLIYHMLQPD 256
Cdd:cd05594 188 GTPEYLAPEVLEDNDYGRAV-DWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT--LSPEAKSLLSGLLKKD 264
                       250
                ....*....|....*...
gi 14042947 257 VNRRL-----HIDEILSH 269
Cdd:cd05594 265 PKQRLgggpdDAKEIMQH 282
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
9-271 7.86e-31

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: 117.84  E-value: 7.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGinlgEGSYAKVKSAYSERLKFNVAIKI--IDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIfETSHGKV 86
Cdd:cd06625   3 KQGKLLG----QGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGC-LQDEKSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR--CLRD 164
Cdd:cd06625  78 SIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRlqTICS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGrmalSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddSNIKKMLRIQK--EHRVNFPRSKHLT 242
Cdd:cd06625 158 STG----MKSVTGTPYWMSPEVINGEGYGRKA-DIWSVGCTVVEMLTTKPPW--AEFEPMAAIFKiaTQPTNPQLPPHVS 230
                       250       260
                ....*....|....*....|....*....
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd06625 231 EDARDFLSLIFVRNKKQRPSAEELLSHSF 259
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
18-279 8.31e-31

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: 117.65  E-value: 8.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     18 LGEGSYAKVKSAY----SERLKFNVAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELA 93
Cdd:smart00221   7 LGEGAFGEVYKGTlkgkGDGKEVEVAVKTL-KEDASEQQIEEFL-REARIMRKLDHPNIVKLLGVC-TEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     94 VQGDLLELIKTRGAlHEDEARKKFH---QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMA 170
Cdd:smart00221  84 PGGDLLDYLRKNRP-KELSLSDLLSfalQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    171 LSKtfcgSP-AYAAPEVLQ-GIpYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSkhltgeCK 246
Cdd:smart00221 163 GGK----LPiRWMAPESLKeGK-FTSKS-DVWSFGVLLWeIFTLGEEPYPGmSNAEVLEYLKKGYRLPKPPN------CP 230
                          250       260       270
                   ....*....|....*....|....*....|....
gi 14042947    247 DLIYhmlqpdvnrrlhidEILSHCWM-QPKARGS 279
Cdd:smart00221 231 PELY--------------KLMLQCWAeDPEDRPT 250
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
12-272 8.70e-31

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: 117.97  E-value: 8.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFL---EKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYI 88
Cdd:cd14105   7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRgvsREDIEREVSILRQVLHPNIITLHDVFE-NKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDN-LLLDKDF---NIKLSDFSFSKRClrd 164
Cdd:cd14105  86 ILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNVpipRIKLIDFGLAHKI--- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQkehRVNFPRS----K 239
Cdd:cd14105 163 EDG--NEFKNIFGTPEFVAPEIVNYEPLGLEA-DMWSIGVITYILLSGASPFlGDTKQETLANIT---AVNYDFDdeyfS 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14105 237 NTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
18-344 9.08e-31

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: 119.03  E-value: 9.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD------FLEK---FLPREIEILAMLNHCsiiktyeiFETSHgKVYI 88
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDddvectMVEKrvlALSGKPPFLTQLHSC--------FQTMD-RLYF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgr 168
Cdd:cd05587  75 VMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGG--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 mALSKTFCGSPAYAAPEVlqgIPYQP--KVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECK 246
Cdd:cd05587 152 -KTTRTFCGTPDYIAPEI---IAYQPygKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKS--LSKEAV 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 247 DLIYHMLQPDVNRRLHI-----DEILSHCWMQPkargspsvaINKEGESSRGTEPLWTPEPGSdKKSATKLEPEGEAQPQ 321
Cdd:cd05587 226 SICKGLLTKHPAKRLGCgptgeRDIKEHPFFRR---------IDWEKLERREIQPPFKPKIKS-PRDAENFDKEFTKEPP 295
                       330       340
                ....*....|....*....|...
gi 14042947 322 AQpeTKPEGTAMQMSRQSEILGF 344
Cdd:cd05587 296 VL--TPTDKLVIMNIDQSEFEGF 316
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
18-269 1.17e-30

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: 118.83  E-value: 1.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK------IIDRKKAPADFLEKflpreiEILAMLNhCSIIKTYEIFETSHGKVYIVME 91
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKtirkahIVSRSEVTHTLAER------TVLAQVD-CPFIVPLKFSFQSPEKLYLVLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGrmal 171
Cdd:cd05585  75 FINGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDK---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECKDLIYH 251
Cdd:cd05585 151 TNTFCGTPEYLAPELLLGHGYT-KAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDG--FDRDAKDLLIG 227
                       250       260
                ....*....|....*....|.
gi 14042947 252 MLQPDVNRRLHI---DEILSH 269
Cdd:cd05585 228 LLNRDPTKRLGYngaQEIKNH 248
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
12-269 1.96e-30

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: 117.42  E-value: 1.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKI-------IDRKKApaDFLEKFLpREIEILAMLNHCSIIKTYEIFETSHG 84
Cdd:cd13990   2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIhqlnkdwSEEKKQ--NYIKHAL-REYEIHKSLDHPRIVKLYDVFEIDTD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDF---NIKLSDFSFSK 159
Cdd:cd13990  79 SFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNvsgEIKITDFGLSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 160 RCLRDD--SGRMALSKTFCGSPAYAAPEVLQGIPYQPKV---YDIWSLGVILYIMVCGSMPY-DDSNIKKMLR---IQKE 230
Cdd:cd13990 159 IMDDESynSDGMELTSQGAGTYWYLPPECFVVGKTPPKIsskVDVWSVGVIFYQMLYGRKPFgHNQSQEAILEentILKA 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 14042947 231 HRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd13990 239 TEVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLAND 277
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-272 4.32e-30

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: 115.84  E-value: 4.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKApADFLE----KFLPREIEILAMLNH--CSIIKTYEIFETSHGK 85
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRV-SEWGElpngTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFSfSKRCLRD 164
Cdd:cd14100  81 VLVLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFG-SGALLKD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 dsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSniKKMLRIQKEHRvnfprsKHLTGE 244
Cdd:cd14100 160 -----TVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHD--EEIIRGQVFFR------QRVSSE 226
                       250       260
                ....*....|....*....|....*...
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14100 227 CQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
18-261 4.38e-30

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: 117.87  E-value: 4.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd05593  23 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKD-RLCFVMEYVNGGE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDdsgrMALSKTFCG 177
Cdd:cd05593 102 LFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITD----AATMKTFCG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhLTGECKDLIYHMLQPDV 257
Cdd:cd05593 178 TPEYLAPEVLEDNDYGRAV-DWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT--LSADAKSLLSGLLIKDP 254

                ....
gi 14042947 258 NRRL 261
Cdd:cd05593 255 NKRL 258
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
53-272 7.49e-30

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 115.51  E-value: 7.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  53 LEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDV 132
Cdd:cd14088  42 VRKAAKNEINILKMVKHPNILQLVDVFETRK-EYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 133 VHRDLKCDNLLLD---KDFNIKLSDFSFSKRclrddsgRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIM 209
Cdd:cd14088 121 VHRNLKLENLVYYnrlKNSKIVISDFHLAKL-------ENGLIKEPCGTPEYLAPEVVGRQRYGRPV-DCWAIGVIMYIL 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 210 VCGSMPYDD--------SNIKKMLR--IQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14088 193 LSGNPPFYDeaeeddyeNHDKNLFRkiLAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
52-272 9.02e-30

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: 114.92  E-value: 9.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  52 FLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLE--LIKTRGALHEDEARKKFHQLSLAIKYCHD 129
Cdd:cd14109  38 YGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELVRdnLLPGKDYYTERQVAVFVRQLLLALKHMHD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 130 LDVVHRDLKCDNLLLDKDfNIKLSDFSFSKRCLRDDsgrmaLSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIM 209
Cdd:cd14109 118 LGIAHLDLRPEDILLQDD-KLKLADFGQSRRLLRGK-----LTTLIYGSPEFVSPEIVNSYPVT-LATDMWSVGVLTYVL 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 210 VCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14109 191 LGGISPFLGDNDRETLTNVRSGKWSFDSSplGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
18-348 1.20e-29

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: 116.22  E-value: 1.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEIL-AMLNHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSE-KLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKTFC 176
Cdd:cd05603  82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEE----TTSTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHlTGECkDLIYHMLQPD 256
Cdd:cd05603 158 GTPEYLAPEVLRKEPYDRTV-DWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKT-VAAC-DLLQGLLHKD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 257 VNRRL----HIDEILSHCWMQPkargspsvaINKEGESSRGTEPLWTPE---PGSDKksatKLEPE--GEAQPQAQPETk 327
Cdd:cd05603 235 QRRRLgakaDFLEIKNHVFFSP---------INWDDLYHKRITPPYNPNvagPADLR----HFDPEftQEAVPHSVGRT- 300
                       330       340
                ....*....|....*....|.
gi 14042947 328 PEGTAMQMSRQSEILGFPSKP 348
Cdd:cd05603 301 PDLTASSSSSSSAFLGFSYAP 321
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
18-285 1.44e-29

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: 115.33  E-value: 1.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKK---APADFLEKfLPREIEILAMLNH---CSIIKTYeifeTSHGKVYIVME 91
Cdd:cd14094  11 IGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsSPGLSTED-LKREASICHMLKHphiVELLETY----SSDGMLYMVFE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDL-LELIKTRGA---LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRClrD 164
Cdd:cd14094  86 FMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL--G 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGRMALSKTfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQK-EHRVNFPRSKHLTG 243
Cdd:cd14094 164 ESGLVAGGRV--GTPHFMAPEVVKREPYGKPV-DVWGCGVILFILLSGCLPFYGTKERLFEGIIKgKYKMNPRQWSHISE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 14042947 244 ECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAIN 285
Cdd:cd14094 241 SAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLP 282
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-268 1.63e-29

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: 114.70  E-value: 1.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKF---NVAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYeifeTS---HGKVYIVME 91
Cdd:cd13996  14 LGSGGFGSV---YKVRNKVdgvTYAIKKI-RLTEKSSASEKVL-REVKALAKLNHPNIVRYY----TAwveEPPLYIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRG---ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN-IKLSDFSFSKRCLRDD-- 165
Cdd:cd13996  85 LCEGGTLRDWIDRRNsssKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLqVKIGDFGLATSIGNQKre 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 --------SGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSmpydDSNIKKMLRIQKEHRVNFPR 237
Cdd:cd13996 165 lnnlnnnnNGNTSNNSVGIGTPLYASPEQLDGENYNEKA-DIYSLGIILFEMLHPF----KTAMERSTILTDLRNGILPE 239
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 238 S--KHLTGEcKDLIYHMLQPDVNRRLHIDEILS 268
Cdd:cd13996 240 SfkAKHPKE-ADLIQSLLSKNPEERPSAEQLLR 271
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
18-220 2.11e-29

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: 115.67  E-value: 2.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAML-NHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAaKHPFLTALHSCFQTKD-RLFFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTrgALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmALSKT 174
Cdd:cd05591  82 DLMFQIQR--ARKFDEPRARFYaaEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG----KTTTT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN 220
Cdd:cd05591 156 FCGTPDYIAPEILQELEYGPSV-DWWALGVLMYEMMAGQPPFEADN 200
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
18-337 2.89e-29

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: 115.19  E-value: 2.89e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-----------KSAYSERLKFNVAIKIIDRKKAPAdflekflprEIEILAMLNHCSIIKTYEIFETShGKV 86
Cdd:cd05582   3 LGQGSFGKVflvrkitgpdaGTLYAMKVLKKATLKVRDRVRTKM---------ERDILADVNHPFIVKLHYAFQTE-GKL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrDDS 166
Cdd:cd05582  73 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESI-DHE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRmalSKTFCGSPAYAAPEVL--QGipyQPKVYDIWSLGVILYIMVCGSMPYDDSNIKK-MLRIQKEhRVNFPrsKHLTG 243
Cdd:cd05582 152 KK---AYSFCGTVEYMAPEVVnrRG---HTQSADWWSFGVLMFEMLTGSLPFQGKDRKEtMTMILKA-KLGMP--QFLSP 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 244 ECKDLIYHMLQPDVNRRL-----HIDEILSHCWMQpkargspsvAINKEGESSRGTEPLWTPEPGSDkKSATKLEPEGEA 318
Cdd:cd05582 223 EAQSLLRALFKRNPANRLgagpdGVEEIKRHPFFA---------TIDWNKLYRKEIKPPFKPAVSRP-DDTFYFDPEFTS 292
                       330       340
                ....*....|....*....|
gi 14042947 319 Q-PQAQPETKPEGTAMQMSR 337
Cdd:cd05582 293 RtPKDSPGVPPSANAHQLFR 312
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
41-261 2.91e-29

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: 115.36  E-value: 2.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  41 KIIDRKKAPADFLEKflpREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQL 120
Cdd:cd05586  29 KVIVAKKEVAHTIGE---RNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIAEL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 121 SLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVYDIW 200
Cdd:cd05586 106 VLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDN----KTTNTFCGTTEYLAPEVLLDEKGYTKMVDFW 181
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 201 SLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKhLTGECKDLIYHMLQPDVNRRL 261
Cdd:cd05586 182 SLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDV-LSDEGRSFVKGLLNRNPKHRL 241
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-272 3.57e-29

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: 113.13  E-value: 3.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAP--ADFLEKFLPREIEILAMLNHC--SIIKTYEIFETSHGKVY 87
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTewGTLNGVMVPLEIVLLKKVGSGfrGVIKLLDWYERPDGFLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFSfSKRCLRDds 166
Cdd:cd14102  82 VMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFG-SGALLKD-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 grmALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSniKKMLRIqkehRVNFPRskHLTGECK 246
Cdd:cd14102 159 ---TVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQD--EEILRG----RLYFRR--RVSPECQ 227
                       250       260
                ....*....|....*....|....*.
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14102 228 QLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
14-272 3.91e-29

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: 113.40  E-value: 3.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSErlkfNVAIKIIDRKKAPADFLEkflpREIEILAMLNHCSIIKtYEIFETSHGKVYIVMELA 93
Cdd:cd06628  18 LGMNASSGELMAVKQVELP----SVSAENKDRKKSMLDALQ----REIALLRELQHENIVQ-YLGSSSDANHLNIFLEYV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSGRMALSK 173
Cdd:cd06628  89 PGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKK-LEANSLSTKNNG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 ---TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHRVNFPrsKHLTGECKDLI 249
Cdd:cd06628 168 arpSLQGSVFWMAPEVVKQTSYTRKA-DIWSLGCLVVEMLTGTHPFPDcTQMQAIFKIGENASPTIP--SNISSEARDFL 244
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06628 245 EKTFEIDHNKRPTADELLKHPFL 267
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-272 4.02e-29

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: 114.36  E-value: 4.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII-DRKKAPadflekflpREIEILAMLNHCS----IIKTYEIFETSHGKVYIVMEL 92
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKMLqDCPKAR---------REVELHWRASQCPhivrIVDVYENLYAGRKCLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL-DKDFN--IKLSDFSFSKRCLRDDSg 167
Cdd:cd14170  81 LDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYtSKRPNaiLKLTDFGFAKETTSHNS- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmalSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSN-------IKKMLRIQKEHRVNfPRSKH 240
Cdd:cd14170 160 ----LTTPCYTPYYVAPEVLGPEKYD-KSCDMWSLGVIMYILLCGYPPFYSNHglaispgMKTRIRMGQYEFPN-PEWSE 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14170 234 VSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 265
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
87-271 4.84e-29

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: 114.75  E-value: 4.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskRCLRDD 165
Cdd:cd05597  77 YLVMDYYCGGDLLTLLsKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG---SCLKLR 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRMALSKTFCGSPAYAAPEVLQGIP-----YQPKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLRI-QKEHRVNFPRS 238
Cdd:cd05597 154 EDGTVQSSVAVGTPDYISPEILQAMEdgkgrYGPEC-DWWSLGVCMYEMLYGETPfYAESLVETYGKImNHKEHFSFPDD 232
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14042947 239 K-HLTGECKDLIYHMLQpDVNRRL---HIDEILSHCW 271
Cdd:cd05597 233 EdDVSEEAKDLIRRLIC-SRERRLgqnGIDDFKKHPF 268
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
16-269 8.19e-29

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 113.54  E-value: 8.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaVQ 95
Cdd:cd06659  27 VKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQR---RELLFNEVVIMRDYQHPNVVEMYKSYLVGE-ELWVLMEY-LQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTF 175
Cdd:cd06659 102 GGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKR----KSL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQ 254
Cdd:cd06659 178 VGTPYWMAPEVISRCPYGTEV-DIWSLGIMVIEMVDGEPPYfSDSPVQAMKRLRDSPPPKLKNSHKASPVLRDFLERMLV 256
                       250
                ....*....|....*
gi 14042947 255 PDVNRRLHIDEILSH 269
Cdd:cd06659 257 RDPQERATAQELLDH 271
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
18-263 1.19e-28

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: 113.50  E-value: 1.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAM------LNHcsiikTYEIFETSHgKVYIVME 91
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALawenpfLTH-----LYCTFQTKE-HLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALheDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGrm 169
Cdd:cd05620  77 FLNGGDLMFHIQDKGRF--DLYRATFYaaEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNR-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 alSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY---DDSNIKKMLRIQKEHrvnFPRskHLTGECK 246
Cdd:cd05620 153 --ASTFCGTPDYIAPEILQGLKYTFSV-DWWSFGVLLYEMLIGQSPFhgdDEDELFESIRVDTPH---YPR--WITKESK 224
                       250
                ....*....|....*..
gi 14042947 247 DLIYHMLQPDVNRRLHI 263
Cdd:cd05620 225 DILEKLFERDPTRRLGV 241
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
12-260 1.24e-28

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 116.12  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDrkkapadfLEKFLPREI-----EILAMLNhC---SIIKTYEIF---- 79
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVD--------MEGMSEADKnraqaEVCCLLN-CdffSIVKCHEDFakkd 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   80 ---ETSHGKVYIVMELAVQGDLLELIKTRG----ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKL 152
Cdd:PTZ00283 105 prnPENVLMIALVLDYANAGDLRQEIKSRAktnrTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  153 SDFSFSK---RCLRDDSGRmalskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQK 229
Cdd:PTZ00283 185 GDFGFSKmyaATVSDDVGR-----TFCGTPYYVAPEIWRRKPYSKKA-DMFSLGVLLYELLTLKRPFDGENMEEVMHKTL 258
                        250       260       270
                 ....*....|....*....|....*....|.
gi 14042947  230 EHRVNfPRSKHLTGECKDLIYHMLQPDVNRR 260
Cdd:PTZ00283 259 AGRYD-PLPPSISPEMQEIVTALLSSDPKRR 288
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
18-269 1.48e-28

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: 112.43  E-value: 1.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApaDFLEKFLPrEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMEL----A 93
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIETKSE--EELEDYMV-EIEILATCNHPYIVKLLGAF-YWDGKLWIMIEFcpggA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELikTRGaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsK 173
Cdd:cd06644  96 VDAIMLEL--DRG-LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRR----D 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEV-----LQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKD 247
Cdd:cd06644 169 SFIGTPYWMAPEVvmcetMKDTPYDYKA-DIWSLGITLIEMAQIEPPHHELNpMRVLLKIAKSEPPTLSQPSKWSMEFRD 247
                       250       260
                ....*....|....*....|..
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd06644 248 FLKTALDKHPETRPSAAQLLEH 269
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
18-249 2.18e-28

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: 113.17  E-value: 2.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSII-KTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLtQLHSCFQTVD-RLYFVMEYVNGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmALSKTFC 176
Cdd:cd05615  97 DLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEG----VTTRTFC 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 177 GSPAYAAPEVlqgIPYQP--KVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPR--SKHLTGECKDLI 249
Cdd:cd05615 173 GTPDYIAPEI---IAYQPygRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKslSKEAVSICKGLM 246
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
18-274 2.60e-28

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: 112.62  E-value: 2.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK--------IIDRKKApadflekfLpREIEILAMLNHCSIIKTYEIFE----TSHGK 85
Cdd:cd07834   8 IGSGAYGVVCSAYDKRTGRKVAIKkisnvfddLIDAKRI--------L-REIKILRHLKHENIIGLLDILRppspEEFND 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAvQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrdd 165
Cdd:cd07834  79 VYIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDF---------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 sgrmALSKTFCGSPA------------YAAPEVLQGIPYQPKVYDIWSLGVIL--------------YI-------MVCG 212
Cdd:cd07834 148 ----GLARGVDPDEDkgflteyvvtrwYRAPELLLSSKKYTKAIDIWSVGCIFaelltrkplfpgrdYIdqlnlivEVLG 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 213 SMPYDD------SNIKKMLRIQKEHRVNfPRSKHLTG---ECKDLIYHMLQPDVNRRLHIDEILSHCWMQP 274
Cdd:cd07834 224 TPSEEDlkfissEKARNYLKSLPKKPKK-PLSEVFPGaspEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
18-272 3.46e-28

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: 110.83  E-value: 3.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEkflpREIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAVQGD 97
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVT----HELGVLQSLQHPQLVGLLDTFETPTSYI-LVLEMADQGR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN---IKLSDFSfskrclrdDSgrMALSKT 174
Cdd:cd14113  90 LLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFG--------DA--VQLNTT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 F-----CGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHrVNFPRS--KHLTGECK 246
Cdd:cd14113 160 YyihqlLGSPEFAAPEIILGNPVS-LTSDLWSIGVLTYVLLSGVSPFlDESVEETCLNICRLD-FSFPDDyfKGVSQKAK 237
                       250       260
                ....*....|....*....|....*.
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14113 238 DFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
21-273 3.52e-28

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: 113.95  E-value: 3.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  21 GSYAKVKSAYSERLkfnVAIKIIDR----KKApadflEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQG 96
Cdd:cd05624  86 GEVAVVKMKNTERI---YAMKILNKwemlKRA-----ETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGG 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskRCLRDDSGRMALSKTF 175
Cdd:cd05624 158 DLLTLLsKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG---SCLKMNDDGTVQSSVA 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGI-----PYQPKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQK-EHRVNFPrsKHLTG---EC 245
Cdd:cd05624 235 VGTPDYISPEILQAMedgmgKYGPEC-DWWSLGVCMYEMLYGETPfYAESLVETYGKIMNhEERFQFP--SHVTDvseEA 311
                       250       260       270
                ....*....|....*....|....*....|.
gi 14042947 246 KDLIYHMLQPDvNRRL---HIDEILSHCWMQ 273
Cdd:cd05624 312 KDLIQRLICSR-ERRLgqnGIEDFKKHAFFE 341
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
18-285 5.05e-28

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: 110.64  E-value: 5.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkAPADFLEKfLPREIEILAMLNHC---SIIKTYEIFeTSHGKVYIVMELAV 94
Cdd:cd06917   9 VGRGSYGAVYRGYHVKTGRVVALKVLNLD-TDDDDVSD-IQKEVALLSQLKLGqpkNIIKYYGSY-LKGPSLWIIMDYCE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTrGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKT 174
Cdd:cd06917  86 GGSIRTLMRA-GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKR----ST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEV-LQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKK--MLRIQKEHrvnfPR--SKHLTGECKDLI 249
Cdd:cd06917 161 FVGTPYWMAPEViTEGKYYDTKA-DIWSLGITTYEMATGNPPYSDVDALRavMLIPKSKP----PRleGNGYSPLLKEFV 235
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWMQPKARgSPSVAIN 285
Cdd:cd06917 236 AACLDEEPKDRLSADELLKSKWIKQHSK-TPTSVLK 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
40-271 5.16e-28

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: 110.36  E-value: 5.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  40 IKIIDRKKAPADFLEKFLP----------REIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAVQGDLLELIKTRGALH 109
Cdd:cd14107  18 VKRVTHKGNGECCAAKFIPlrsstrarafQERDILARLSHRRLTCLLDQFETRKTLI-LILELCSSEELLDRLFLKGVVT 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 110 EDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFskrCLRDDSGRMALSKTfcGSPAYAAPEVL 187
Cdd:cd14107  97 EAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGF---AQEITPSEHQFSKY--GSPEFVAPEIV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 188 QGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNF--PRSKHLTGECKDLIYHMLQPDVNRRLHIDE 265
Cdd:cd14107 172 HQEPVS-AATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWdtPEITHLSEDAKDFIKRVLQPDPEKRPSASE 250

                ....*.
gi 14042947 266 ILSHCW 271
Cdd:cd14107 251 CLSHEW 256
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
18-302 7.97e-28

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: 111.65  E-value: 7.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAM-LNHCSIIKTYEIFETShGKVYIVMELAVQG 96
Cdd:cd05602  15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKnVKHPFLVGLHFSFQTT-DKLYFVLDYINGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKTFC 176
Cdd:cd05602  94 ELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNG----TTSTFC 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLriqkEHRVNFPRS--KHLTGECKDLIYHMLQ 254
Cdd:cd05602 170 GTPEYLAPEVLHKQPYDRTV-DWWCLGAVLYEMLYGLPPFYSRNTAEMY----DNILNKPLQlkPNITNSARHLLEGLLQ 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 255 PDVNRRL----HIDEILSHCWMQP-------KARGSPSVAINKEGESS-RGTEPLWTPEP 302
Cdd:cd05602 245 KDRTKRLgakdDFTEIKNHIFFSPinwddliNKKITPPFNPNVSGPNDlRHFDPEFTDEP 304
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
18-261 8.14e-28

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: 111.24  E-value: 8.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK------IIDRKKAPADFLEKflpREIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKalkkgdIIARDEVESLMCEK---RIFETVNSARHPFLVNLFACFQTPE-HVCFVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIktrgalHED---EARKKFHQ--LSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrDDS 166
Cdd:cd05589  83 YAAGGDLMMHI------HEDvfsEPRAVFYAacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK----EGM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY--DDS-----NIkkmlrIQKEhrVNFPRsk 239
Cdd:cd05589 153 GFGDRTSTFCGTPEFLAPEVLTDTSYTRAV-DWWGLGVLIYEMLVGESPFpgDDEeevfdSI-----VNDE--VRYPR-- 222
                       250       260
                ....*....|....*....|..
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRL 261
Cdd:cd05589 223 FLSTEAISIMRRLLRKNPERRL 244
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
18-273 8.18e-28

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: 109.63  E-value: 8.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd06647  15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIkTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06647  91 LTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR----STMVG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPD 256
Cdd:cd06647 166 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMD 244
                       250
                ....*....|....*..
gi 14042947 257 VNRRLHIDEILSHCWMQ 273
Cdd:cd06647 245 VEKRGSAKELLQHPFLK 261
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
56-269 8.28e-28

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: 111.70  E-value: 8.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  56 FLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIkTRGALHEDEARKKFHQLSLAIKYCHDLDVVHR 135
Cdd:cd05596  72 FFWEERDIMAHANSEWIVQLHYAFQDDK-YLYMVMDYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFVHR 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 136 DLKCDNLLLDKDFNIKLSDFSfskRCLRDDSGRMALSKTFCGSPAYAAPEVL--QGipyQPKVY----DIWSLGVILYIM 209
Cdd:cd05596 150 DVKPDNMLLDASGHLKLADFG---TCMKMDKDGLVRSDTAVGTPDYISPEVLksQG---GDGVYgrecDWWSVGVFLYEM 223
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 210 VCGSMP-YDDSNIKKMLRIQkEHR--VNFPRSKHLTGECKDLIYHMLQpDVNRRL---HIDEILSH 269
Cdd:cd05596 224 LVGDTPfYADSLVGTYGKIM-NHKnsLQFPDDVEISKDAKSLICAFLT-DREVRLgrnGIEEIKAH 287
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
18-238 8.58e-28

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: 111.36  E-value: 8.58e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEIL-AMLNHCSIIKTYEIFETShGKVYIVMELAVQG 96
Cdd:cd05588   3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFeTASNHPFLVGLHSCFQTE-SRLFFVIEFVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKTFC 176
Cdd:cd05588  82 DLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGD----TTSTFC 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD--------DSNIKKML-RIQKEHRVNFPRS 238
Cdd:cd05588 158 GTPNYIAPEILRGEDYGFSV-DWWALGVLMFEMLAGRSPFDivgssdnpDQNTEDYLfQVILEKPIRIPRS 227
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
18-277 1.40e-27

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: 109.08  E-value: 1.40e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIF--ETSHGkvyIVMELAVQ 95
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCL-HSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCveRRSLG---LVMEYMEN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKtrgALHEDEA---RKKF-HQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDFNIKLSDFSFSK-RCLRDDSGR 168
Cdd:cd13978  77 GSLKSLLE---REIQDVPwslRFRIiHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKlGMKSISANR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVLQGIPYQPKV-YDIWSLGVILYIMVCGSMPYDD--SNIKKMLRIQKEHRvnfprsKHLTGEC 245
Cdd:cd13978 154 RRGTENLGGTPIYMAPEAFDDFNKKPTSkSDVYSFAIVIWAVLTRKEPFENaiNPLLIMQIVSKGDR------PSLDDIG 227
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 246 KDLIYHMLQpdvnrrlHIDEILSHCWMQ-PKAR 277
Cdd:cd13978 228 RLKQIENVQ-------ELISLMIRCWDGnPDAR 253
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
12-304 1.68e-27

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: 110.40  E-value: 1.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAML-NHCSIIKTYEIFETSHgKVYIVM 90
Cdd:cd05619   7 FVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKE-NLFFVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTrgaLHE-DEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsg 167
Cdd:cd05619  86 EYLNGGDLMFHIQS---CHKfDLPRATFYaaEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGD-- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRskHLTGECKD 247
Cdd:cd05619 161 --AKTSTFCGTPDYIAPEILLGQKYNTSV-DWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPR--WLEKEAKD 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 248 LIYHMLQPDVNRRLHID-EILSHCWMQpkargspsvAINKEGESSRGTEPLWTPEPGS 304
Cdd:cd05619 236 ILVKLFVREPERRLGVRgDIRQHPFFR---------EINWEALEEREIEPPFKPKVKS 284
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
79-269 3.62e-27

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: 109.33  E-value: 3.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FETSHgKVYIVMELAVQGDLL-ELIKTRgalHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF 155
Cdd:cd05575  65 FQTKD-KLYFVLDYVNGGELFfHLQRER---HFPEPRARFYaaEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDF 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 156 SFSKrclrDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRV 233
Cdd:cd05575 141 GLCK----EGIEPSDTTSTFCGTPEYLAPEVLRKQPYDRTV-DWWCLGAVLYEMLYGLPPFYSRDTAEMYDniLHKPLRL 215
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14042947 234 nfprSKHLTGECKDLIYHMLQPDVNRRL----HIDEILSH 269
Cdd:cd05575 216 ----RTNVSPSARDLLEGLLQKDRTKRLgsgnDFLEIKNH 251
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
60-273 3.96e-27

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: 109.33  E-value: 3.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKC 139
Cdd:cd05598  51 ERDILAEADNEWVVKLYYSFQDKE-NLYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKP 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 140 DNLLLDKDFNIKLSDFSFSK--RCLRDDSGRMALSktFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMP-Y 216
Cdd:cd05598 130 DNILIDRDGHIKLTDFGLCTgfRWTHDSKYYLAHS--LVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILYEMLVGQPPfL 206
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 217 DDSNIKKMLR-IQKEHRVNFPRSKHLTGECKDLIYHMLQpDVNRRL---HIDEILSHCWMQ 273
Cdd:cd05598 207 AQTPAETQLKvINWRTTLKIPHEANLSPEAKDLILRLCC-DAEDRLgrnGADEIKAHPFFA 266
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-269 4.04e-27

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: 107.89  E-value: 4.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKV------KSAYSERLKFNVAIKIIDRKkaPADFLEKFlpREIEILAMLNHCSIIKTYEIFeTSHGK 85
Cdd:cd08222   2 YRVVRKLGSGNFGTVylvsdlKATADEELKVLKEISVGELQ--PDETVDAN--REAKLLSKLDHPAIVKFHDSF-VEKES 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELI----KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLdKDFNIKLSDFSFSkRC 161
Cdd:cd08222  77 FCIVTEYCEGGDLDDKIseykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGIS-RI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 162 LrddSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPrsKH 240
Cdd:cd08222 155 L---MGTSDLATTFTGTPYYMSPEVLKHEGYNSKS-DIWSLGCILYEMCCLKHAFDGQNlLSVMYKIVEGETPSLP--DK 228
                       250       260
                ....*....|....*....|....*....
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd08222 229 YSKELNAIYSRMLNKDPALRPSAAEILKI 257
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
12-273 5.27e-27

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: 107.78  E-value: 5.27e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD---FLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYI 88
Cdd:cd14195   7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgVSREEIEREVNILREIQHPNIITLHDIFE-NKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDN-LLLDKDF---NIKLSDFSFSKRCLRD 164
Cdd:cd14195  86 ILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIEAG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSgrmalSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKehrVNFPRSKHL-- 241
Cdd:cd14195 166 NE-----FKNIFGTPEFVAPEIVNYEPLGLEA-DMWSIGVITYILLSGASPFlGETKQETLTNISA---VNYDFDEEYfs 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 242 -TGE-CKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14195 237 nTSElAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
18-261 5.80e-27

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: 109.74  E-value: 5.80e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAML-NHCSIIKTYEIFETsHGKVYIVMELAVQG 96
Cdd:cd05618  28 IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQAsNHPFLVGLHSCFQT-ESRLFFVIEYVNGG 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKTFC 176
Cdd:cd05618 107 DLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGD----TTSTFC 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD--------DSNIKKML-RIQKEHRVNFPRSkhLTGECKD 247
Cdd:cd05618 183 GTPNYIAPEILRGEDYGFSV-DWWALGVLMFEMMAGRSPFDivgssdnpDQNTEDYLfQVILEKQIRIPRS--LSVKAAS 259
                       250
                ....*....|....
gi 14042947 248 LIYHMLQPDVNRRL 261
Cdd:cd05618 260 VLKSFLNKDPKERL 273
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
60-261 1.81e-26

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: 106.72  E-value: 1.81e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKC 139
Cdd:cd05609  50 ERDILTFAENPFVVSMYCSFETKR-HLCMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 140 DNLLLDKDFNIKLSDFSFSKRCLR-----------DDSGRMALSKTFCGSPAYAAPEVL--QGipYQPKVyDIWSLGVIL 206
Cdd:cd05609 129 DNLLITSMGHIKLTDFGLSKIGLMslttnlyeghiEKDTREFLDKQVCGTPEYIAPEVIlrQG--YGKPV-DWWAMGIIL 205
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 207 YIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKH-LTGECKDLIYHMLQPDVNRRL 261
Cdd:cd05609 206 YEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDDaLPDDAQDLITRLLQQNPLERL 261
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
16-269 1.85e-26

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: 106.34  E-value: 1.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIdrkkaPADFLEKFLP--REIEILAMLNHCSIIKtYEIFETSHGKVYIVMELA 93
Cdd:cd06624  14 VVLGKGTFGVVYAARDLSTQVRIAIKEI-----PERDSREVQPlhEEIALHSRLSHKNIVQ-YLGSVSEDGFFKIFMEQV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTR-GALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKdFN--IKLSDFSFSKRClrddSGR 168
Cdd:cd06624  88 PGGSLSALLRSKwGPLKDNENTIGYYtkQILEGLKYLHDNKIVHRDIKGDNVLVNT-YSgvVKISDFGTSKRL----AGI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVL-QGIP-YQPKVyDIWSLGVILYIMVCGSMPYDD--SNIKKMLRIQ--KEHRvNFPRSkhLT 242
Cdd:cd06624 163 NPCTETFTGTLQYMAPEVIdKGQRgYGPPA-DIWSLGCTIIEMATGKPPFIElgEPQAAMFKVGmfKIHP-EIPES--LS 238
                       250       260
                ....*....|....*....|....*..
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd06624 239 EEAKSFILRCFEPDPDKRATASDLLQD 265
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
60-267 8.12e-26

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: 104.05  E-value: 8.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLDVVHRDL 137
Cdd:cd08221  49 EIDILSLLNHDNIITYYNHF-LDGESLFIEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDI 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 138 KCDNLLLDKDFNIKLSDFSFSKRClrDDSGRMAlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD 217
Cdd:cd08221 128 KTLNIFLTKADLVKLGDFGISKVL--DSESSMA--ESIVGTPYYMSPELVQGVKYNFKS-DIWAVGCVLYELLTLKRTFD 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 218 DSN-IKKMLRIQKEHRVNFprSKHLTGECKDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd08221 203 ATNpLRLAVKIVQGEYEDI--DEQYSEEIIQLVHDCLHQDPEDRPTAEELL 251
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
60-226 1.67e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 107.02  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   60 EIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGDLLELIKTRGALH----EDEARKKFHQLSLAIKYCHDLDVVHR 135
Cdd:PTZ00267 115 ELHCLAACDHFGIVKHFDDFK-SDDKLLLIMEYGSGGDLNKQIKQRLKEHlpfqEYEVGLLFYQIVLALDEVHSRKMMHR 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  136 DLKCDNLLLDKDFNIKLSDFSFSKRclRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP 215
Cdd:PTZ00267 194 DLKSANIFLMPTGIIKLGDFGFSKQ--YSDSVSLDVASSFCGTPYYLAPELWERKRYSKKA-DMWSLGVILYELLTLHRP 270
                        170
                 ....*....|.
gi 14042947  216 YDDSNIKKMLR 226
Cdd:PTZ00267 271 FKGPSQREIMQ 281
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
18-272 2.57e-25

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: 102.69  E-value: 2.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAVQGD 97
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFI-KCRKAKDRED--VRNEIEIMNQLRHPRLLQLYDAFETPREMV-LVMEYVAGGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFN-IKLSDFSFSKRCLRDDSGRMAlskt 174
Cdd:cd14103  77 LFErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLKVL---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 fCGSPAYAAPEVlqgIPYQPKVY--DIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQK-EHRVNFPRSKHLTGECKDLIY 250
Cdd:cd14103 153 -FGTPEFVAPEV---VNYEPISYatDMWSVGVICYVLLSGLSPFmGDNDAETLANVTRaKWDFDDEAFDDISDEAKDFIS 228
                       250       260
                ....*....|....*....|..
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14103 229 KLLVKDPRKRMSAAQCLQHPWL 250
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
18-291 2.59e-25

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: 103.65  E-value: 2.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd06655  27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPK---KELIINEILVMKELKNPNIVNFLDSFLVGD-ELFVVMEYLAGGS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIkTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06655 103 LTDVV-TETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKR----STMVG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPD 256
Cdd:cd06655 178 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMD 256
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 14042947 257 VNRRLHIDEILSHCWM---QPKARGSPSVAINKEGESS 291
Cdd:cd06655 257 VEKRGSAKELLQHPFLklaKPLSSLTPLILAAKEAMKS 294
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
18-269 2.74e-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. 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: 103.55  E-value: 2.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiiDRKKAPAD-FLEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELaVQG 96
Cdd:cd07833   9 VGEGAYGVVLKCRNKATGEIVAIK--KFKESEDDeDVKKTALREVKVLRQLRHENIVNLKEAFRRK-GRLYLVFEY-VER 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRdDSGRMALSkTF 175
Cdd:cd07833  85 TLLELLeASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFA-RALT-ARPASPLT-DY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQG-IPYQPKVyDIWSLGVILYIMVCGS--MPyDDSNIKKMLRIQK-------EHRVNFPRSKHLTG-- 243
Cdd:cd07833 162 VATRWYRAPELLVGdTNYGKPV-DVWAIGCIMAELLDGEplFP-GDSDIDQLYLIQKclgplppSHQELFSSNPRFAGva 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 244 --------------ECK------DLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07833 240 fpepsqpeslerryPGKvsspalDFLKACLRMDPKERLTCDELLQH 285
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
18-269 3.17e-25

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: 103.14  E-value: 3.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYA---KVKSAYSERLkfnVAIKII------DRKKAPadflekflpREIEILAMLNHCSIIK--TYEIFETSHGK- 85
Cdd:cd13986   8 LGEGGFSfvyLVEDLSTGRL---YALKKIlchskeDVKEAM---------REIENYRLFNHPNILRllDSQIVKEAGGKk 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 -VYIVMELAVQGDLLELIKTRGA----LHEDEARKKFHQLSLAIKYCHDLDVV---HRDLKCDNLLLDKDFNIKLSDF-S 156
Cdd:cd13986  76 eVYLLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLgS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 157 FSKRCLRDDSGRMALS----KTFCGSPAYAAPEVLQGIPYQ---PKVyDIWSLGVILYIMVCGSMPYDDSNIKK---MLR 226
Cdd:cd13986 156 MNPARIEIEGRREALAlqdwAAEHCTMPYRAPELFDVKSHCtidEKT-DIWSLGCTLYALMYGESPFERIFQKGdslALA 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 14042947 227 IQKEhRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd13986 235 VLSG-NYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
108-269 3.55e-25

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: 103.25  E-value: 3.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 108 LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN-IKLSDFSFSKRCLRDDSgrmaLSKTFCGSPAYAAPEV 186
Cdd:cd13974 129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDD----LLKDQRGSPAYISPDV 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 187 LQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEI 266
Cdd:cd13974 205 LSGKPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDGRVSENTVCLIRKLLVLNPQKRLTASEV 284

                ...
gi 14042947 267 LSH 269
Cdd:cd13974 285 LDS 287
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
18-271 5.48e-25

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: 102.75  E-value: 5.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII----DRKKAPADFLekflpREIEILAMLNHCSIIKTYEIfETSHGKVYIVMELa 93
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALKKIrletEDEGVPSTAI-----REISLLKELNHPNIVRLLDV-VHSENKLYLVFEF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEAR-KKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsgrmAL 171
Cdd:cd07835  80 LDLDLKKYMDSSPLTGLDPPLiKSYlYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADF--------------GL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFcGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMV------CGsmpydDSNIKKMLRIQK----- 229
Cdd:cd07835 146 ARAF-GVPVrtythevvtlwYRAPEILLGSKHYSTPVDIWSVGCIFAEMVtrrplfPG-----DSEIDQLFRIFRtlgtp 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 230 ------------EHRVNFPR------SKHLTG---ECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07835 220 dedvwpgvtslpDYKPTFPKwarqdlSKVVPSldeDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
18-272 5.59e-25

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: 102.07  E-value: 5.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYserLKFNV------AIK-------IIDRKKAPADFLEKFLPREIEILAMLNHCSIIkTYEIFETSHG 84
Cdd:cd06629   9 IGKGTYGRV---Y---LAMNAttgemlAVKqvelpktSSDRADSRQKTVVDALKSEIDTLKDLDHPNIV-QYLGFEETED 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRC--L 162
Cdd:cd06629  82 YFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSddI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 RDDSGRMALSktfcGSPAYAAPEVL--QGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRI-QKEHRVNFPRS 238
Cdd:cd06629 162 YGNNGATSMQ----GSVFWMAPEVIhsQGQGYSAKV-DIWSLGCVVLEMLAGRRPWsDDEAIAAMFKLgNKRSAPPVPED 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 239 KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06629 237 VNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
40-271 5.98e-25

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: 101.90  E-value: 5.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  40 IKIIDRKKAPADFLEKFLP----------REIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQgDLLELIKTRGALH 109
Cdd:cd14108  18 LRRVKEKSSDLSFAAKFIPvrakkktsarRELALLAELDHKSIVRFHDAFEKRRV-VIIVTELCHE-ELLERITKRPTVC 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 110 EDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRCLRDDsgrmalsKTFC--GSPAYAAPE 185
Cdd:cd14108  96 ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNE-------PQYCkyGTPEFVAPE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 186 VLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKDLIYHMLqpdVNRRLHI 263
Cdd:cd14108 169 IVNQSPVS-KVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESmfKDLCREAKGFIIKVL---VSDRLRP 244
                       250
                ....*....|
gi 14042947 264 D--EILSHCW 271
Cdd:cd14108 245 DaeETLEHPW 254
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
32-272 5.99e-25

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: 102.00  E-value: 5.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  32 ERL---KFNVAIKIIDRK----------KAPADFLEKFLPREIEILAMLNHCSIIKTYEIFEtshGKVYIVM--ELAVQG 96
Cdd:cd14191   8 ERLgsgKFGQVFRLVEKKtkkvwagkffKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFE---EKANIVMvlEMVSGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRClrDDSGRMalsK 173
Cdd:cd14191  85 ELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRL--ENAGSL---K 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVlqgIPYQPKVY--DIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKDLI 249
Cdd:cd14191 160 VLFGTPEFVAPEV---INYEPIGYatDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEafDEISDDAKDFI 236
                       250       260
                ....*....|....*....|...
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14191 237 SNLLKKDMKARLTCTQCLQHPWL 259
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
18-292 6.59e-25

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: 102.88  E-value: 6.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd06656  27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIkTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06656 103 LTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR----STMVG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPD 256
Cdd:cd06656 178 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMD 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 14042947 257 VNRRLHIDEILSHCWM---QPKARGSPSVAINKEG--ESSR 292
Cdd:cd06656 257 VDRRGSAKELLQHPFLklaKPLSSLTPLIIAAKEAikNSSR 297
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
18-261 6.73e-25

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: 103.95  E-value: 6.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLN-HCSIIKTYEIFETShGKVYIVMELAVQG 96
Cdd:cd05617  23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTT-SRLFLVIEYVNGG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKTFC 176
Cdd:cd05617 102 DLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGD----TTSTFC 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD------DSNIKKML-RIQKEHRVNFPRSkhLTGECKDLI 249
Cdd:cd05617 178 GTPNYIAPEILRGEEYGFSV-DWWALGVLMFEMMAGRSPFDiitdnpDMNTEDYLfQVILEKPIRIPRF--LSVKASHVL 254
                       250
                ....*....|..
gi 14042947 250 YHMLQPDVNRRL 261
Cdd:cd05617 255 KGFLNKDPKERL 266
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
19-270 6.92e-25

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: 102.58  E-value: 6.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVKSAYSERLKFNVAIKiidrkKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETSHGK---VY--IVMELa 93
Cdd:cd14137  13 GSGSFGVVYQAKLLETGEVVAIK-----KVLQD--KRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKkdeVYlnLVMEY- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKtrgalHEDEARKKF---------HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNI-KLSDFSFSKRCLR 163
Cdd:cd14137  85 MPETLYRVIR-----HYSKNKQTIpiiyvklysYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKLCDFGSAKRLVP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSgrmalSKTFCGSPAYAAPEVLQGIP-YQPKVyDIWSLGVILYIMVCGS--MPYDDSN-----------------IKK 223
Cdd:cd14137 160 GEP-----NVSYICSRYYRAPELIFGATdYTTAI-DIWSAGCVLAELLLGQplFPGESSVdqlveiikvlgtptreqIKA 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 224 MLRIQKEHRvnFPRSK----------HLTGECKDLIYHMLQPDVNRRLHIDEILSHC 270
Cdd:cd14137 234 MNPNYTEFK--FPQIKphpwekvfpkRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
18-269 1.05e-24

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: 100.92  E-value: 1.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYA---KVKSAYSERLkfnVAIKIIDRKKAPADFLEKFLpREIEILAML-NHCSIIKTYEIFETShGKVYIVMELA 93
Cdd:cd13997   8 IGSGSFSevfKVRSKVDGCL---YAVKKSKKPFRGPKERARAL-REVEAHAALgQHPNIVRYYSSWEEG-GHLYIQMELC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGA---LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFskrCLRDDSGRMA 170
Cdd:cd13997  83 ENGSLQDALEELSPiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGL---ATRLETSGDV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSktfcGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRiqkEHRVNFPRSKHLTGECKDLIY 250
Cdd:cd13997 160 EE----GDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLR---QGKLPLPPGLVLSQELTRLLK 232
                       250
                ....*....|....*....
gi 14042947 251 HMLQPDVNRRLHIDEILSH 269
Cdd:cd13997 233 VMLDPDPTRRPTADQLLAH 251
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
18-271 1.08e-24

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: 101.79  E-value: 1.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIID---RKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaV 94
Cdd:cd07836   8 LGEGTYATVYKGRNRTTGEIVALKEIHldaEEGTPSTAI-----REISLMKELKHENIVRLHDVIHTEN-KLMLVFEY-M 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKT---RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsgrmAL 171
Cdd:cd07836  81 DKDLKKYMDThgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADF--------------GL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFcGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSN----IKKMLRIQ-------- 228
Cdd:cd07836 147 ARAF-GIPVntfsnevvtlwYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNnedqLLKIFRIMgtptestw 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 229 ------KEHRVNFPRSK---------HLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07836 226 pgisqlPEYKPTFPRYPpqdlqqlfpHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
12-206 1.59e-24

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: 101.49  E-value: 1.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKII--DRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIV 89
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklGERKEAKDGINFTALREIKLLQELKHPNIIGLLDVF-GHKSNINLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAvQGDLLELIKTRgALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsg 167
Cdd:cd07841  81 FEFM-ETDLEKVIKDK-SIVLTPADIKSYmlMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADF------------ 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 168 rmALSKTFcGSPA-----------YAAPEVLQGIP-YQPKVyDIWSLGVIL 206
Cdd:cd07841 147 --GLARSF-GSPNrkmthqvvtrwYRAPELLFGARhYGVGV-DMWSVGCIF 193
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
18-269 1.65e-24

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 101.49  E-value: 1.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII--DRKKapadflEKFlP----REIEILAMLNHCSIIKTYEI-----FETSHGKV 86
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKKIrmENEK------EGF-PitaiREIKLLQKLDHPNVVRLKEIvtskgSAKYKGSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAvQGDLLELIKTRGaLHEDEARKK--FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF----SFSKR 160
Cdd:cd07840  80 YMVFEYM-DHDLTGLLDNPE-VKFTESQIKcyMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFglarPYTKE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 CLRDDSGRMAlskTFCgspaYAAPEVLQG-IPYQPKVyDIWSLGVILYIM---------------------VCGSmPYDD 218
Cdd:cd07840 158 NNADYTNRVI---TLW----YRPPELLLGaTRYGPEV-DMWSVGCILAELftgkpifqgkteleqlekifeLCGS-PTEE 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 219 S--NIKKM-----LRIQKEHRVNFPR--SKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07840 229 NwpGVSDLpwfenLKPKKPYKRRLREvfKNVIDPSALDLLDKLLTLDPKKRISADQALQH 288
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-269 1.74e-24

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: 103.16  E-value: 1.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd05621  60 IGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDK-YLYMVMEYMPGGD 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGAlheDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskRCLRDDSGRMALSKTF 175
Cdd:cd05621 139 LVNLMSNYDV---PEKWAKFYtaEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFG---TCMKMDETGMVHCDTA 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQ---GIPYQPKVYDIWSLGVILYIMVCGSMP-YDDSNIKKMLRI-QKEHRVNFPRSKHLTGECKDLIY 250
Cdd:cd05621 213 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPfYADSLVGTYSKImDHKNSLNFPDDVEISKHAKNLIC 292
                       250       260
                ....*....|....*....|.
gi 14042947 251 HMLQPDVNR--RLHIDEILSH 269
Cdd:cd05621 293 AFLTDREVRlgRNGVEEIKQH 313
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
18-288 2.91e-24

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: 100.95  E-value: 2.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd06654  28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIkTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06654 104 LTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR----STMVG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPD 256
Cdd:cd06654 179 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMD 257
                       250       260       270
                ....*....|....*....|....*....|....*
gi 14042947 257 VNRRLHIDEILSHCWM---QPKARGSPSVAINKEG 288
Cdd:cd06654 258 VEKRGSAKELLQHQFLkiaKPLSSLTPLIAAAKEA 292
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-269 3.33e-24

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: 102.39  E-value: 3.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd05622  81 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDR-YLYMVMEYMPGGD 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskRCLRDDSGRMALSKTFCG 177
Cdd:cd05622 160 LVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG---TCMKMNKEGMVRCDTAVG 235
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQ---GIPYQPKVYDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQK-EHRVNFPRSKHLTGECKDLIYHM 252
Cdd:cd05622 236 TPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPfYADSLVGTYSKIMNhKNSLTFPDDNDISKEAKNLICAF 315
                       250
                ....*....|....*....
gi 14042947 253 LQPDVNR--RLHIDEILSH 269
Cdd:cd05622 316 LTDREVRlgRNGVEEIKRH 334
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
18-267 3.81e-24

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 100.10  E-value: 3.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdfLEKFLpREIEILAMLNHCSIIKTY---EIFETSHGK-VYIVMELA 93
Cdd:cd13985   8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQ--LRVAI-KEIEIMKRLCGHPNIVQYydsAILSSEGRKeVLLLMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 vQGDLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDFNIKLSDF----SFSKRCLR-- 163
Cdd:cd13985  85 -PGSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFgsatTEHYPLERae 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 ------DDSGRMAlsktfcgSPAYAAPEVLQGIPYQP---KVyDIWSLGVILYIMVCGSMPYDDSNIkkmLRIQKEhRVN 234
Cdd:cd13985 164 evniieEEIQKNT-------TPMYRAPEMIDLYSKKPigeKA-DIWALGCLLYKLCFFKLPFDESSK---LAIVAG-KYS 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 235 FPRSKHLTGECKDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd13985 232 IPEQPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
18-273 4.52e-24

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: 99.73  E-value: 4.52e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILaMLNHCS-IIKTYEIFeTSHGKVYIVMELAVQG 96
Cdd:cd06605   9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEA--LQKQILRELDVL-HKCNSPyIVGFYGAF-YSEGDISICMEYMDGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHD-LDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDsgrmaLSKTF 175
Cdd:cd06605  85 SLDKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQ-LVDS-----LAKTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRI--QKEHRVNFPR----SKHLTGECKDLI 249
Cdd:cd06605 159 VGTRSYMAPERISGGKYTVKS-DIWSLGLSLVELATGRFPYPPPNAKPSMMIfeLLSYIVDEPPpllpSGKFSPDFQDFV 237
                       250       260
                ....*....|....*....|....
gi 14042947 250 YHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd06605 238 SQCLQKDPTERPSYKELMEHPFIK 261
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
74-271 5.08e-24

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: 98.96  E-value: 5.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  74 KTYEIFETSHGkvyivmelavqgDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLS 153
Cdd:cd14022  59 KAYVFFERSYG------------DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVK 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 154 DFSFSKRCL---RDDSgrmaLSKTFcGSPAYAAPEVLQGI-PYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQK 229
Cdd:cd14022 127 LESLEDAYIlrgHDDS----LSDKH-GCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR 201
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 14042947 230 EHRVNFPRSkhLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14022 202 RGQFNIPET--LSPKAKCLIRSILRREPSERLTSQEILDHPW 241
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-219 6.56e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 102.95  E-value: 6.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKII------DrkkapADFLEKFLpREIEILAMLNHCSIIKTYEIFETsHGK 85
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLrpdlarD-----PEFVARFR-REAQSAASLSHPNIVSVYDVGED-GGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   86 VYIVMELaVQG-DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrd 164
Cdd:NF033483  82 PYIVMEY-VDGrTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR----- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947  165 dsgrmALSKT-------FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD-DS 219
Cdd:NF033483 156 -----ALSSTtmtqtnsVLGTVHYLSPEQARGGTVDARS-DIYSLGIVLYEMLTGRPPFDgDS 212
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
13-269 7.04e-24

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: 99.69  E-value: 7.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  13 LLGInLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMEL 92
Cdd:cd07848   5 VLGV-VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTL-RELKMLRTLKQENIVELKEAFR-RRGKLYLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLELIKT--RGALhEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrdDSGRMA 170
Cdd:cd07848  82 -VEKNMLELLEEmpNGVP-PEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNL---SEGSNA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKE------------------H 231
Cdd:cd07848 157 NYTEYVATRWYRSPELLLGAPYG-KAVDMWSVGCILGELSDGQPLFpGESEIDQLFTIQKVlgplpaeqmklfysnprfH 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 232 RVNFPRSKH-----------LTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07848 236 GLRFPAVNHpqslerrylgiLSGVLLDLMKNLLKLNPTDRYLTEQCLNH 284
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
60-218 7.37e-24

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: 98.34  E-value: 7.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETShgKVY-IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLK 138
Cdd:cd14059  31 DIKHLRKLNHPNIIKFKGVCTQA--PCYcILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLK 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 139 CDNLLLDKDFNIKLSDFSFSKRcLRDDSGRMalskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD 218
Cdd:cd14059 109 SPNVLVTYNDVLKISDFGTSKE-LSEKSTKM----SFAGTVAWMAPEVIRNEPCSEKV-DIWSFGVVLWELLTGEIPYKD 182
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
18-224 7.81e-24

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: 100.42  E-value: 7.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAM-LNHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTD-KLYFVLDFVNGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKTFC 176
Cdd:cd05604  83 ELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSD----TTTTFC 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKM 224
Cdd:cd05604 159 GTPEYLAPEVIRKQPYDNTV-DWWCLGSVLYEMLYGLPPFYCRDTAEM 205
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
14-269 7.95e-24

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: 98.96  E-value: 7.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSERLKFNVAIKIID-RKKAPADFLE-KFLPREIEILAMLNHCSIIKTYEIFETSHGK-VYIVM 90
Cdd:cd06652   6 LGKLLGQGAFGRVYLCYDADTGRELAVKQVQfDPESPETSKEvNALECEIQLLKNLLHERIVQYYGCLRDPQERtLSIFM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR----CLrddS 166
Cdd:cd06652  86 EYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRlqtiCL---S 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRMALSKTfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddSNIKKMLRIQK--EHRVNFPRSKHLTGE 244
Cdd:cd06652 163 GTGMKSVT--GTPYWMSPEVISGEGYGRKA-DIWSVGCTVVEMLTEKPPW--AEFEAMAAIFKiaTQPTNPQLPAHVSDH 237
                       250       260
                ....*....|....*....|....*
gi 14042947 245 CKDLIYHMLQpDVNRRLHIDEILSH 269
Cdd:cd06652 238 CRDFLKRIFV-EAKLRPSADELLRH 261
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
79-261 1.05e-23

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: 99.99  E-value: 1.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FETShGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05614  74 FQTD-AKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KRCLRDDSGRmalSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYD-----DSNIKKMLRIQKehrV 233
Cdd:cd05614 153 KEFLTEEKER---TYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTlegekNTQSEVSRRILK---C 226
                       170       180
                ....*....|....*....|....*...
gi 14042947 234 NFPRSKHLTGECKDLIYHMLQPDVNRRL 261
Cdd:cd05614 227 DPPFPSFIGPVARDLLQKLLCKDPKKRL 254
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
18-272 1.21e-23

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: 98.49  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKapaDFLEKFLpREIEILAMLN------HCSIIKTYEIFeTSHGKVYIVME 91
Cdd:cd14133   7 LGKGTFGQVVKCYDLLTGEEVALKIIKNNK---DYLDQSL-DEIRLLELLNkkdkadKYHIVRLKDVF-YFKNHLCIVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQG--DLLELIKTRGaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSkrCLRDDsg 167
Cdd:cd14133  82 LLSQNlyEFLKQNKFQY-LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSS--CFLTQ-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 rmALSkTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECK- 246
Cdd:cd14133 157 --RLY-SYIQSRYYRAPEVILGLPYDEKI-DMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKADd 232
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 247 ----DLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14133 233 elfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
3-269 1.40e-23

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: 99.55  E-value: 1.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   3 DAAVLKRrgYLLGINLGEGSYAKVKSAYSERLKFNVAIK-IIDRKKAPADFLEKFlpREIEIL-AMLNHCSIIKTYEIFE 80
Cdd:cd07852   2 DKHILRR--YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAFRNATDAQRTF--REIMFLqELNDHPNIIKLLNVIR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  81 TSHGK-VYIVMELaVQGDLLELIKtRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSk 159
Cdd:cd07852  78 AENDKdIYLVFEY-METDLHAVIR-ANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLA- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 160 RCLRDDSGRMalsktfcGSPA---------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS----------------- 213
Cdd:cd07852 155 RSLSQLEEDD-------ENPVltdyvatrwYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKplfpgtstlnqlekiie 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 214 ---MPY--DDSNIKKMLRIQKEHRVNFPRSKHLTG-------ECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07852 228 vigRPSaeDIESIQSPFAATMLESLPPSRPKSLDElfpkaspDALDLLKKLLVFNPNKRLTAEEALRH 295
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
9-284 1.82e-23

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: 98.57  E-value: 1.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYI 88
Cdd:cd06658  21 REYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQR---RELLFNEVVIMRDYHHENVVDMYNSYLVGD-ELWV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELaVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGR 168
Cdd:cd06658  97 VMEF-LEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKR 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 malsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRSKHLTGECKD 247
Cdd:cd06658 176 ----KSLVGTPYWMAPEVISRLPYGTEV-DIWSLGIMVIEMIDGEPPYfNEPPLQAMRRIRDNLPPRVKDSHKVSSVLRG 250
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSHCWMqpKARGSPSVAI 284
Cdd:cd06658 251 FLDLMLVREPSQRATAQELLQHPFL--KLAGPPSCIV 285
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
60-221 1.94e-23

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: 97.96  E-value: 1.94e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEIL-AMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKT----RGALHEDEARKKFHQLSLAIKYCH-DLDVV 133
Cdd:cd08528  58 EVNIIkEQLRHPNIVRYYKTFLEND-RLYIVMELIEGAPLGEHFSSlkekNEHFTEDRIWNIFVQMVLALRYLHkEKQIV 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 134 HRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgRMalsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGS 213
Cdd:cd08528 137 HRDLKPNNIMLGEDDKVTITDFGLAKQKGPESS-KM---TSVVGTILYSCPEIVQNEPYGEKA-DIWALGCILYQMCTLQ 211

                ....*...
gi 14042947 214 MPYDDSNI 221
Cdd:cd08528 212 PPFYSTNM 219
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
18-274 2.56e-23

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: 99.29  E-value: 2.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFlEKFLPREIEILAMLNHCSIIKTYEIFETSHG-----KVYIVMEL 92
Cdd:cd07851  23 VGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIH-AKRTYRELRLLKHMKHENVIGLLDVFTPASSledfqDVYLVTHL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLELIKTRgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAls 172
Cdd:cd07851 102 -MGADLNNIVKCQ-KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVA-- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 ktfcgSPAYAAPEV-LQGIPYQPKVyDIWSLGVILYIMVCGS--MPYDDSN--IKK------------MLRIQKEHRVNF 235
Cdd:cd07851 178 -----TRWYRAPEImLNWMHYNQTV-DIWSVGCIMAELLTGKtlFPGSDHIdqLKRimnlvgtpdeelLKKISSESARNY 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 14042947 236 PRSKHLTGECK-------------DLIYHMLQPDVNRRLHIDEILSHCWMQP 274
Cdd:cd07851 252 IQSLPQMPKKDfkevfsganplaiDLLEKMLVLDPDKRITAAEALAHPYLAE 303
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
11-272 2.72e-23

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: 97.51  E-value: 2.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKApADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVM 90
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNA-SKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLRDDSGR 168
Cdd:cd08223  80 GFCEGGDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR--VLESSSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MAlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddsNIKKM----LRIQKEHRVNFPrsKHLTGE 244
Cdd:cd08223 158 MA--TTLIGTPYYMSPELFSNKPYNHKS-DVWALGCCVYEMATLKHAF---NAKDMnslvYKILEGKLPPMP--KQYSPE 229
                       250       260
                ....*....|....*....|....*...
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd08223 230 LGELIKAMLHQDPEKRPSVKRILRQPYI 257
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
60-269 2.83e-23

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 97.62  E-value: 2.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   60 EIEILA---MLNHCSIIKTYEIFETSHGkVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRD 136
Cdd:PHA03390  56 AIEPMVhqlMKDNPNFIKLYYSVTTLKG-HVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHND 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  137 LKCDNLLLD-KDFNIKLSDFSFSKR----CLRDdsgrmalsktfcGSPAYAAPEVLQGIPYQPKvYDIWSLGVILYIMVC 211
Cdd:PHA03390 135 IKLENVLYDrAKDRIYLCDYGLCKIigtpSCYD------------GTLDYFSPEKIKGHNYDVS-FDWWAVGVLTYELLT 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947  212 GSMPYDDS-----NIKKMLRIQKEHrvnFPRSKHLTGECKDLIYHMLQPDVNRRLH-IDEILSH 269
Cdd:PHA03390 202 GKHPFKEDedeelDLESLLKRQQKK---LPFIKNVSKNANDFVQSMLKYNINYRLTnYNEIIKH 262
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
19-272 2.90e-23

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 97.76  E-value: 2.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVKSAYSERLKFNVAIKIIDRKkapADFLEKFLPrEIEILAML-NHCSIIKTYEIF-----ETSHGKVYIVMEL 92
Cdd:cd06608  15 GEGTYGKVYKARHKKTGQLAAIKIMDII---EDEEEEIKL-EINILRKFsNHPNIATFYGAFikkdpPGGDDQLWLVMEY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKtrgALHEDEARKKFHQLS-------LAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDD 165
Cdd:cd06608  91 CGGGSVTDLVK---GLRKKGKRLKEEWIAyilretlRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS-AQLDST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRmalSKTFCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQkehRVNFPRSKH 240
Cdd:cd06608 167 LGR---RNTFIGTPYWMAPEVIACDQQPDASYdarcDVWSLGITAIELADGKPPLCDMHpMRALFKIP---RNPPPTLKS 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 14042947 241 LTGECK---DLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06608 241 PEKWSKefnDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
52-272 3.06e-23

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 97.27  E-value: 3.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  52 FLEKFLP-----------REIEILAMLNHCSIIKTYEIFETSHGKVYIvMELAVQGDLLELIKTRG-ALHEDEARKKFHQ 119
Cdd:cd14114  30 FAAKFIMtphesdketvrKEIQIMNQLHHPKLINLHDAFEDDNEMVLI-LEFLSGGELFERIAAEHyKMSEAEVINYMRQ 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 120 LSLAIKYCHDLDVVHRDLKCDNLLLD--KDFNIKLSDFSFSKRCLRDDSgrmalSKTFCGSPAYAAPEVLQGIP---YQp 194
Cdd:cd14114 109 VCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKES-----VKVTTGTAEFAAPEIVEREPvgfYT- 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 195 kvyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14114 183 ---DMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSafSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
79-273 3.38e-23

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: 97.76  E-value: 3.38e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FETShGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05613  74 FQTD-TKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLS 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KRCLRDDSGRmalSKTFCGSPAYAAPEVLQGIPY-QPKVYDIWSLGVILYIMVCGSMPY-----DDSNIKKMLRIQKEHR 232
Cdd:cd05613 153 KEFLLDENER---AYSFCGTIEYMAPEIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFtvdgeKNSQAEISRRILKSEP 229
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 233 vnfPRSKHLTGECKDLIYHMLQPDVNRRL-----HIDEILSHCWMQ 273
Cdd:cd05613 230 ---PYPQEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQ 272
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
12-286 3.48e-23

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: 97.62  E-value: 3.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadflEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVME 91
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGAD----QVLVKKEISILNIARHRNILRLHESFE-SHEELVMIFE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKT-RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRCLRDDSGR 168
Cdd:cd14104  77 FISGVDIFERITTaRFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQLKPGDKFR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSktfcgSPAYAAPEVLQGiPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECK 246
Cdd:cd14104 157 LQYT-----SAEFYAPEVHQH-ESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEafKNISIEAL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAINK 286
Cdd:cd14104 231 DFVDRLLVKERKSRMTAQEALNHPWLKQGMETVSSKDIKT 270
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
60-269 4.00e-23

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 97.11  E-value: 4.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEifETSHGKVY-IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLK 138
Cdd:cd06630  53 EIRMMARLNHPNIVRMLG--ATQHKSHFnIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLK 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 139 CDNLLLDKD-FNIKLSDFSFSKRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYD 217
Cdd:cd06630 131 GANLLVDSTgQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGEQYG-RSCDVWSVGCVIIEMATAKPPWN 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 218 DSNIKKMLR-IQKEHRVNFPRS--KHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd06630 210 AEKISNHLAlIFKIASATTPPPipEHLSPGLRDVTLRCLELQPEDRPPARELLKH 264
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-269 4.86e-23

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: 98.95  E-value: 4.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkapadFLEKFLPR-----EIEILAMLNHCSIIKTYEIFETSHgKVYIVMEL 92
Cdd:cd05600  19 VGQGGYGSVFLARKKDTGEICALKIMKKK-----VLFKLNEVnhvltERDILTTTNSPWLVKLLYAFQDPE-NVYLAMEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSK------------- 159
Cdd:cd05600  93 VPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesmki 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 160 ----------------------RCLRDDSGRMAlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD 217
Cdd:cd05600 173 rleevkntafleltakerrniyRAMRKEDQNYA--NSVVGSPDYMAPEVLRGEGYDLTV-DYWSLGCILFECLVGFPPFS 249
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 218 DSNI----------KKMLR--IQKEHRVNFprskHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd05600 250 GSTPnetwanlyhwKKTLQrpVYTDPDLEF----NLSDEAWDLITKLITDPQDRLQSPEQIKNH 309
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
18-269 6.02e-23

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: 96.80  E-value: 6.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQgD 97
Cdd:cd07860   8 IGEGTYGVVYKARNKLTGEVVALKKI-RLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTEN-KLYLVFEFLHQ-D 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLEL--IKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsgrmALSKTF 175
Cdd:cd07860  85 LKKFmdASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADF--------------GLARAF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 cGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRI---------------- 227
Cdd:cd07860 151 -GVPVrtythevvtlwYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFpGDSEIDQLFRIfrtlgtpdevvwpgvt 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 14042947 228 -QKEHRVNFPR---------SKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07860 230 sMPDYKPSFPKwarqdfskvVPPLDEDGRDLLSQMLHYDPNKRISAKAALAH 281
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
18-260 6.56e-23

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 98.13  E-value: 6.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   18 LGEGSYAKVKSAYSERLKFN-VAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQG 96
Cdd:PTZ00426  38 LGTGSFGRVILATYKNEDFPpVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFK-DESYLYLVLEFVIGG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrddsgrMALSKTFC 176
Cdd:PTZ00426 117 EFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV-------DTRTYTLC 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  177 GSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSniKKMLRIQK--EHRVNFPrsKHLTGECKDLIYHMLQ 254
Cdd:PTZ00426 190 GTPEYIAPEILLNVGHG-KAADWWTLGIFIYEILVGCPPFYAN--EPLLIYQKilEGIIYFP--KFLDNNCKHLMKKLLS 264

                 ....*.
gi 14042947  255 PDVNRR 260
Cdd:PTZ00426 265 HDLTKR 270
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
18-272 7.40e-23

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: 96.14  E-value: 7.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVI-NKQNSKD--KEMVLLEIQVMNQLNHRNLIQLYEAIETPN-EIVLFMEYVEGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRClrddSGRMALSKT 174
Cdd:cd14190  88 LFErIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRY----NPREKLKVN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FcGSPAYAAPEVLQgipYQPKVY--DIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKDLIY 250
Cdd:cd14190 164 F-GTPEFLSPEVVN---YDQVSFptDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEEtfEHVSDEAKDFVS 239
                       250       260
                ....*....|....*....|..
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14190 240 NLIIKERSARMSATQCLKHPWL 261
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
18-269 9.19e-23

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: 95.97  E-value: 9.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKF----NVAIKIIDRKKAPADFlEKfLPREIEILAMLNHCSIIkTYEIFETSHGKVYIVMELA 93
Cdd:cd06631   9 LGKGAYGTVYCGLTSTGQLiavkQVELDTSDKEKAEKEY-EK-LQEEVDLLKTLKHVNIV-GYLGTCLEDNVVSIFMEFV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR-CLRDDSGRMA-L 171
Cdd:cd06631  86 PGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRlCINLSSGSQSqL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRIqKEHRVNFPR-SKHLTGECKDLI 249
Cdd:cd06631 166 LKSMRGTPYWMAPEVINETGHGRKS-DIWSIGCTVFEMATGKPPWADMNpMAAIFAI-GSGRKPVPRlPDKFSPEARDFV 243
                       250       260
                ....*....|....*....|
gi 14042947 250 YHMLQPDVNRRLHIDEILSH 269
Cdd:cd06631 244 HACLTRDQDERPSAEQLLKH 263
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
84-272 9.38e-23

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: 95.57  E-value: 9.38e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  84 GKVYIVMELAvQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCL- 162
Cdd:cd13976  58 TKAYVFFERD-HGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVIl 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 --RDDSgrmaLSKTFcGSPAYAAPEVLQ-GIPYQPKVYDIWSLGVILYIMVCGSMPYDDSniKKMLRIQKEHRVNFPRSK 239
Cdd:cd13976 137 egEDDS----LSDKH-GCPAYVSPEILNsGATYSGKAADVWSLGVILYTMLVGRYPFHDS--EPASLFAKIRRGQFAIPE 209
                       170       180       190
                ....*....|....*....|....*....|...
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd13976 210 TLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
18-269 9.90e-23

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: 96.28  E-value: 9.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYA---KVKSAYSERLkfnVAIKIIdrKKAPADFLEKFLPREIEILAMLNHCSIIKTYEI-FETSHgkVYIVMELA 93
Cdd:cd14046  14 LGKGAFGqvvKVRNKLDGRY---YAIKKI--KLRSESKNNSRILREVMLLSRLNHQHVVRYYQAwIERAN--LYIQMEYC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF---SFSKRCLRDDSGRMA 170
Cdd:cd14046  87 EKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFglaTSNKLNVELATQDIN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPA-----------YAAPEVLQGIP--YQPKVyDIWSLGVILYIMvcgSMPYDDS----NIKKMLRIQK-EHR 232
Cdd:cd14046 167 KSTSAALGSSgdltgnvgtalYVAPEVQSGTKstYNEKV-DMYSLGIIFFEM---CYPFSTGmervQILTALRSVSiEFP 242
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 14042947 233 VNFPRSKHltGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14046 243 PDFDDNKH--SKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
18-267 1.30e-22

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: 95.53  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERlkfNVAIKIIDRKKAPADFLEKFlpREIEILAMLNHCSIIKTYEIfETSHGKV---YIVMELA 93
Cdd:cd13979  11 LGSGGFGSVyKATYKGE---TVAVKIVRRRRKNRASRQSF--WAELNAARLRHENIVRVLAA-ETGTDFAslgLIIMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSGRMALS 172
Cdd:cd13979  85 GNGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVK-LGEGNEVGTPR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-------IKKMLRIQKEHRVNFprskhLTGE- 244
Cdd:cd13979 164 SHIGGTYTYRAPELLKGERVTPKA-DIYSFGITLWQMLTRELPYAGLRqhvlyavVAKDLRPDLSGLEDS-----EFGQr 237
                       250       260
                ....*....|....*....|...
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd13979 238 LRSLISRCWSAQPAERPNADESL 260
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
66-272 1.55e-22

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: 94.95  E-value: 1.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  66 MLNHCSIIKTYEIFeTSHGKVYIVMElAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD 145
Cdd:cd14024  41 LGPHEGVCSVLEVV-IGQDRAYAFFS-RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFT 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 146 KDFNIKLSDFSFSKRCLRDDSGRMALSKTFCgsPAYAAPEVLQ-GIPYQPKVYDIWSLGVILYIMVCGSMPYDDSniKKM 224
Cdd:cd14024 119 DELRTKLVLVNLEDSCPLNGDDDSLTDKHGC--PAYVGPEILSsRRSYSGKAADVWSLGVCLYTMLLGRYPFQDT--EPA 194
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 225 LRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14024 195 ALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
18-225 2.43e-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: 94.68  E-value: 2.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPADFLEkFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd06613   8 IGSGTYGDVYKARNIATGELAAVKVI--KLEPGDDFE-IIQQEISMLKECRHPNIVAYFGSYLRRD-KLWIVMEYCGGGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF--------SFSKRclrddsgrm 169
Cdd:cd06613  84 LQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFgvsaqltaTIAKR--------- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 170 alsKTFCGSPAYAAPEVLQ---GIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKML 225
Cdd:cd06613 155 ---KSFIGTPYWMAPEVAAverKGGYDGKC-DIWALGITAIELAELQPPMFDLHPMRAL 209
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
18-261 4.56e-22

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: 94.52  E-value: 4.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKD-KLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrcLRDDSGRMALSKTF 175
Cdd:cd05577  80 LKYHIYNVGTRGFSEARAIFYaaEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLG-----LAVEFKGGKKIKGR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQ-GIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKK----MLRIQKEHRVNFPRSkhLTGECKDLIY 250
Cdd:cd05577 155 VGTHGYMAPEVLQkEVAYDFSV-DWFALGCMLYEMIAGRSPFRQRKEKVdkeeLKRRTLEMAVEYPDS--FSPEARSLCE 231
                       250
                ....*....|.
gi 14042947 251 HMLQPDVNRRL 261
Cdd:cd05577 232 GLLQKDPERRL 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
18-253 4.94e-22

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: 96.24  E-value: 4.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDR----KKApadflEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELA 93
Cdd:cd05623  80 IGRGAFGEVAVVKLKNADKVFAMKILNKwemlKRA-----ETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYY 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalS 172
Cdd:cd05623 155 VGGDLLTLLsKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQ---S 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIP-----YQPKVyDIWSLGVILYIMVCGSMP-YDDSNIKKMLRIQK-EHRVNFP-RSKHLTGE 244
Cdd:cd05623 232 SVAVGTPDYISPEILQAMEdgkgkYGPEC-DWWSLGVCMYEMLYGETPfYAESLVETYGKIMNhKERFQFPtQVTDVSEN 310

                ....*....
gi 14042947 245 CKDLIYHML 253
Cdd:cd05623 311 AKDLIRRLI 319
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
18-269 5.72e-22

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: 93.88  E-value: 5.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV--KSAYSERlkfNVAIKIIDRkkapaDFLEkFLPREIEIL-AMLNHCSIIKtYEIFETSHGKVYIVMELAv 94
Cdd:cd13982   9 LGYGSEGTIvfRGTFDGR---PVAVKRLLP-----EFFD-FADREVQLLrESDEHPNVIR-YFCTEKDRQFLYIALELC- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKtRGALHEDEARKKF------HQLSLAIKYCHDLDVVHRDLKCDNLLLDKD-----FNIKLSDFSFSKRClr 163
Cdd:cd13982  78 AASLQDLVE-SPRESKLFLRPGLepvrllRQIASGLAHLHSLNIVHRDLKPQNILISTPnahgnVRAMISDFGLCKKL-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 dDSGRMALSKTF--CGSPAYAAPEVL-QGIPYQP-KVYDIWSLG-VILYIMVCGSMPYDD-----SNIKKmlriqkeHRV 233
Cdd:cd13982 155 -DVGRSSFSRRSgvAGTSGWIAPEMLsGSTKRRQtRAVDIFSLGcVFYYVLSGGSHPFGDklereANILK-------GKY 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 14042947 234 NFPRSKHLtGEC----KDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd13982 227 SLDKLLSL-GEHgpeaQDLIERMIDFDPEKRPSAEEVLNH 265
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
18-269 6.06e-22

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: 95.17  E-value: 6.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDR--------KKAPadflekflpREIEILAMLNHCSII---------KTYEIFE 80
Cdd:cd07850   8 IGSGAQGIVCAAYDTVTGQNVAIKKLSRpfqnvthaKRAY---------RELVLMKLVNHKNIIgllnvftpqKSLEEFQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  81 tshgKVYIVMELaVQGDLLELIKtrgaLHEDEARKKF--HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd07850  79 ----DVYLVMEL-MDANLCQVIQ----MDLDHERMSYllYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 krclrddsgRMAlSKTFCGSPA-----YAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSM--PYDD------------- 218
Cdd:cd07850 150 ---------RTA-GTSFMMTPYvvtryYRAPEVILGMGYKENV-DIWSVGCIMGEMIRGTVlfPGTDhidqwnkiieqlg 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 219 -------SNIKKMLRIQKEHR--------------VNFP-----RSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07850 219 tpsdefmSRLQPTVRNYVENRpkyagysfeelfpdVLFPpdseeHNKLKASQARDLLSKMLVIDPEKRISVDDALQH 295
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
18-269 7.96e-22

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: 95.12  E-value: 7.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRkkapADFLEK----FLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd05627  10 IGRGAFGEVRLVQKKDTGHIYAMKILRK----ADMLEKeqvaHIRAERDILVEADGAWVVKMFYSFQDKR-NLYLIMEFL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS---KRCLRDD----- 165
Cdd:cd05627  85 PGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglKKAHRTEfyrnl 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 -----------------------SGRMALSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIK 222
Cdd:cd05627 165 thnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFMQTGYN-KLCDWWSLGVIMYEMLIGYPPFCSETPQ 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 223 KMLR--IQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNR--RLHIDEILSH 269
Cdd:cd05627 244 ETYRkvMNWKETLVFPPEVPISEKAKDLILRFCTDAENRigSNGVEEIKSH 294
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
18-226 1.15e-21

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 93.11  E-value: 1.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFN--VAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAVQ 95
Cdd:cd14066   1 IGSGGFGTV---YKGVLENGtvVAVKRLNEMNCAA--SKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKL-LVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELiktrgaLHEDEARK--KFHQ-LSLA------IKYCH---DLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLR 163
Cdd:cd14066  75 GSLEDR------LHCHKGSPplPWPQrLKIAkgiargLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLAR--LI 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 164 DDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR 226
Cdd:cd14066 147 PPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKS-DVYSFGVVLLELLTGKPAVDENRENASRK 208
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-267 1.63e-21

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: 92.78  E-value: 1.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIID-----RKKAPADFLekflpREIEILAMLNHCSIIKTYEIFeTSHGKV 86
Cdd:cd08228   4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemmDAKARQDCV-----KEIDLLKQLNHPNVIKYLDSF-IEDNEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELI----KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrcl 162
Cdd:cd08228  78 NIVLELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG---- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 RDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFP--RSKH 240
Cdd:cd08228 154 RFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKS-DIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPplPTEH 232
                       250       260
                ....*....|....*....|....*..
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd08228 233 YSEKLRELVSMCIYPDPDQRPDIGYVH 259
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
21-269 1.74e-21

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: 94.18  E-value: 1.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  21 GSYAKVKSAYSERLKFNVAIKIIDRkkapADFLEKFLPREI----EILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQG 96
Cdd:cd05610  15 GAFGKVYLGRKKNNSKLYAVKVVKK----ADMINKNMVHQVqaerDALALSKSPFIVHLYYSLQSAN-NVYLVMEYLIGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKT-- 174
Cdd:cd05610  90 DVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRELNMMDILTTps 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 -----------------------------------------------FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILY 207
Cdd:cd05610 170 makpkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAV-DWWALGVCLF 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 208 IMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKH-LTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd05610 249 EFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEeLSVNAQNAIEILLTMDPTKRAGLKELKQH 311
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
21-270 2.17e-21

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: 92.04  E-value: 2.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  21 GSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKF--LPREIEILAMLNHCSII-----KTYEIFETSHGKVYIVMELA 93
Cdd:cd14012   7 GTFYLVYEVVLDNSKKPGKFLTSQEYFKTSNGKKQIqlLEKELESLKKLRHPNLVsylafSIERRGRSDGWKVYLLTEYA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF---NIKLSDFSFSKRCLRDDSGRma 170
Cdd:cd14012  87 PGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLLDMCSRG-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 lSKTFCGSPAYAAPEVLQG-IPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIqkehrvnfprSKHLTGECKDLI 249
Cdd:cd14012 165 -SLDEFKQTYWLPPELAQGsKSPTRKT-DVWDLGLLFLQMLFGLDVLEKYTSPNPVLV----------SLDLSASLQDFL 232
                       250       260
                ....*....|....*....|.
gi 14042947 250 YHMLQPDVNRRLHIDEILSHC 270
Cdd:cd14012 233 SKCLSLDPKKRPTALELLPHE 253
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
10-274 3.26e-21

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: 93.20  E-value: 3.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIK--------IIDRKKAPadflekflpREIEILAMLNHCSIIKTYEIFET 81
Cdd:cd07858   5 TKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKkianafdnRIDAKRTL---------REIKLLRHLDHENVIAIKDIMPP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHGK----VYIVMELaVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSF 157
Cdd:cd07858  76 PHREafndVYIVYEL-MDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 158 SkrclRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVI---------------------LYIMVCGSMPY 216
Cdd:cd07858 155 A----RTTSEKGDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIfaellgrkplfpgkdyvhqlkLITELLGSPSE 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 217 DD------SNIKKMLR-IQKEHRVNFPRS-KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQP 274
Cdd:cd07858 231 EDlgfirnEKARRYIRsLPYTPRQSFARLfPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLAS 296
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
60-269 3.82e-21

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: 93.38  E-value: 3.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKC 139
Cdd:cd05629  51 ERDVLAESDSPWVVSLYYSFQDAQ-YLYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKP 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 140 DNLLLDKDFNIKLSDFSFS------------KRCLRDDS-------------------------------GRMALSKTFC 176
Cdd:cd05629 130 DNILIDRGGHIKLSDFGLStgfhkqhdsayyQKLLQGKSnknridnrnsvavdsinltmsskdqiatwkkNRRLMAYSTV 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLR--IQKEHRVNFPRSKHLTGECKDLIYHMLQ 254
Cdd:cd05629 210 GTPDYIAPEIFLQQGYGQEC-DWWSLGAIMFECLIGWPPFCSENSHETYRkiINWRETLYFPDDIHLSVEAEDLIRRLIT 288
                       250
                ....*....|....*..
gi 14042947 255 PDVNR--RLHIDEILSH 269
Cdd:cd05629 289 NAENRlgRGGAHEIKSH 305
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-284 4.65e-21

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: 90.97  E-value: 4.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSeRLKFNVAIKIIDRKK-APADFLEkflprEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQG 96
Cdd:cd05059  12 LGSGQFGVVHLGKW-RGKIDVAIKMIKEGSmSEDDFIE-----EAKVMMKLSHPKLVQLYGVC-TKQRPIFIVTEYMANG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrDDSGRMALSKTF 175
Cdd:cd05059  85 CLLNYLRERrGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVL-DDEYTSSVGTKF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 cgsPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSkhltgeCKDLIYhm 252
Cdd:cd05059 164 ---PVkWSPPEVFMYSKFSSKS-DVWSFGVLMWeVFSEGKMPYERfSNSEVVEHISQGYRLYRPHL------APTEVY-- 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 253 lqpdvnrrlhidEILSHCWmQPKARGSPSVAI 284
Cdd:cd05059 232 ------------TIMYSCW-HEKPEERPTFKI 250
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
15-272 4.66e-21

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: 91.54  E-value: 4.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  15 GINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCS-IIKTYEIFETShGKVYIVMELA 93
Cdd:cd14197  14 GRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEII-HEIAVLELAQANPwVINLHEVYETA-SEMILVLEYA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLE--LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF---NIKLSDFSFSKRCLRDDSGR 168
Cdd:cd14197  92 AGGEIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKNSEELR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALsktfcGSPAYAAPEVLQgipYQP--KVYDIWSLGVILYIMVCGSMPY--DDS-----NIKKMLRIQKEHRVNfprsk 239
Cdd:cd14197 172 EIM-----GTPEYVAPEILS---YEPisTATDMWSIGVLAYVMLTGISPFlgDDKqetflNISQMNVSYSEEEFE----- 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 240 HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14197 239 HLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
18-272 6.12e-21

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: 91.79  E-value: 6.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidrkKAPADFLEKFLP----REIEILAMLNHCSIIKTYEI---------FETSHG 84
Cdd:cd07864  15 IGEGTYGQVYKAKDKDTGELVALK-----KVRLDNEKEGFPitaiREIKILRQLNHRSVVNLKEIvtdkqdaldFKKDKG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELaVQGDLLELIKTrGALH--EDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCL 162
Cdd:cd07864  90 AFYLVFEY-MDHDLMGLLES-GLVHfsEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLA-RLY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 RDDSGRMALSKTFcgSPAYAAPEVLQGIP-YQPKVyDIWSLGVILYIM---------------------VCGS-MPYDDS 219
Cdd:cd07864 167 NSEESRPYTNKVI--TLWYRPPELLLGEErYGPAI-DVWSCGCILGELftkkpifqanqelaqlelisrLCGSpCPAVWP 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 220 NIKKM-----LRIQKEHRVNFPRS-KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd07864 244 DVIKLpyfntMKPKKQYRRRLREEfSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
18-213 6.19e-21

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: 91.24  E-value: 6.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidrkKAPADFLEKFLP----REIEILAMLNHCS-IIKTYEIFetSHGK-VYIVME 91
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALK-----KVALRKLEGGIPnqalREIKALQACQGHPyVVKLRDVF--PHGTgFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LaVQGDLLELIK-TRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMA 170
Cdd:cd07832  81 Y-MLSSLSEVLRdEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA-RLFSEEDPRLY 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 14042947 171 LSKtfCGSPAYAAPEVLQGIP-YQPKVyDIWSLGVILYIMVCGS 213
Cdd:cd07832 159 SHQ--VATRWYRAPELLYGSRkYDEGV-DLWAVGCIFAELLNGS 199
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
18-206 6.49e-21

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: 91.84  E-value: 6.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKapadfleKFLPR---EIEILAMLNH------CSIIKTYEIFE-TSHgkVY 87
Cdd:cd14210  21 LGKGSFGQVVKCLDHKTGQLVAIKIIRNKK-------RFHQQalvEVKILKHLNDndpddkHNIVRYKDSFIfRGH--LC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQgDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSkrCLR 163
Cdd:cd14210  92 IVFELLSI-NLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFGSS--CFE 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14042947 164 DdsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14210 169 G-----EKVYTYIQSRFYRAPEVILGLPYDTAI-DMWSLGCIL 205
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
16-269 6.76e-21

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: 91.62  E-value: 6.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaVQ 95
Cdd:cd06657  26 IKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQR---RELLFNEVVIMRDYQHENVVEMYNSYLVGD-ELWVVMEF-LE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTF 175
Cdd:cd06657 101 GGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRR----KSL 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQ 254
Cdd:cd06657 177 VGTPYWMAPELISRLPYGPEV-DIWSLGIMVIEMVDGEPPYfNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRLLV 255
                       250
                ....*....|....*
gi 14042947 255 PDVNRRLHIDEILSH 269
Cdd:cd06657 256 RDPAQRATAAELLKH 270
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
17-210 6.79e-21

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: 92.04  E-value: 6.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFET----SHGK-VYIVME 91
Cdd:cd07855  12 TIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTL-RELKILRHFKHDNIIAIRDILRPkvpyADFKdVYVVLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LaVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMAL 171
Cdd:cd07855  91 L-MESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMA-RGLCTSPEEHKY 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14042947 172 SKT-FCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMV 210
Cdd:cd07855 169 FMTeYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEML 208
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
18-267 8.62e-21

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: 90.20  E-value: 8.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIfETSHGKVYIVMELAVQGD 97
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTC-RETLPPDLKRKFL-QEARILKQYDHPNIVKLIGV-CVQKQPIMIVMELVPGGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGAlheDEARKKFHQLSL----AIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclRDDSGRMALSK 173
Cdd:cd05041  80 LLTFLRKKGA---RLTVKQLLQMCLdaaaGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR---EEEDGEYTVSD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSP-AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVnfPRSKHLTGECKDLIY 250
Cdd:cd05041 154 GLKQIPiKWTAPEALNYGRYTSES-DVWSFGILLWeIFSLGATPYPGmSNQQTREQIESGYRM--PAPELCPEAVYRLML 230
                       250
                ....*....|....*..
gi 14042947 251 HMLQPDVNRRLHIDEIL 267
Cdd:cd05041 231 QCWAYDPENRPSFSEIY 247
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
18-279 8.90e-21

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: 90.19  E-value: 8.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSErlKFNVAIKIIDRKKAPADFLekflpREIEILAMLNHCSIIKTYEIfETSHGKVYIVMELAVQGD 97
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVKIIESESEKKAFE-----VEVRQLSRVDHPNIIKLYGA-CSNQKPVCLVMEYAEGGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELiktrgaLHEDEARKKF---H------QLSLAIKYCHDLD---VVHRDLKCDNLLL-DKDFNIKLSDFSFSkrClrD 164
Cdd:cd14058  73 LYNV------LHGKEPKPIYtaaHamswalQCAKGVAYLHSMKpkaLIHRDLKPPNLLLtNGGTVLKICDFGTA--C--D 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGRMALSKtfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD---SNIKKMLRIQKehrvnfprskhl 241
Cdd:cd14058 143 ISTHMTNNK---GSAAWMAPEVFEGSKYSEKC-DVFSWGIILWEVITRRKPFDHiggPAFRIMWAVHN------------ 206
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 14042947 242 tGECKDLIYHMLQPdvnrrlhIDEILSHCWMQ-PKARGS 279
Cdd:cd14058 207 -GERPPLIKNCPKP-------IESLMTRCWSKdPEKRPS 237
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
85-271 9.66e-21

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: 90.11  E-value: 9.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVqGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCL-- 162
Cdd:cd14023  59 KAYVFFEKDF-GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHImk 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 -RDDsgrmALSKTFcGSPAYAAPEVLQGI-PYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLriQKEHRVNFPRSKH 240
Cdd:cd14023 138 gEDD----ALSDKH-GCPAYVSPEILNTTgTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALF--SKIRRGQFCIPDH 210
                       170       180       190
                ....*....|....*....|....*....|.
gi 14042947 241 LTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14023 211 VSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
20-271 9.94e-21

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: 90.75  E-value: 9.94e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  20 EGSYAKVKSAYSERLKFNVAIK--IIDRKKapadflEKFlP----REIEILAMLNHCSIIKTYEI-FETSHGKVYIVMEL 92
Cdd:cd07843  15 EGTYGVVYRARDKKTGEIVALKklKMEKEK------EGF-PitslREINILLKLQHPNIVTVKEVvVGSNLDKIYMVMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLELIKT-RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRclrddsgrmal 171
Cdd:cd07843  88 -VEHDLKSLMETmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE----------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 sktfCGSPA-----------YAAPEVLQGIP-YQPKVyDIWSLGVIL---------------------YIMVCGSmPYDD 218
Cdd:cd07843 156 ----YGSPLkpytqlvvtlwYRAPELLLGAKeYSTAI-DMWSVGCIFaelltkkplfpgkseidqlnkIFKLLGT-PTEK 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 219 S--------NIKKMLRiqKEHRVNFPRSK----HLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07843 230 IwpgfselpGAKKKTF--TKYPYNQLRKKfpalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
18-213 2.21e-20

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: 90.83  E-value: 2.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidrKKAPAD---FLEKFLpREIEILAMLNHCSIIKTYEI-----FETSHgKVYIV 89
Cdd:cd07849  13 IGEGAYGMVCSAVHKPTGQKVAIK----KISPFEhqtYCLRTL-REIKILLRFKHENIIGILDIqrpptFESFK-DVYIV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELaVQGDLLELIKTRgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCL--RDDSG 167
Cdd:cd07849  87 QEL-METDLYKLIKTQ-HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADpeHDHTG 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 168 RMAlskTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS 213
Cdd:cd07849 165 FLT---EYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNR 207
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
18-272 3.32e-20

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: 88.82  E-value: 3.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKII-KARSQKE--KEEVKNEIEVMNQLNHANLIQLYDAFE-SRNDIVLVMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFN-IKLSDFSFSKRClrddSGRMALSKT 174
Cdd:cd14193  88 LFDrIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRY----KPREKLRVN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FcGSPAYAAPEVLQgIPYQPKVYDIWSLGVILYIMVCGSMPY----DDSNIKKMLRIQKEhrVNFPRSKHLTGECKDLIY 250
Cdd:cd14193 164 F-GTPEFLAPEVVN-YEFVSFPTDMWSLGVIAYMLLSGLSPFlgedDNETLNNILACQWD--FEDEEFADISEEAKDFIS 239
                       250       260
                ....*....|....*....|..
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14193 240 KLLIKEKSWRMSASEALKHPWL 261
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
18-249 3.37e-20

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: 90.87  E-value: 3.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRkkapADFLEK----FLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd05628   9 IGRGAFGEVRLVQKKDTGHVYAMKILRK----ADMLEKeqvgHIRAERDILVEADSLWVVKMFYSFQDKL-NLYLIMEFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS---KRCLRDD----- 165
Cdd:cd05628  84 PGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCtglKKAHRTEfyrnl 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 -----------------------SGRMALSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIK 222
Cdd:cd05628 164 nhslpsdftfqnmnskrkaetwkRNRRQLAFSTVGTPDYIAPEVFMQTGYN-KLCDWWSLGVIMYEMLIGYPPFCSETPQ 242
                       250       260
                ....*....|....*....|....*....
gi 14042947 223 KMLR--IQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd05628 243 ETYKkvMNWKETLIFPPEVPISEKAKDLI 271
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
18-271 3.40e-20

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: 88.48  E-value: 3.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadflEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKK----KEQAAHEAALLQHLQHPQYITLHDTYE-SPTSYILVLELMDDGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF---NIKLSDFsfskrclrDDSGRMALSKT 174
Cdd:cd14115  76 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDL--------EDAVQISGHRH 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 ---FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQkehRVNFPRSKHLTGE----CK 246
Cdd:cd14115 148 vhhLLGNPEFAAPEVIQGTPVSLAT-DIWSIGVLTYVMLSGVSPFlDESKEETCINVC---RVDFSFPDEYFGDvsqaAR 223
                       250       260
                ....*....|....*....|....*
gi 14042947 247 DLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14115 224 DFINVILQEDPRRRPTAATCLQHPW 248
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
18-220 4.47e-20

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: 89.84  E-value: 4.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIF-------------ETSHG 84
Cdd:cd07854  13 LGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQS---VKHALREIKIIRRLDHDNIVKVYEVLgpsgsdltedvgsLTELN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELaVQGDLLELIKtRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFSFSKRCLR 163
Cdd:cd07854  90 SVYIVQEY-METDLANVLE-QGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLARIVDP 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 164 DDSGRMALSKTFCgSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSN 220
Cdd:cd07854 168 HYSHKGYLSEGLV-TKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAH 223
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
18-269 5.83e-20

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 88.58  E-value: 5.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApADFLEKfLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQGD 97
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEA-EDEIED-IQQEITVLSQCDSPYITRYYGSYLKG-TKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTrGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06642  89 ALDLLKP-GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR----NTFVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHlTGECKDLIYHMLQPDV 257
Cdd:cd06642 164 TPFWMAPEVIKQSAYDFKA-DIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQH-SKPFKEFVEACLNKDP 241
                       250
                ....*....|..
gi 14042947 258 NRRLHIDEILSH 269
Cdd:cd06642 242 RFRPTAKELLKH 253
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
18-272 8.30e-20

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: 87.71  E-value: 8.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdflEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKE---REEVKNEINIMNQLNHVNLIQLYDAFESKT-NLTLIMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRClrddSGRMALSKT 174
Cdd:cd14192  88 LFDrITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLARRY----KPREKLKVN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FcGSPAYAAPEVLQgipYQPKVY--DIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRS--KHLTGECKDLIY 250
Cdd:cd14192 164 F-GTPEFLAPEVVN---YDFVSFptDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEafENLSEEAKDFIS 239
                       250       260
                ....*....|....*....|..
gi 14042947 251 HMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14192 240 RLLVKEKSCRMSATQCLKHEWL 261
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
18-269 8.78e-20

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: 89.72  E-value: 8.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELAVQGD 97
Cdd:cd05625   9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ-DKDNLYFVMDYIPGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSF--------------SKRCLR 163
Cdd:cd05625  88 MMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqSGDHLR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDS-----------------------------GRMALSKTFCGSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSM 214
Cdd:cd05625 168 QDSmdfsnewgdpencrcgdrlkplerraarqHQRCLAHSLVGTPNYIAPEVLLRTGYT-QLCDWWSVGVILFEMLVGQP 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 215 PY-DDSNIKKMLRIQK-EHRVNFPRSKHLTGECKDLIYHMLQPDVNR--RLHIDEILSH 269
Cdd:cd05625 247 PFlAQTPLETQMKVINwQTSLHIPPQAKLSPEASDLIIKLCRGPEDRlgKNGADEIKAH 305
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
18-269 9.84e-20

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: 88.10  E-value: 9.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrkKAPADflEKFLP----REIEILAML---NHCSIIKTYEIFETSHG----KV 86
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKV---RVPLS--EEGIPlstiREIALLKQLesfEHPNVVRLLDVCHGPRTdrelKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQgDL---LELIKTRGaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclr 163
Cdd:cd07838  82 TLVFEHVDQ-DLatyLDKCPKPG-LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADF-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 ddsgrmALSKTFCGSPA---------YAAPEVLQGIPYQPKVyDIWSLGVILYIM------VCGsmPYDDSNIKKMLRI- 227
Cdd:cd07838 152 ------GLARIYSFEMAltsvvvtlwYRAPEVLLQSSYATPV-DMWSVGCIFAELfnrrplFRG--SSEADQLGKIFDVi 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14042947 228 ----QKE-------HRVNFPRS---------KHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07838 223 glpsEEEwprnsalPRSSFPSYtprpfksfvPEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
18-269 1.06e-19

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: 88.95  E-value: 1.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRkkaPADFL--EKFLPREIEILAMLNHCSIIKTYEIFETS-----HGKVYIVM 90
Cdd:cd07878  23 VGSGAYGSVCSAYDTRLRQKVAVKKLSR---PFQSLihARRTYRELRLLKHMKHENVIGLLDVFTPAtsienFNEVYLVT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELaVQGDLLELIKTRgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMA 170
Cdd:cd07878 100 NL-MGADLNNIVKCQ-KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVA 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 lsktfcgSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS--MPYDD--SNIKKML------------RIQKEHRVN 234
Cdd:cd07878 178 -------TRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKalFPGNDyiDQLKRIMevvgtpspevlkKISSEHARK 250
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 235 FPRS-KHLTGE------------CKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07878 251 YIQSlPHMPQQdlkkifrganplAIDLLEKMLVLDSDKRISASEALAH 298
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
59-269 1.80e-19

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 86.95  E-value: 1.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAML-NHCSIIK--TYEIFETSHG--KVYIVMELAVQGDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLD 131
Cdd:cd14037  49 REIEIMKRLsGHKNIVGyiDSSANRSGNGvyEVLLLMEYCKGGGVIDLMNQRlqTGLTESEILKIFCDVCEAVAAMHYLK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 132 --VVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRD---DSGRMALSK-----TfcgSPAYAAPEVL---QGIPYQPKVyD 198
Cdd:cd14037 129 ppLIHRDLKVENVLISDSGNYKLCDFGSATTKILPpqtKQGVTYVEEdikkyT---TLQYRAPEMIdlyRGKPITEKS-D 204
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 199 IWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLtgecKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14037 205 IWALGCLLYKLCFYTTPFEESGQLAILNGNFTFPDNSRYSKRL----HKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
18-261 2.24e-19

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: 86.88  E-value: 2.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFET-SHgkVYIVMELAVQG 96
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETkTH--LCLVMSLMNGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrcLRDDSGRMALSKT 174
Cdd:cd05607  88 DLKYHIYNVGERGIEMERVIFYsaQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLA---VEVKEGKPITQRA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 fcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIK----KMLRIQKEHRVNFpRSKHLTGECKDLIY 250
Cdd:cd05607 165 --GTNGYMAPEILKEESYSYPV-DWFAMGCSIYEMVAGRTPFRDHKEKvskeELKRRTLEDEVKF-EHQNFTEEAKDICR 240
                       250
                ....*....|.
gi 14042947 251 HMLQPDVNRRL 261
Cdd:cd05607 241 LFLAKKPENRL 251
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
12-206 2.35e-19

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: 86.82  E-value: 2.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadfLEKFLP-REIEILAMLN-HCSIIKTYEIF-ETSHgkVYI 88
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYS---WEECMNlREVKSLRKLNeHPNIVKLKEVFrENDE--LYF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELaVQGDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrclrdds 166
Cdd:cd07830  76 VFEY-MEGNLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA-------- 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 14042947 167 gRMALSK----TFCGSPAYAAPEV-LQGIPYQPKVyDIWSLGVIL 206
Cdd:cd07830 147 -REIRSRppytDYVSTRWYRAPEIlLRSTSYSSPV-DIWALGCIM 189
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
18-269 2.90e-19

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: 86.64  E-value: 2.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApADFLEKfLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEA-EDEIED-IQQEITVLSQCDSPYVTKYYGSY-LKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTrGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06640  89 ALDLLRA-GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR----NTFVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRiqkeHRVNFPrSKHLTGE----CKDLIYHML 253
Cdd:cd06640 164 TPFWMAPEVIQQSAYDSKA-DIWSLGITAIELAKGEPPNSDMHPMRVLF----LIPKNN-PPTLVGDfskpFKEFIDACL 237
                       250
                ....*....|....*.
gi 14042947 254 QPDVNRRLHIDEILSH 269
Cdd:cd06640 238 NKDPSFRPTAKELLKH 253
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
16-272 3.65e-19

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: 85.74  E-value: 3.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEI-FETSHGKVYIVMELAV 94
Cdd:cd13983   7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFK-QEIEILKSLKHPNIIKFYDSwESKSKKEVIFITELMT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDFN-IKLSDFSFSKRClrddsgRMAL 171
Cdd:cd13983  86 SGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGeVKIGDLGLATLL------RQSF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFCGSPAYAAPEVLQGiPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLR--IQKEHRVNFPRSKHltGECKDL 248
Cdd:cd13983 160 AKSVIGTPEFMAPEMYEE-HYDEKV-DIYAFGMCLLEMATGEYPYSEcTNAAQIYKkvTSGIKPESLSKVKD--PELKDF 235
                       250       260
                ....*....|....*....|....
gi 14042947 249 IYHMLQPdVNRRLHIDEILSHCWM 272
Cdd:cd13983 236 IEKCLKP-PDERPSARELLEHPFF 258
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-272 4.17e-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: 86.13  E-value: 4.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLG-INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHC-SIIKTYEIFETSHgKVYIV 89
Cdd:cd14198   9 YILTsKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEIL-HEIAVLELAKSNpRVVNLHEVYETTS-EIILI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF---NIKLSDFSFSKRClrD 164
Cdd:cd14198  87 LEYAAGGEIFNLCVPDLAemVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKI--G 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 DSGRMalsKTFCGSPAYAAPEVLQgipYQP--KVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQKEH----RVNFPR 237
Cdd:cd14198 165 HACEL---REIMGTPEYLAPEILN---YDPitTATDMWNIGVIAYMLLTHESPFvGEDNQETFLNISQVNvdysEETFSS 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 14042947 238 SKHLTgecKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14198 239 VSQLA---TDFIQKLLVKNPEKRPTAEICLSHSWL 270
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
18-280 4.23e-19

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 86.34  E-value: 4.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII--DRKKApadfLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQ 95
Cdd:cd06620  13 LGAGNGGSVSKVLHIPTGTIMAKKVIhiDAKSS----VRKQILRELQILHECHSPYIVSFYGAFLNENNNIIICMEYMDC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHD-LDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRddsgrmALSKT 174
Cdd:cd06620  89 GSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELIN------SIADT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-----------IKKML-RIQKEHRVNFPRSKHLT 242
Cdd:cd06620 163 FVGTSTYMSPERIQGGKYSVKS-DVWSLGLSIIELALGEFPFAGSNddddgyngpmgILDLLqRIVNEPPPRLPKDRIFP 241
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSP 280
Cdd:cd06620 242 KDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASD 279
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
18-227 4.73e-19

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: 87.02  E-value: 4.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRkkaPADFL--EKFLPREIEILAMLNHCSIIKTYEIFETSHG-----KVYIVM 90
Cdd:cd07877  25 VGSGAYGSVCAAFDTKTGLRVAVKKLSR---PFQSIihAKRTYRELRLLKHMKHENVIGLLDVFTPARSleefnDVYLVT 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELaVQGDLLELIKTRgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMA 170
Cdd:cd07877 102 HL-MGADLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVA 179
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 171 lsktfcgSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS--MPYDD--SNIKKMLRI 227
Cdd:cd07877 180 -------TRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRtlFPGTDhiDQLKLILRL 233
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
14-269 5.32e-19

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: 85.46  E-value: 5.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSERLKFNVAIKII----DRKKAPADFleKFLPREIEILAMLNHCSIIKTYEIF-ETSHGKVYI 88
Cdd:cd06653   6 LGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpDSQETSKEV--NALECEIQLLKNLRHDRIVQYYGCLrDPEEKKLSI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR----CLrd 164
Cdd:cd06653  84 FVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRiqtiCM-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 165 dSGRMALSKTfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddSNIKKMLRIQK-EHRVNFPR-SKHLT 242
Cdd:cd06653 162 -SGTGIKSVT--GTPYWMSPEVISGEGYGRKA-DVWSVACTVVEMLTEKPPW--AEYEAMAAIFKiATQPTKPQlPDGVS 235
                       250       260
                ....*....|....*....|....*..
gi 14042947 243 GECKDLIYHMLQPDvNRRLHIDEILSH 269
Cdd:cd06653 236 DACRDFLRQIFVEE-KRRPTAEFLLRH 261
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
18-274 5.34e-19

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: 86.88  E-value: 5.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETS---HG--KVYIVMEL 92
Cdd:cd07879  23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAY-RELTLLKHMQHENVIGLLDVFTSAvsgDEfqDFYLVMPY 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLeliKTRGA-LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGrmal 171
Cdd:cd07879 102 -MQTDLQ---KIMGHpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEMTG---- 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 sktFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS--------------------MPYDD-----------SN 220
Cdd:cd07879 174 ---YVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKtlfkgkdyldqltqilkvtgVPGPEfvqkledkaakSY 250
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 221 IKKMLRI-QKEHRVNFPRSkhlTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQP 274
Cdd:cd07879 251 IKSLPKYpRKDFSTLFPKA---SPQAVDLLEKMLELDVDKRLTATEALEHPYFDS 302
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
18-272 5.39e-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: 85.94  E-value: 5.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIF-ETSHGKVYIVMELAVQG 96
Cdd:cd06621   9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPNPD--VQKQILRELEINKSCASPYIVKYYGAFlDEQDSSIGIAMEYCEGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLEL---IKTRGALHEDEARKKFHQLSL-AIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRddsgrmALS 172
Cdd:cd06621  87 SLDSIykkVKKKGGRIGEKVLGKIAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVN------SLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQ-KEHRVNFPRSK---------HLT 242
Cdd:cd06621 161 GTFTGTSYYMAPERIQGGPYSITS-DVWSLGLTLLEVAQNRFPFPPEGEPPLGPIElLSYIVNMPNPElkdepengiKWS 239
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06621 240 ESFKDFIEKCLEKDGTRRPGPWQMLAHPWI 269
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
18-269 5.56e-19

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: 86.20  E-value: 5.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDrkkaPADFLEKFLPREIEILAML-NHCSIIKTYEIF----ETSHGKVYIVMEL 92
Cdd:cd06639  30 IGKGTYGKVYKVTNKKDGSLAAVKILD----PISDVDEEIEAEYNILRSLpNHPNVVKFYGMFykadQYVGGQLWLVLEL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKT--RGALHEDEARKKF--HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrdDSGR 168
Cdd:cd06639 106 CNGGSVTELVKGllKCGQRLDEAMISYilYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL---TSAR 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MAlSKTFCGSPAYAAPEVL---QGIPYQPKVY-DIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKE------HRVNFPR 237
Cdd:cd06639 183 LR-RNTSVGTPFWMAPEVIaceQQYDYSYDARcDVWSLGITAIELADGDPPLFDMHpVKALFKIPRNppptllNPEKWCR 261
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 238 S-KHLTGECkdliyhmLQPDVNRRLHIDEILSH 269
Cdd:cd06639 262 GfSHFISQC-------LIKDFEKRPSVTHLLEH 287
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
6-284 7.57e-19

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: 86.64  E-value: 7.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRGYLLGInlGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETSHG- 84
Cdd:cd07875  22 VLKRYQNLKPI--GSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAY-RELVLMKCVNHKNIIGLLNVFTPQKSl 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 ----KVYIVMELaVQGDLLELIKTRgaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKr 160
Cdd:cd07875  99 eefqDVYIVMEL-MDANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 clrdDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-------------------I 221
Cdd:cd07875 175 ----TAGTSFMMTPYVVTRYYRAPEVILGMGYKENV-DIWSVGCIMGEMIKGGVLFPGTDhidqwnkvieqlgtpcpefM 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 222 KKM---LRIQKEHR--------------VNFP----RSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH----CWMQPKA 276
Cdd:cd07875 250 KKLqptVRTYVENRpkyagysfeklfpdVLFPadseHNKLKASQARDLLSKMLVIDASKRISVDEALQHpyinVWYDPSE 329

                ....*...
gi 14042947 277 RGSPSVAI 284
Cdd:cd07875 330 AEAPPPKI 337
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
17-269 9.72e-19

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 85.17  E-value: 9.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNV-AIKIIDRKKAPADFLEKFLpREIEILAML---NHCSIIKTYEIFEtSHGKVYIVMEL 92
Cdd:cd14052   7 LIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRL-EEVSILRELtldGHDNIVQLIDSWE-YHGHLYIQTEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDL---LELIKTRGALheDEAR--KKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClRDDSG 167
Cdd:cd14052  85 CENGSLdvfLSELGLLGRL--DEFRvwKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVW-PLIRG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMALsktfcGSPAYAAPEVLQGIPYQpKVYDIWSLGVILY-IMVCGSMP-------------YDDSNIKKMLRIQKEHRV 233
Cdd:cd14052 162 IERE-----GDREYIAPEILSEHMYD-KPADIFSLGLILLeAAANVVLPdngdawqklrsgdLSDAPRLSSTDLHSASSP 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 14042947 234 N------FPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14052 236 SsnpppdPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLAT 277
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
18-271 1.10e-18

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: 85.06  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV---KSAYSERLKFNVAIKIIDRKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHGkVYIVMELaV 94
Cdd:cd07871  13 LGEGTYATVfkgRSKLTENLVALKEIRLEHEEGAPCTAI-----REVSLLKNLKHANIVTLHDIIHTERC-LTLVFEY-L 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrddsGRMALSK 173
Cdd:cd07871  86 DSDLKQYLDNCGNLMSMHNVKIFmFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLAR-------AKSVPTK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRI------------------QKEHR 232
Cdd:cd07871 159 TYSNEVVtlwYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLifrllgtpteetwpgvtsNEEFR 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 233 V-NFPRSK---------HLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07871 239 SyLFPQYRaqplinhapRLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
18-269 1.24e-18

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 85.06  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDrkkaPADFLEKFLPREIEIL-AMLNHCSIIKTYEIF---ETSHG-KVYIVMEL 92
Cdd:cd06638  26 IGKGTYGKVFKVLNKKNGSKAAVKILD----PIHDIDEEIEAEYNILkALSDHPNVVKFYGMYykkDVKNGdQLWLVLEL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKtrGALHEDEARKK------FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDS 166
Cdd:cd06638 102 CNGGSVTDLVK--GFLKRGERMEEpiiayiLHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRmalsKTFCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPYDDSN-IKKMLRIQKEHRVNFPRSKHL 241
Cdd:cd06638 180 RR----NTSVGTPFWMAPEVIACEQQLDSTYdarcDVWSLGITAIELGDGDPPLADLHpMRALFKIPRNPPPTLHQPELW 255
                       250       260
                ....*....|....*....|....*...
gi 14042947 242 TGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd06638 256 SNEFNDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
9-273 1.30e-18

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: 84.75  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGinlgEGSYAKVKSAYSERLKFNVAIKIID-RKKAPADFLE-KFLPREIEILAMLNHCSIIKTYEIFEtSHGK- 85
Cdd:cd06651  10 RRGKLLG----QGAFGRVYLCYDVDTGRELAAKQVQfDPESPETSKEvSALECEIQLLKNLQHERIVQYYGCLR-DRAEk 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 -VYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR---- 160
Cdd:cd06651  85 tLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqti 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 CLrddSGRMALSKTfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKH 240
Cdd:cd06651 165 CM---SGTGIRSVT--GTPYWMSPEVISGEGYGRKA-DVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 241 LTGECKDLIYHMLQpDVNRRLHIDEILSHCWMQ 273
Cdd:cd06651 239 ISEHARDFLGCIFV-EARHRPSAEELLRHPFAQ 270
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
18-269 1.39e-18

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: 84.63  E-value: 1.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidRKKAPADFLEKFLP-REIEILAMLN-HCSIIKTYEI-FETSHGKVYIVMELaV 94
Cdd:cd07831   7 IGEGTFSEVLKAQSRKTGKYYAIK---CMKKHFKSLEQVNNlREIQALRRLSpHPNILRLIEVlFDRKTGRLALVFEL-M 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDfNIKLSDFSfskrclrddSGRMALSK 173
Cdd:cd07831  83 DMNLYELIKGRkRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG---------SCRGIYSK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 ----TFCGSPAYAAPE-VLQGIPYQPKVyDIWSLGVILYIMVC------GSMPYD------------DSNIKKMLRIQKE 230
Cdd:cd07831 153 ppytEYISTRWYRAPEcLLTDGYYGPKM-DIWAVGCVFFEILSlfplfpGTNELDqiakihdvlgtpDAEVLKKFRKSRH 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 231 HRVNFPRSK---------HLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07831 232 MNYNFPSKKgtglrkllpNASAEGLDLLKKLLAYDPDERITAKQALRH 279
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
14-229 1.49e-18

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: 84.78  E-value: 1.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGInLGEGSYAKV-KSAYSERLKFnVAIKIIdRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMEL 92
Cdd:cd07846   6 LGL-VGEGSYGMVmKCRHKETGQI-VAIKKF-LESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKK-RWYLVFEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrclRDDSGRMALS 172
Cdd:cd07846  82 VDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA----RTLAAPGEVY 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSmPY--DDSNIKKMLRIQK 229
Cdd:cd07846 158 TDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGE-PLfpGDSDIDQLYHIIK 215
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
12-285 1.73e-18

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: 85.11  E-value: 1.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD----FLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVY 87
Cdd:cd14041   8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDekkeNYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDF---NIKLSDFSFSKRCL 162
Cdd:cd14041  88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTacgEIKITDFGLSKIMD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 RDDSGR---MALSKTFCGSPAYAAPEVLQGIPYQPKV---YDIWSLGVILYIMVCGSMPY----DDSNIKKMLRIQKEHR 232
Cdd:cd14041 168 DDSYNSvdgMELTSQGAGTYWYLPPECFVVGKEPPKIsnkVDVWSVGVIFYQCLYGRKPFghnqSQQDILQENTILKATE 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 14042947 233 VNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAIN 285
Cdd:cd14041 248 VQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSP 300
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
18-212 2.05e-18

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: 84.35  E-value: 2.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFN---VAIK-IIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd07847   9 IGEGSYGVV---FKCRNRETgqiVAIKkFVESEDDPV--IKKIALREIRMLKQLKHPNLVNLIEVFRRKR-KLHLVFEYC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLrddSGRMALSK 173
Cdd:cd07847  83 DHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFA-RIL---TGPGDDYT 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQG-IPYQPKVyDIWSLGVILYIMVCG 212
Cdd:cd07847 159 DYVATRWYRAPELLVGdTQYGPPV-DVWAIGCVFAELLTG 197
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
6-298 2.11e-18

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: 85.47  E-value: 2.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRGYLLGInlGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETSHG- 84
Cdd:cd07876  19 VLKRYQQLKPI--GSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAY-RELVLLKCVNHKNIISLLNVFTPQKSl 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 ----KVYIVMELaVQGDLLELIKTRgaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKr 160
Cdd:cd07876  96 eefqDVYLVMEL-MDANLCQVIHME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 clrddsgrmALSKTFCGSP-----AYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN--------------- 220
Cdd:cd07876 172 ---------TACTNFMMTPyvvtrYYRAPEVILGMGYKENV-DIWSVGCIMGELVKGSVIFQGTDhidqwnkvieqlgtp 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 221 -IKKMLRIQK------EHRVNFP------------------RSKHLTGECKDLIYHMLQPDVNRRLHIDEILSH----CW 271
Cdd:cd07876 242 sAEFMNRLQPtvrnyvENRPQYPgisfeelfpdwifpseseRDKLKTSQARDLLSKMLVIDPDKRISVDEALRHpyitVW 321
                       330       340
                ....*....|....*....|....*...
gi 14042947 272 MQP-KARGSPSVAINKEGESSRGTEPLW 298
Cdd:cd07876 322 YDPaEAEAPPPQIYDAQLEEREHAIEEW 349
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
18-277 2.15e-18

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: 83.97  E-value: 2.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06641  12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIED--IQQEITVLSQCDSPYVTKYYGSY-LKDTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTrGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCG 177
Cdd:cd06641  89 ALDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKR----N*FVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 178 SPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGeCKDLIYHMLQPDV 257
Cdd:cd06641 164 TPFWMAPEVIKQSAYDSKA-DIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKP-LKEFVEACLNKEP 241
                       250       260
                ....*....|....*....|
gi 14042947 258 NRRLHIDEILSHCWMQPKAR 277
Cdd:cd06641 242 SFRPTAKELLKHKFILRNAK 261
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-254 2.62e-18

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: 83.55  E-value: 2.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLK---FNVAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKtyeIFETSHGKVYI-VMELA 93
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKSgkeVEVAVKTLKQEHEKAG--KKEFLREASVMAQLDHPCIVR---LIGVCKGEPLMlVMELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDS------- 166
Cdd:cd05060  78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMS-RALGAGSdyyratt 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 -GRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC-GSMPYDD-SNIKKMLRIQKEHRVNFPRskhltg 243
Cdd:cd05060 157 aGRWPLK--------WYAPECINYGKFSSKS-DVWSYGVTLWEAFSyGAKPYGEmKGPEVIAMLESGERLPRPE------ 221
                       250
                ....*....|.
gi 14042947 244 ECKDLIYHMLQ 254
Cdd:cd05060 222 ECPQEIYSIML 232
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
59-273 3.59e-18

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: 83.58  E-value: 3.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKT---YEIFETShgkVYIVMEL-AVQGDLLeLIKTRGALHEDEARKkfhqLSLAI-KYCHDL--- 130
Cdd:cd06618  62 MDLDVVLKSHDCPYIVKcygYFITDSD---VFICMELmSTCLDKL-LKRIQGPIPEDILGK----MTVSIvKALHYLkek 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 131 -DVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrdDSgrMALSKTfCGSPAYAAPEVLQgIPYQPKvYDI----WSLGVI 205
Cdd:cd06618 134 hGVIHRDVKPSNILLDESGNVKLCDFGISGRLV--DS--KAKTRS-AGCAAYMAPERID-PPDNPK-YDIradvWSLGIS 206
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 206 LYIMVCGSMPYD--DSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd06618 207 LVELATGQFPYRncKTEFEVLTKILNEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
15-279 3.70e-18

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: 83.06  E-value: 3.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  15 GINLGEGSYAKVksaYSERLKFN---VAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETSHgKVYIVME 91
Cdd:cd05084   1 GERIGRGNFGEV---FSGRLRADntpVAVKSC-RETLPPDLKAKFL-QEARILKQYSHPNIVRLIGVCTQKQ-PIYIVME 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGA-LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclRDDSGRMA 170
Cdd:cd05084  75 LVQGGDFLTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR---EEEDGVYA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTFCGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRskhltgECKD 247
Cdd:cd05084 152 ATGGMKQIPVkWTAPEALNYGRYSSES-DVWSFGILLWeTFSLGAVPYANlSNQQTREAVEQGVRLPCPE------NCPD 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 14042947 248 LIYHMLQpdvnrrlhideilsHCW-MQPKARGS 279
Cdd:cd05084 225 EVYRLME--------------QCWeYDPRKRPS 243
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-268 4.75e-18

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 83.54  E-value: 4.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELI----KTRGALHEDEARKKFHQLSLAIKYCHDLDVVH 134
Cdd:cd08229  73 KEIDLLKQLNHPNVIKYYASF-IEDNELNIVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMH 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 135 RDLKCDNLLLDKDFNIKLSDFSFSkrclRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSM 214
Cdd:cd08229 152 RDIKPANVFITATGVVKLGDLGLG----RFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKS-DIWSLGCLLYEMAALQS 226
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 215 PYDDSNIKKMLRIQKEHRVNFP--RSKHLTGECKDLIYHMLQPDVNRRLHIDEILS 268
Cdd:cd08229 227 PFYGDKMNLYSLCKKIEQCDYPplPSDHYSEELRQLVNMCINPDPEKRPDITYVYD 282
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
18-204 5.28e-18

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: 82.50  E-value: 5.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADflEKF--LPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME--LA 93
Cdd:cd06607   9 IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQST--EKWqdIIKEVKFLRQLRHPNTIEYKGCYLREH-TAWLVMEycLG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTrgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF-SFSKRClrddsgrmaLS 172
Cdd:cd06607  86 SASDIVEVHKK--PLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFgSASLVC---------PA 154
                       170       180       190
                ....*....|....*....|....*....|....*
gi 14042947 173 KTFCGSPAYAAPEVLQGI---PYQPKVyDIWSLGV 204
Cdd:cd06607 155 NSFVGTPYWMAPEVILAMdegQYDGKV-DVWSLGI 188
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
18-274 8.89e-18

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: 83.01  E-value: 8.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK-IIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELaVQG 96
Cdd:cd07856  18 VGMGAFGLVCSARDQLTGQNVAVKkIMKPFSTPV--LAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTEL-LGT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLRDDSGRMALSKTFc 176
Cdd:cd07856  95 DLHRLLTSR-PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR--IQDPQMTGYVSTRY- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 gspaYAAPEV-LQGIPYQPKVyDIWSLGVILYIMVCGS--MPYDD-----SNIKKML---------RIQKEHRVNFPRS- 238
Cdd:cd07856 171 ----YRAPEImLTWQKYDVEV-DIWSAGCIFAEMLEGKplFPGKDhvnqfSIITELLgtppddvinTICSENTLRFVQSl 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 239 ------------KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQP 274
Cdd:cd07856 246 pkrervpfsekfKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAP 293
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
18-284 9.14e-18

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: 81.92  E-value: 9.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERlKFNVAIKIIdRKKAPA--DFLEkflprEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQ 95
Cdd:cd05112  12 IGSGQFGLVHLGYWLN-KDKVAIKTI-REGAMSeeDFIE-----EAEVMMKLSHPKLVQLYGVC-LEQAPICLVFEFMEH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKT-RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrmaLSKT 174
Cdd:cd05112  84 GCLSDYLRTqRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQY----TSST 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRskhltgeckdliyh 251
Cdd:cd05112 160 GTKFPVkWSSPEVFSFSRYSSKS-DVWSFGVLMWeVFSEGKIPYENrSNSEVVEDINAGFRLYKPR-------------- 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 252 mLQPDvnrrlHIDEILSHCW-MQPKARgsPSVAI 284
Cdd:cd05112 225 -LAST-----HVYEIMNHCWkERPEDR--PSFSL 250
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
60-249 9.70e-18

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: 83.52  E-value: 9.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKC 139
Cdd:cd05626  51 ERDILAEADNEWVVKLYYSFQDKD-NLYFVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKP 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 140 DNLLLDKDFNIKLSDFSF---------SK-----RCLRDDS-----------------------------GRMALSKTFC 176
Cdd:cd05626 130 DNILIDLDGHIKLTDFGLctgfrwthnSKyyqkgSHIRQDSmepsdlwddvsncrcgdrlktleqratkqHQRCLAHSLV 209
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 177 GSPAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLR-IQKEHRVNFPRSKHLTGECKDLI 249
Cdd:cd05626 210 GTPNYIAPEVLLRKGYT-QLCDWWSVGVILFEMLVGQPPFlAPTPTETQLKvINWENTLHIPPQVKLSPEAVDLI 283
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
18-269 1.09e-17

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: 82.08  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELaVQGD 97
Cdd:cd07861   8 IGEGTYGVVYKGRNKKTGQIVAMKKI-RLESEEEGVPSTAIREISLLKELQHPNIVCLEDVL-MQENRLYLVFEF-LSMD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 L---LELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsgrmALSKT 174
Cdd:cd07861  85 LkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADF--------------GLARA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FcGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS-MPYDDSNIKKMLRI--------------- 227
Cdd:cd07861 151 F-GIPVrvythevvtlwYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKpLFHGDSEIDQLFRIfrilgtptediwpgv 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 14042947 228 --QKEHRVNFPR---------SKHLTGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd07861 230 tsLPDYKNTFPKwkkgslrtaVKNLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
58-218 1.27e-17

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: 81.41  E-value: 1.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  58 PREIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDL 137
Cdd:cd14111  47 LQEYEILKSLHHERIMALHEAYITPRYLV-LIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDI 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 138 KCDNLLLDKDFNIKLSDF----SFSKRCLRDDSGRMalsktfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGS 213
Cdd:cd14111 126 KPDNIMVTNLNAIKIVDFgsaqSFNPLSLRQLGRRT-------GTLEYMAPEMVKGEPVGPPA-DIWSIGVLTYIMLSGR 197

                ....*
gi 14042947 214 MPYDD 218
Cdd:cd14111 198 SPFED 202
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-206 2.06e-17

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: 81.40  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFN---VAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIF-ETSHGKVYIVMELA 93
Cdd:cd14049  14 LGKGGYGKV---YKVRNKLDgqyYAIKKILIKKVTKRDCMKVL-REVKVLAGLQHPNIVGYHTAWmEHVQLMLYIQMQLC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 vQGDLLELIKTR--------------GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFSFS 158
Cdd:cd14049  90 -ELSLWDWIVERnkrpceeefksapyTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLA 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 159 -KRCLRD--DSGRMALSKTF-----CGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14049 169 cPDILQDgnDSTTMSRLNGLthtsgVGTCLYAAPEQLEGSHYDFKS-DMYSIGVIL 223
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
18-273 2.22e-17

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: 82.48  E-value: 2.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidrkKAPADFLE----KFLPREIEILAMLNHCSIIKTYEIFETSH----GKVYIV 89
Cdd:cd07853   8 IGYGAFGVVWSVTDPRDGKRVALK-----KMPNVFQNlvscKRVFRELKMLCFFKHDNVLSALDILQPPHidpfEEIYVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELaVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRM 169
Cdd:cd07853  83 TEL-MQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHM 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTfcgSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCG-------------SMPYD---DSNIKKMLRIQKEHRV 233
Cdd:cd07853 162 TQEVV---TQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRrilfqaqspiqqlDLITDllgTPSLEAMRSACEGARA 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 14042947 234 NFPRSKH--------------LTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd07853 239 HILRGPHkppslpvlytlssqATHEAVHLLCRMLVFDPDKRISAADALAHPYLD 292
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
18-213 4.08e-17

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 80.00  E-value: 4.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSErlKFNVAIKIIDRKKApadflEKFLPREIEILAMLNHCSIIktYEIFETSHGKVyIVMELAVQGD 97
Cdd:cd14068   2 LGDGGFGSVYRAVYR--GEDVAVKIFNKHTS-----FRLLRQELVVLSHLHHPSLV--ALLAAGTAPRM-LVMELAPKGS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELiktrgaLHEDEA---RKKFHQLSL----AIKYCHDLDVVHRDLKCDNLLL-----DKDFNIKLSDFSFSKRCLRdd 165
Cdd:cd14068  72 LDAL------LQQDNAsltRTLQHRIALhvadGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCR-- 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 166 sgrMALsKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILY-IMVCGS 213
Cdd:cd14068 144 ---MGI-KTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYdILTCGE 188
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
7-279 4.69e-17

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: 80.03  E-value: 4.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYSERLKfnVAIKIIDRKKAPADFLEkflprEIEILAMLNHCSIIKTYEIFETSHGKV 86
Cdd:cd05082   3 LNMKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCIKNDATAQAFLA-----EASVMTQLRHSNLVQLLGVIVEEKGGL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELIKTRG-ALHEDEARKKFH-QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLR- 163
Cdd:cd05082  76 YIVTEYMAKGSLVDYLRSRGrSVLGGDCLLKFSlDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGRMALSKTfcgspayaAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKML-RIQKEHRVNFPRSkhl 241
Cdd:cd05082 156 QDTGKLPVKWT--------APEALREKKFSTKS-DVWSFGILLWeIYSFGRVPYPRIPLKDVVpRVEKGYKMDAPDG--- 223
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 14042947 242 tgeCKDLIYhmlqpdvnrrlhidEILSHCW-MQPKARGS 279
Cdd:cd05082 224 ---CPPAVY--------------DVMKNCWhLDAAMRPS 245
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
18-205 4.80e-17

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: 81.14  E-value: 4.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPADFLEKFLprEIEILAMLN-------HCSIIKTYEIFeTSHGKVYIVM 90
Cdd:cd14212   7 LGQGTFGQVVKCQDLKTNKLVAVKVL--KNKPAYFRQAML--EIAILTLLNtkydpedKHHIVRLLDHF-MHHGHLCIVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQgDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD--FNIKLSDFS---FSKRCLR 163
Cdd:cd14212  82 ELLGV-NLYELLKQNQfrGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGsacFENYTLY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 14042947 164 ddsgrmalskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVI 205
Cdd:cd14212 161 ----------TYIQSRFYRSPEVLLGLPYSTAI-DMWSLGCI 191
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
19-268 4.95e-17

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 79.62  E-value: 4.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVKSAYSERLKFNVAIKIIDRkkapadflekfLPREIEILAMLNHCSIIKTY-EIFETSHgkVYIVMELAVQGD 97
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK-----------IEKEAEILSVLSHRNIIQFYgAILEAPN--YGIVTEYASYGS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGA--LHEDEARKKFHQLSLAIKYCHD---LDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLRDDSGRMALS 172
Cdd:cd14060  69 LFDYLNSNESeeMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTTHMSLV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFcgspAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKM--LRIQKEHRVNFPRSkhLTGECKDLIY 250
Cdd:cd14060 147 GTF----PWMAPEVIQSLPVS-ETCDTYSYGVVLWEMLTREVPFKGLEGLQVawLVVEKNERPTIPSS--CPRSFAELMR 219
                       250
                ....*....|....*...
gi 14042947 251 HMLQPDVNRRLHIDEILS 268
Cdd:cd14060 220 RCWEADVKERPSFKQIIG 237
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
18-273 5.20e-17

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 80.43  E-value: 5.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV---KSAYSERLKFNVAIKIIDRKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaV 94
Cdd:cd07873  10 LGEGTYATVykgRSKLTDNLVALKEIRLEHEEGAPCTAI-----REVSLLKDLKHANIVTLHDIIHTEK-SLTLVFEY-L 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRG-ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrddsGRMALSK 173
Cdd:cd07873  83 DKDLKQYLDDCGnSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR-------AKSIPTK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRI------------------QKEHR 232
Cdd:cd07873 156 TYSNEVVtlwYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFifrilgtpteetwpgilsNEEFK 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 233 V-NFPR---------SKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd07873 236 SyNYPKyradalhnhAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFH 286
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
12-281 6.10e-17

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: 80.49  E-value: 6.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAD----FLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVY 87
Cdd:cd14040   8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDekkeNYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDF---NIKLSDFSFSKrCL 162
Cdd:cd14040  88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSK-IM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 RDDS---GRMALSKTFCGSPAYAAPEVLQGIPYQPKV---YDIWSLGVILYIMVCGSMPY----DDSNIKKMLRIQKEHR 232
Cdd:cd14040 167 DDDSygvDGMDLTSQGAGTYWYLPPECFVVGKEPPKIsnkVDVWSVGVIFFQCLYGRKPFghnqSQQDILQENTILKATE 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 233 VNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPS 281
Cdd:cd14040 247 VQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSNS 295
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
6-284 6.22e-17

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: 80.90  E-value: 6.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRGYLLGInlGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETSHG- 84
Cdd:cd07874  15 VLKRYQNLKPI--GSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAY-RELVLMKCVNHKNIISLLNVFTPQKSl 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 ----KVYIVMELaVQGDLLELIKTRgaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKr 160
Cdd:cd07874  92 eefqDVYLVMEL-MDANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 clrdDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY------DDSN-------------I 221
Cdd:cd07874 168 ----TAGTSFMMTPYVVTRYYRAPEVILGMGYKENV-DIWSVGCIMGEMVRHKILFpgrdyiDQWNkvieqlgtpcpefM 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 222 KKMLRIQKEHRVNFPRSKHLT---------------------GECKDLIYHMLQPDVNRRLHIDEILSH----CWMQPKA 276
Cdd:cd07874 243 KKLQPTVRNYVENRPKYAGLTfpklfpdslfpadsehnklkaSQARDLLSKMLVIDPAKRISVDEALQHpyinVWYDPAE 322

                ....*...
gi 14042947 277 RGSPSVAI 284
Cdd:cd07874 323 VEAPPPQI 330
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
18-216 7.21e-17

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 79.48  E-value: 7.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDrkkapadfLEKFLPREIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQGD 97
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVR--------LEVFRAEELMACAGLTSPRVVPLYGAVREG-PWVNIFMDLKEGGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKD-FNIKLSDFSFSKrCLRDD--SGRMALSKT 174
Cdd:cd13991  85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAE-CLDPDglGKSLFTGDY 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 14042947 175 FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd13991 164 IPGTETHMAPEVVLGKPCDAKV-DVWSSCCMMLHMLNGCHPW 204
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
18-206 7.29e-17

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: 80.53  E-value: 7.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIidrKKAPADFLEKFLP----REIEILAML-NHCSIIKTYE---IFETSHGKVYIV 89
Cdd:cd07857   8 LGQGAYGIVCSARNAETSEEETVAI---KKITNVFSKKILAkralRELKLLRHFrGHKNITCLYDmdiVFPGNFNELYLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELaVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRM 169
Cdd:cd07857  85 EEL-MEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSENPGENA 163
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 14042947 170 ALSKTFCGSPAYAAPEVLqgIPYQP--KVYDIWSLGVIL 206
Cdd:cd07857 164 GFMTEYVATRWYRAPEIM--LSFQSytKAIDVWSVGCIL 200
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
7-253 8.49e-17

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: 79.40  E-value: 8.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSA-YSERLKfnVAIKIIdrKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGK 85
Cdd:cd05148   3 RPREEFTLERKLGSGYFGEVWEGlWKNRVR--VAIKIL--KSDDLLKQQDFQ-KEVQALKRLRHKHLISLFAVC-SVGEP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELIKTRgalhEDEARKKFHQLSLA------IKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSk 159
Cdd:cd05148  77 VYIITELMEKGSLLAFLRSP----EGQVLPVASLIDMAcqvaegMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLA- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 160 RCLRDDSGRMALSKTfcgsP-AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKML-RIQKEHRVNFP 236
Cdd:cd05148 152 RLIKEDVYLSSDKKI----PyKWTAPEAASHGTFSTKS-DVWSFGILLYeMFTYGQVPYPGMNNHEVYdQITAGYRMPCP 226
                       250
                ....*....|....*..
gi 14042947 237 rskhltGECKDLIYHML 253
Cdd:cd05148 227 ------AKCPQEIYKIM 237
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
14-279 1.50e-16

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: 78.38  E-value: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAysERLKFNVAIKIIDRKKAPADFLEkflprEIEILAMLNHCSIIKTYEIFetSHGKVYIVMELA 93
Cdd:cd05083  10 LGEIIGEGEFGAVLQG--EYMGQKVAVKNIKCDVTAQAFLE-----ETAVMTKLQHKNLVRLLGVI--LHNGLYIVMELM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLA--IKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLR-DDSGRMA 170
Cdd:cd05083  81 SKGNLVNFLRSRGRALVPVIQLLQFSLDVAegMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMgVDNSRLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 LSKTfcgspayaAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLR-IQKEHRVNFPRskhltgECKDL 248
Cdd:cd05083 161 VKWT--------APEALKNKKFSSKS-DVWSYGVLLWeVFSYGRAPYPKMSVKEVKEaVEKGYRMEPPE------GCPPD 225
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 249 IYhmlqpdvnrrlhidEILSHCW-MQPKARGS 279
Cdd:cd05083 226 VY--------------SIMTSCWeAEPGKRPS 243
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
14-289 1.83e-16

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: 78.85  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYSERLK-----FNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFeTSHGKVYI 88
Cdd:cd05045   4 LGKTLGEGEFGKVVKATAFRLKgragyTTVAVKMLKENASSSELRD--LLSEFNLLKQVNHPHVIKLYGAC-SQDGPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTR-----GALHEDEARKK---FH----------------QLSLAIKYCHDLDVVHRDLKCDNLLL 144
Cdd:cd05045  81 IVEYAKYGSLRSFLRESrkvgpSYLGSDGNRNSsylDNpderaltmgdlisfawQISRGMQYLAEMKLVHRDLAARNVLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 145 DKDFNIKLSDFSFSKRCLRDDS------GRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYD 217
Cdd:cd05045 161 AEGRKMKISDFGLSRDVYEEDSyvkrskGRIPVK--------WMAIESLFDHIYTTQS-DVWSFGVLLWeIVTLGGNPYP 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 218 DSNIKKMLRIQKE-HRVNFPRSkhltgeCKDLIYhmlqpdvnrrlhidEILSHCWMQpKARGSPSVA-INKEGE 289
Cdd:cd05045 232 GIAPERLFNLLKTgYRMERPEN------CSEEMY--------------NLMLTCWKQ-EPDKRPTFAdISKELE 284
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
18-216 2.47e-16

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: 77.70  E-value: 2.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFN--VAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETShgKVYIVMELAVQ 95
Cdd:cd05116   3 LGSGNFGTVKKGYYQMKKVVktVAVKILKNEANDPALKDELL-REANVMQQLDNPYIVRMIGICEAE--SWMLVMEMAEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAlsKTF 175
Cdd:cd05116  80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKA--QTH 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14042947 176 CGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPY 216
Cdd:cd05116 158 GKWPVkWYAPECMNYYKFSSKS-DVWSFGVLMWeAFSYGQKPY 199
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
18-268 3.05e-16

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: 77.80  E-value: 3.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFN------VAIKIID---RKKAPADFLekflpREIEILAMLNHCSIIKTYEIFeTSHGKVYI 88
Cdd:cd05033  12 IGGGEFGEV---CSGSLKLPgkkeidVAIKTLKsgySDKQRLDFL-----TEASIMGQFDHPNVIRLEGVV-TKSRPVMI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSG 167
Cdd:cd05033  83 VTEYMENGSLDKfLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRR-LEDSEA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMalsKTFCG-SPA-YAAPEVLQGIPYQPkVYDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRskhltg 243
Cdd:cd05033 162 TY---TTKGGkIPIrWTAPEAIAYRKFTS-ASDVWSFGIVMWeVMSYGERPYWDmSNQDVIKAVEDGYRLPPPM------ 231
                       250       260
                ....*....|....*....|....*....
gi 14042947 244 ECKDLIYH-ML---QPDVNRRLHIDEILS 268
Cdd:cd05033 232 DCPSALYQlMLdcwQKDRNERPTFSQIVS 260
pknD PRK13184
serine/threonine-protein kinase PknD;
18-236 3.43e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 80.20  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaVQGD 97
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGD-PVYYTMPY-IEGY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   98 LLE-LIKT-------RGALHEDEARKK----FHQLSLAIKYCHDLDVVHRDLKCDNLLLDK-------DFNIKLS----- 153
Cdd:PRK13184  88 TLKsLLKSvwqkeslSKELAEKTSVGAflsiFHKICATIEYVHSKGVLHRDLKPDNILLGLfgevvilDWGAAIFkklee 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  154 ----DFSFSKRCLRddSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDsniKKMLRIQK 229
Cdd:PRK13184 168 edllDIDVDERNIC--YSSMTIPGKIVGTPDYMAPERLLGVPASEST-DIYALGVILYQMLTLSFPYRR---KKGRKISY 241

                 ....*..
gi 14042947  230 EHRVNFP 236
Cdd:PRK13184 242 RDVILSP 248
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
18-254 4.39e-16

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: 76.97  E-value: 4.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAySERLKFNVAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd05085   4 LGKGNFGEVYKG-TLKDKTPVAVKTC-KEDLPQELKIKFL-SEARILKQYDHPNIVKLIGVC-TQRQPIYIVMELVPGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRgalhEDEAR-KKFHQLSL----AIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclRDDSGRMALS 172
Cdd:cd05085  80 FLSFLRKK----KDELKtKQLVKFSLdaaaGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR---QEDDGVYSSS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRskhltgECKDLIY 250
Cdd:cd05085 153 GLKQIPIKWTAPEALNYGRYSSES-DVWSFGILLWeTFSLGVCPYPGmTNQQAREQVEKGYRMSAPQ------RCPEDIY 225

                ....
gi 14042947 251 HMLQ 254
Cdd:cd05085 226 KIMQ 229
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
18-267 5.67e-16

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: 77.16  E-value: 5.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidRKKAPADFLEKFLPREIEILAMLN-HCSIIKTY-------EIFETSHGKVYIV 89
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALK---RLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCsaasigkEESDQGQAEYLLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAvQGDLLELIKT---RGALHEDEARKKFHQLSLAIKYCH--DLDVVHRDLKCDNLLLDKDFNIKLSDF-SFSKRCLR 163
Cdd:cd14036  85 TELC-KGQLVDFVKKveaPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLCDFgSATTEAHY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGRMALSKTFC-------GSPAYAAPEVL---QGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSnikKMLRIqkehrV 233
Cdd:cd14036 164 PDYSWSAQKRSLVedeitrnTTPMYRTPEMIdlySNYPIGEKQ-DIWALGCILYLLCFRKHPFEDG---AKLRI-----I 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 14042947 234 N----FPRSKHLTGECKDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd14036 235 NakytIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-300 5.88e-16

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 77.31  E-value: 5.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLprEIEILAMLNHCSIIKTYEIFE-----TSHGKVYIVMEL 92
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCL--EIQIMKRLNHPNVVAARDVPEglqklAPNDLPLLAMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDL---LELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRClrdDS 166
Cdd:cd14038  80 CQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqgEQRLIHKIIDLGYAKEL---DQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY--DDSNIKKMLRIQKEHRVNFPRSKHLTGE 244
Cdd:cd14038 157 G--SLCTSFVGTLQYLAPELLEQQKYTVTV-DYWSFGTLAFECITGFRPFlpNWQPVQWHGKVRQKSNEDIVVYEDLTGA 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 245 CKdliYHMLQPDVNrrlHIDEILS---HCWMQPKARGSPsvainkegeSSRGTEPLWTP 300
Cdd:cd14038 234 VK---FSSVLPTPN---NLNGILAgklERWLQCMLMWHP---------RQRGTDPPQNP 277
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
18-281 5.90e-16

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: 77.00  E-value: 5.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYserlkFNVAIKIIDRKKAPADF-LEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQG 96
Cdd:cd05072  15 LGAGQFGEVWMGY-----YNNSTKVAVKTLKPGTMsVQAFL-EEANLMKTLQHDKLVRLYAVV-TKEEPIYIITEYMAKG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTrgalheDEARKKF--------HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGR 168
Cdd:cd05072  88 SLLDFLKS------DEGGKVLlpklidfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLA-RVIEDNEYT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVnfPRSKHltgeCK 246
Cdd:cd05072 161 AREGAKF--PIKWTAPEAINFGSFTIKS-DVWSFGILLYeIVTYGKIPYPGmSNSDVMSALQRGYRM--PRMEN----CP 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 14042947 247 DLIYhmlqpdvnrrlhidEILSHCWmQPKARGSPS 281
Cdd:cd05072 232 DELY--------------DIMKTCW-KEKAEERPT 251
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
39-261 6.49e-16

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: 77.09  E-value: 6.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  39 AIKIIDRKKAPADFLEKFLPREIEILAMLNHCS----IIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEAR 114
Cdd:cd05606  23 AMKCLDKKRIKMKQGETLALNERIMLSLVSTGGdcpfIVCMTYAFQTPD-KLCFILDLMNGGDLHYHLSQHGVFSEAEMR 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 115 KKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF----SFSKRclrddsgrmaLSKTFCGSPAYAAPEVLQ-G 189
Cdd:cd05606 102 FYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLglacDFSKK----------KPHASVGTHGYMAPEVLQkG 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 190 IPYQpKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQK---EHRVNFPRSkhLTGECKDLIYHMLQPDVNRRL 261
Cdd:cd05606 172 VAYD-SSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRmtlTMNVELPDS--FSPELKSLLEGLLQRDVSKRL 243
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
15-230 7.03e-16

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: 77.15  E-value: 7.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  15 GINLGEGSYAKVKSAYSERLkfNVAIK-IIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEiFETSHGKVYIVMELA 93
Cdd:cd14158  20 GNKLGEGGFGVVFKGYINDK--NVAVKkLAAMVDISTEDLTKQFEQEIQVMAKCQHENLVELLG-YSCDGPQLCLVYTYM 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLEliktRGALHEDEARKKFHQ-------LSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDS 166
Cdd:cd14158  97 PNGSLLD----RLACLNDTPPLSWHMrckiaqgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQ 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 167 GRMalSKTFCGSPAYAAPEVLQGiPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKE 230
Cdd:cd14158 173 TIM--TERIVGTTAYMAPEALRG-EITPKS-DIFSFGVVLLEIITGLPPVDENRDPQLLLDIKE 232
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
18-213 8.14e-16

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: 76.92  E-value: 8.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKapadflEKFLP----REIEILAMLNHCSIIKTYEIFETSHGKVYiVMELa 93
Cdd:cd07870   8 LGEGSYATVYKGISRINGQLVALKVISMKT------EEGVPftaiREASLLKGLKHANIVLLHDIIHTKETLTF-VFEY- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrddsGRMALS 172
Cdd:cd07870  80 MHTDLAQyMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAR-------AKSIPS 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 14042947 173 KTFCGSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGS 213
Cdd:cd07870 153 QTYSSEVVtlwYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQ 196
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
18-227 8.52e-16

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: 77.51  E-value: 8.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETSHGK----VYIVMELa 93
Cdd:cd07859   8 IGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRIL-REIKLLRLLRHPDIVEIKHIMLPPSRRefkdIYVVFEL- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMALSK 173
Cdd:cd07859  86 MESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLA-RVAFNDTPTAIFWT 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 174 TFCGSPAYAAPEVLQGI--PYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRI 227
Cdd:cd07859 165 DYVATRWYRAPELCGSFfsKYTPAI-DIWSIGCIFAEVLTGKPLFPGKNVVHQLDL 219
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
18-212 9.17e-16

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: 77.30  E-value: 9.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKkAPADFLEKFLPREIEILAMLNHCSIIKTYEIF--ETSHGKV---YIVMEL 92
Cdd:cd07880  23 VGSGAYGTVCSALDRRTGAKVAIKKLYRP-FQSELFAKRAYRELRLLKHMKHENVIGLLDVFtpDLSLDRFhdfYLVMPF 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 aVQGDLLELIKTRgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAls 172
Cdd:cd07880 102 -MGTDLGKLMKHE-KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVV-- 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14042947 173 ktfcgSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCG 212
Cdd:cd07880 178 -----TRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTG 212
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
6-279 1.01e-15

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: 75.85  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRGYLLGINLGEGSYAKV-KSAYSERlkfNVAIKIIDRKKAPADfleKFLpREIEILAMLNHCSIIKTYEIFeTSHG 84
Cdd:cd05039   2 AINKKDLKLGELIGKGEFGDVmLGDYRGQ---KVAVKCLKDDSTAAQ---AFL-AEASVMTTLRHPNLVQLLGVV-LEGN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVQGDLLELIKTRGALHEDeaRKKFHQLSL----AIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR 160
Cdd:cd05039  74 GLYIVTEYMAKGSLVDYLRSRGRAVIT--RKDQLGFALdvceGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 -CLRDDSGRMALSKTfcgspayaAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLR-IQKEHRVNFPR 237
Cdd:cd05039 152 aSSNQDGGKLPIKWT--------APEALREKKFSTKS-DVWSFGILLWeIYSFGRVPYPRIPLKDVVPhVEKGYRMEAPE 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 14042947 238 SkhltgeCKDLIYhmlqpdvnrrlhidEILSHCW-MQPKARGS 279
Cdd:cd05039 223 G------CPPEVY--------------KVMKNCWeLDPAKRPT 245
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
60-269 1.35e-15

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: 76.07  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQGDLLELIKTrgaLHED-----EARKKFH--QLSLAIKYCHDLDV 132
Cdd:cd05608  51 EKRILAKVHSRFIVSLAYAFQTK-TDLCLVMTIMNGGDLRYHIYN---VDEEnpgfqEPRACFYtaQIISGLEHLHQRRI 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 133 VHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDSGRmalSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCG 212
Cdd:cd05608 127 IYRDLKPENVLLDDDGNVRISDLGLAVE-LKDGQTK---TKGYAGTPGFMAPELLLGEEYDYSV-DYFTLGVTLYEMIAA 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 213 SMPYDDSNIKKMLRIQKEHRVNFP--RSKHLTGECKDLIYHMLQPDVNRRL-----HIDEILSH 269
Cdd:cd05608 202 RGPFRARGEKVENKELKQRILNDSvtYSEKFSPASKSICEALLAKDPEKRLgfrdgNCDGLRTH 265
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
18-227 1.37e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 76.97  E-value: 1.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApadFLEKFLpREIEILAMLNH------CSIIKTYEIFETShGKVYIVME 91
Cdd:cd14226  21 IGKGSFGQVVKAYDHVEQEWVAIKIIKNKKA---FLNQAQ-IEVRLLELMNKhdtenkYYIVRLKRHFMFR-NHLCLVFE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LaVQGDLLELIKT---RGaLHEDEARKKFHQLSLAIKYCH--DLDVVHRDLKCDNLLL--DKDFNIKLSDFSFSKRClrd 164
Cdd:cd14226  96 L-LSYNLYDLLRNtnfRG-VSLNLTRKFAQQLCTALLFLStpELSIIHCDLKPENILLcnPKRSAIKIIDFGSSCQL--- 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 165 dSGRMalsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN-IKKMLRI 227
Cdd:cd14226 171 -GQRI---YQYIQSRFYRSPEVLLGLPYDLAI-DMWSLGCILVEMHTGEPLFSGANeVDQMNKI 229
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
7-266 2.00e-15

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: 75.58  E-value: 2.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKV-----KSAYSERLKFNVAIKIIdrKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFeT 81
Cdd:cd05049   2 IKRDTIVLKRELGEGAFGKVflgecYNLEPEQDKMLVAVKTL--KDASSPDARKDFEREAELLTNLQHENIVKFYGVC-T 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHGKVYIVMELAVQGDLLELIKTRG-----ALHEDEARKKFH---------QLSLAIKYCHDLDVVHRDLKCDNLLLDKD 147
Cdd:cd05049  79 EGDPLLMVFEYMEHGDLNKFLRSHGpdaafLASEDSAPGELTlsqllhiavQIASGMVYLASQHFVHRDLATRNCLVGTN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 148 FNIKLSDFSFSKRCLRDDSGRMALSKTFcgsPA-YAAPEvlqGIPYQPKV--YDIWSLGVILY-IMVCGSMP-YDDSNIK 222
Cdd:cd05049 159 LVVKIGDFGMSRDIYSTDYYRVGGHTML---PIrWMPPE---SILYRKFTteSDVWSFGVVLWeIFTYGKQPwFQLSNTE 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 223 KMLRIQKEHRVNFPRSkhltgeCKDLIYHML----QPDVNRRLHIDEI 266
Cdd:cd05049 233 VIECITQGRLLQRPRT------CPSEVYAVMlgcwKREPQQRLNIKDI 274
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-207 2.20e-15

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: 75.68  E-value: 2.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII---DRKKAPadflEKFLpREIEILAMLNHCSIIKTYEIFETSHGK--------- 85
Cdd:cd14048  14 LGRGGFGVVFEAKNKVDDCNYAVKRIrlpNNELAR----EKVL-REVRALAKLDHPGIVRYFNAWLERPPEgwqekmdev 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 -VYIVMELAVQGDLLELIKTRGALHEDE---ARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS--- 158
Cdd:cd14048  89 yLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVtam 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14042947 159 -----KRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILY 207
Cdd:cd14048 169 dqgepEQTVLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKV-DIFALGLILF 221
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-212 2.56e-15

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 75.50  E-value: 2.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKApadflEKFLP----REIEILAMLNHCSIIKTYEIFETSHgKVYIVMELa 93
Cdd:cd07844   8 LGEGSYATVYKGRSKLTGQLVALKEI-RLEH-----EEGAPftaiREASLLKDLKHANIVTLHDIIHTKK-TLTLVFEY- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrddsGRMALS 172
Cdd:cd07844  80 LDTDLKQYMdDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR-------AKSVPS 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14042947 173 KTFCGSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCG 212
Cdd:cd07844 153 KTYSNEVVtlwYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATG 195
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-280 3.04e-15

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 75.34  E-value: 3.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFETS----HGKVYIVMELAVQGDLLELIKTRG---ALHEDEARKKFHQLSLAIKYCHDLD 131
Cdd:cd14039  40 HEIQIMKKLNHPNVVKACDVPEEMnflvNDVPLLAMEYCSGGDLRKLLNKPEnccGLKESQVLSLLSDIGSGIQYLHENK 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 132 VVHRDLKCDNLLLdKDFNIKLS----DFSFSKrclrdDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILY 207
Cdd:cd14039 120 IIHRDLKPENIVL-QEINGKIVhkiiDLGYAK-----DLDQGSLCTSFVGTLQYLAPELFENKSYTVTV-DYWSFGTMVF 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 208 IMVCGSMPYdDSNIKKML---RIQKEHRVNFPRSKHLTGECKdLIYHMLQPDVNRRLHIDEILShcWMQ------PKARG 278
Cdd:cd14039 193 ECIAGFRPF-LHNLQPFTwheKIKKKDPKHIFAVEEMNGEVR-FSTHLPQPNNLCSLIVEPMEG--WLQlmlnwdPVQRG 268

                ..
gi 14042947 279 SP 280
Cdd:cd14039 269 GG 270
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
18-273 3.19e-15

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 75.41  E-value: 3.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV---KSAYSERLKFNVAIKIIDRKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaV 94
Cdd:cd07872  14 LGEGTYATVfkgRSKLTENLVALKEIRLEHEEGAPCTAI-----REVSLLKDLKHANIVTLHDIVHTDK-SLTLVFEY-L 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrddsGRMALSK 173
Cdd:cd07872  87 DKDLKQYMDDCGNIMSMHNVKIFlYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR-------AKSVPTK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLR-------------------IQKEH 231
Cdd:cd07872 160 TYSNEVVtlwYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHlifrllgtpteetwpgissNDEFK 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 232 RVNFPRSK---------HLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd07872 240 NYNFPKYKpqplinhapRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFR 290
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-216 3.36e-15

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: 75.18  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTY----EIFETSHGKVYIV-MEL 92
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARdvppELEKLSPNDLPLLaMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDL---LELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDK---DFNIKLSDFSFSKrclrdDS 166
Cdd:cd13989  81 CSGGDLrkvLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgggRVIYKLIDLGYAK-----EL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 GRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd13989 156 DQGSLCTSFVGTLQYLAPELFESKKYTCTV-DYWSFGTLAFECITGYRPF 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
18-206 3.55e-15

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: 75.10  E-value: 3.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII--DRKK--APADFLekflpREIEILAMLNHCSIIKTYEIFETSH-GKVYIVMEL 92
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKVrmDNERdgIPISSL-----REITLLLNLRHPNIVELKEVVVGKHlDSIFLVMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQgDLLELIKTRGA-LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsgrmAL 171
Cdd:cd07845  90 CEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADF--------------GL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 172 SKTFcGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVIL 206
Cdd:cd07845 155 ARTY-GLPAkpmtpkvvtlwYRAPELLLGCTTYTTAIDMWAVGCIL 199
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
10-227 4.01e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 76.23  E-value: 4.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKiidrkKAPADflEKFLPREIEILAMLNHCSII--KTY---EIFETSHG 84
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAICIDTSEKVAIK-----KVLQD--PQYKNRELLIMKNLNHINIIflKDYyytECFKKNEK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   85 KVY--IVMEL---AVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD-KDFNIKLSDFSFS 158
Cdd:PTZ00036 139 NIFlnVVMEFipqTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSA 218
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  159 KRCLrddSGRMALSktFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYD-DSNIKKMLRI 227
Cdd:PTZ00036 219 KNLL---AGQRSVS--YICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSgQSSVDQLVRI 283
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
18-209 5.45e-15

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: 74.34  E-value: 5.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFN----VAIKIIDRKKAPA---DFlekflPREIEILAMLNHCSIIKTYEIFETSHGKVY-IV 89
Cdd:cd05038  12 LGEGHFGSVELCRYDPLGDNtgeqVAVKSLQPSGEEQhmsDF-----KREIEILRTLDHEYIVKYKGVCESPGRRSLrLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLE-LIKTRGALHedeaRKKFHQLSLAI----KYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRD 164
Cdd:cd05038  87 MEYLPSGSLRDyLQRHRDQID----LKRLLLFASQIckgmEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPED 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 165 DSGRMALSKTfcGSPA-YAAPEVLQgipyQPKVY---DIWSLGVILYIM 209
Cdd:cd05038 163 KEYYYVKEPG--ESPIfWYAPECLR----ESRFSsasDVWSFGVTLYEL 205
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
18-287 5.71e-15

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: 74.71  E-value: 5.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06650  13 LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPA--IRNQIIRELQVLHECNSPYIVGFYGAF-YSDGEISICMEHMDGGS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDL-DVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrdDSgrmaLSKTFC 176
Cdd:cd06650  90 LDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DS----MANSFV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPD 256
Cdd:cd06650 164 GTRSYMSPERLQGTHYSVQS-DIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMD 242
                       250       260       270
                ....*....|....*....|....*....|.
gi 14042947 257 VNRRLHIDEILSHCWMQPKARgSPSVAINKE 287
Cdd:cd06650 243 SRPPMAIFELLDYIVNEPPPK-LPSGVFSLE 272
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
18-277 7.45e-15

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 74.37  E-value: 7.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadflEKFLPREIEILAMLNHCSIIKTYE---IFETSHG---KVYIVME 91
Cdd:cd06637  14 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDE----EEEIKQEINMLKKYSHHRNIATYYgafIKKNPPGmddQLWLVME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIK-TRG-ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRm 169
Cdd:cd06637  90 FCGAGSVTDLIKnTKGnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 alsKTFCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGEC 245
Cdd:cd06637 169 ---NTFIGTPYWMAPEVIACDENPDATYdfksDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKF 245
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 246 KDLIYHMLQPDVNRRLHIDEILSHCWM--QPKAR 277
Cdd:cd06637 246 QSFIESCLVKNHSQRPSTEQLMKHPFIrdQPNER 279
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
7-244 9.19e-15

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: 73.38  E-value: 9.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKsaYSE-RLKFNVAIKIIDRKKAPAD-FLEkflprEIEILAMLNHCSIIKTYEIFeTSHG 84
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVK--YGKwRGQYDVAIKMIKEGSMSEDeFIE-----EAKVMMNLSHEKLVQLYGVC-TKQR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  85 KVYIVMELAVQGDLLELIK-TRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLr 163
Cdd:cd05113  73 PIFIITEYMANGCLLNYLReMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGRMALSKTFcgsPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPrskH 240
Cdd:cd05113 152 DDEYTSSVGSKF---PVrWSPPEVLMYSKFSSKS-DVWAFGVLMWeVYSLGKMPYERfTNSETVEHVSQGLRLYRP---H 224

                ....
gi 14042947 241 LTGE 244
Cdd:cd05113 225 LASE 228
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
18-272 9.59e-15

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 73.50  E-value: 9.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadflEKFLPREIEILAMLNHCSIIKTYE---IFETSHG---KVYIVME 91
Cdd:cd06636  24 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE----EEEIKLEINMLKKYSHHRNIATYYgafIKKSPPGhddQLWLVME 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIK-TRG-ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRm 169
Cdd:cd06636 100 FCGAGSVTDLVKnTKGnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR- 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 alsKTFCGSPAYAAPEVLQGIPYQPKVY----DIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGEC 245
Cdd:cd06636 179 ---NTFIGTPYWMAPEVIACDENPDATYdyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLKSKKWSKKF 255
                       250       260
                ....*....|....*....|....*..
gi 14042947 246 KDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06636 256 IDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
7-273 9.95e-15

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.41  E-value: 9.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    7 LKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAI---KIIDRKKAPADFLEKF--------LPREIEILAMLNHCSIIKT 75
Cdd:PTZ00024   6 ISERYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIkkvKIIEISNDVTKDRQLVgmcgihftTLRELKIMNEIKHENIMGL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   76 YEIFeTSHGKVYIVMELaVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF 155
Cdd:PTZ00024  86 VDVY-VEGDFINLVMDI-MASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  156 SFSKRCLRDDSGRmALSKTFCGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSN-IKK 223
Cdd:PTZ00024 164 GLARRYGYPPYSD-TLSKDETMQRReemtskvvtlwYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENeIDQ 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947  224 MLRIQK----EHRVNFPRSKHL---------------------TGECKDLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:PTZ00024 243 LGRIFEllgtPNEDNWPQAKKLplyteftprkpkdlktifpnaSDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
18-261 1.36e-14

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: 73.13  E-value: 1.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQGD 97
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDA-LCLVLTLMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDS--GRMalsk 173
Cdd:cd05630  87 LKFHIYHMGQAGFPEARAVFYaaEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTikGRV---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 tfcGSPAYAAPEVLQGIPY--QPkvyDIWSLGVILYIMVCGSMPYDDSNiKKMLRIQKEH---RVNFPRSKHLTGECKDL 248
Cdd:cd05630 163 ---GTVGYMAPEVVKNERYtfSP---DWWALGCLLYEMIAGQSPFQQRK-KKIKREEVERlvkEVPEEYSEKFSPQARSL 235
                       250
                ....*....|...
gi 14042947 249 IYHMLQPDVNRRL 261
Cdd:cd05630 236 CSMLLCKDPAERL 248
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
17-236 1.39e-14

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: 73.80  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAY-SERLKFNVAIKIIDRKkapaDFLEKFLPREIEILAMLN--------HCsiIKTYEIFEtsH-GKV 86
Cdd:cd14135   7 YLGKGVFSNVVRARdLARGNQEVAIKIIRNN----ELMHKAGLKELEILKKLNdadpddkkHC--IRLLRHFE--HkNHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMElAVQGDLLELIKTRGA---LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN-IKLSDF-SFSKrc 161
Cdd:cd14135  79 CLVFE-SLSMNLREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFgSASD-- 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 162 lRDDSGRMA-LSKTFcgspaYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFP 236
Cdd:cd14135 156 -IGENEITPyLVSRF-----YRAPEIILGLPYDYPI-DMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFP 224
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
18-204 1.60e-14

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: 73.53  E-value: 1.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME--LAVQ 95
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDH-TAWLVMEycLGSA 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTrgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrclrdDSGRMALSKTF 175
Cdd:cd06633 108 SDLLEVHKK--PLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG--------SASIASPANSF 177
                       170       180       190
                ....*....|....*....|....*....|..
gi 14042947 176 CGSPAYAAPEVLQGI---PYQPKVyDIWSLGV 204
Cdd:cd06633 178 VGTPYWMAPEVILAMdegQYDGKV-DIWSLGI 208
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
18-261 1.66e-14

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: 73.54  E-value: 1.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLN--HCSIIKTYEIFETSHGKVYIVMELAVQ 95
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrClrDDSGRMALSKTf 175
Cdd:cd14223  88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA--C--DFSKKKPHASV- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 cGSPAYAAPEVLQ-GIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIK---KMLRIQKEHRVNFPRSkhLTGECKDLIYH 251
Cdd:cd14223 163 -GTHGYMAPEVLQkGVAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTMAVELPDS--FSPELRSLLEG 238
                       250
                ....*....|
gi 14042947 252 MLQPDVNRRL 261
Cdd:cd14223 239 LLQRDVNRRL 248
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
18-215 2.67e-14

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 72.47  E-value: 2.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII----DRKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELA 93
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRVrlddDDEGVPSSAL-----REICLLKELKHKNIVRLYDVLHSDK-KLTLVFEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQgDLLELIKT-RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfskrclrddsgrmALS 172
Cdd:cd07839  82 DQ-DLKKYFDScNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADF--------------GLA 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14042947 173 KTFcGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMP 215
Cdd:cd07839 147 RAF-GIPVrcysaevvtlwYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRP 199
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
7-268 3.28e-14

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: 71.92  E-value: 3.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYSERL-----KFNVAIKIIdrKKAPADFLEKFlPREIEILAMLNHCSIIKTYEIFeT 81
Cdd:cd05092   2 IKRRDIVLKWELGEGAFGKVFLAECHNLlpeqdKMLVAVKAL--KEATESARQDF-QREAELLTVLQHQHIVRFYGVC-T 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHGKVYIVMELAVQGDLLELIKTRGA---LHEDEARKKFHQLSLA------------IKYCHDLDVVHRDLKCDNLLLDK 146
Cdd:cd05092  78 EGEPLIMVFEYMRHGDLNRFLRSHGPdakILDGGEGQAPGQLTLGqmlqiasqiasgMVYLASLHFVHRDLATRNCLVGQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 147 DFNIKLSDFSFSKRCLRDD----SGRMALsktfcgsPAYAAPEvlQGIPYQPKVY--DIWSLGVILY-IMVCGSMP-YDD 218
Cdd:cd05092 158 GLVVKIGDFGMSRDIYSTDyyrvGGRTML-------PIRWMPP--ESILYRKFTTesDIWSFGVVLWeIFTYGKQPwYQL 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 14042947 219 SNIKKMLRIQKEHRVNFPRSkhltgeCKDLIYHML----QPDVNRRLHIDEILS 268
Cdd:cd05092 229 SNTEAIECITQGRELERPRT------CPPEVYAIMqgcwQREPQQRHSIKDIHS 276
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
16-224 3.92e-14

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: 71.52  E-value: 3.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSA-YSERLK-FNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETShgKVYIVMELA 93
Cdd:cd05115  10 VELGSGNFGCVKKGvYKMRKKqIDVAIKVLKQGNEKAVRDE--MMREAQIMHQLDNPYIVRMIGVCEAE--ALMLVMEMA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAls 172
Cdd:cd05115  86 SGGPLNKfLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKA-- 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14042947 173 KTFCGSP-AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYddsniKKM 224
Cdd:cd05115 164 RSAGKWPlKWYAPECINFRKFSSRS-DVWSYGVTMWeAFSYGQKPY-----KKM 211
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
7-277 4.55e-14

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 71.61  E-value: 4.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYSERLKFN-----VAIKIIDRKKAPADFLEkFLpREIEILAMLNHCSIIKTYEIFET 81
Cdd:cd05032   3 LPREKITLIRELGQGSFGMVYEGLAKGVVKGepetrVAIKTVNENASMRERIE-FL-NEASVMKEFNCHHVVRLLGVVST 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHgKVYIVMELAVQGDLLELIKTRGALHEDE------ARKKFHQLSLAI----KYCHDLDVVHRDLKCDNLLLDKDFNIK 151
Cdd:cd05032  81 GQ-PTLVVMELMAKGDLKSYLRSRRPEAENNpglgppTLQKFIQMAAEIadgmAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 152 LSDFSFSKRCLRDD----SGRMALsktfcgsPA-YAAPEVLQGIPYQPKVyDIWSLGVILYIMVC-GSMPYddsnikkmL 225
Cdd:cd05032 160 IGDFGMTRDIYETDyyrkGGKGLL-------PVrWMAPESLKDGVFTTKS-DVWSFGVVLWEMATlAEQPY--------Q 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 14042947 226 RIQKEHRVNFPRSKhltgeckdliYHMLQPDvNRRLHIDEILSHCW-MQPKAR 277
Cdd:cd05032 224 GLSNEEVLKFVIDG----------GHLDLPE-NCPDKLLELMRMCWqYNPKMR 265
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
18-216 5.70e-14

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: 71.49  E-value: 5.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFN-VAIKII------DRKKAPADFLEKFLP------------REIEILAMLNHCSIIKTYEI 78
Cdd:cd14000   2 LGDGGFGSV---YRASYKGEpVAVKIFnkhtssNFANVPADTMLRHLRatdamknfrllrQELTVLSHLHHPSIVYLLGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 fetSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSL----AIKYCHDLDVVHRDLKCDNLLL-----DKDFN 149
Cdd:cd14000  79 ---GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 150 IKLSDFSFSKRCLRddSGrmalSKTFCGSPAYAAPEVLQG-IPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd14000 156 IKIADYGISRQCCR--MG----AKGSEGTPGFRAPEIARGnVIYNEKV-DVFSFGMLLYEILSGGAPM 216
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
60-273 6.02e-14

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: 71.23  E-value: 6.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  60 EIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQGDLLELIKTRGALHEDEARKKFH--QLSLAIKYCHDLDVVHRDL 137
Cdd:cd05605  50 EKQILEKVNSRFVVSLAYAYETKDA-LCLVLTIMNGGDLKFHIYNMGNPGFEEERAVFYaaEITCGLEHLHSERIVYRDL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 138 KCDNLLLDKDFNIKLSDFSFSKRCLRDDS--GRMalsktfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP 215
Cdd:cd05605 129 KPENILLDDHGHVRISDLGLAVEIPEGETirGRV-------GTVGYMAPEVVKNERYTFSP-DWWGLGCLIYEMIEGQAP 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 216 YDDSNiKKMLRIQKEHRVNFPR---SKHLTGECKDLIYHMLQPDVNRRL-----HIDEILSHCWMQ 273
Cdd:cd05605 201 FRARK-EKVKREEVDRRVKEDQeeySEKFSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFFK 265
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-269 6.44e-14

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: 70.98  E-value: 6.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYA---KVKSAYSERLKFNVAIKIIDRKkapadflekfLPREIEILAMLNHCSIIKTYEIFE-------------- 80
Cdd:cd14047  14 IGSGGFGqvfKAKHRIDGKTYAIKRVKLNNEK----------AEREVKALAKLDHPNIVRYNGCWDgfdydpetsssnss 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  81 TSHGK-VYIVMELAVQGDLLELIKTRGALHED--EARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSF 157
Cdd:cd14047  84 RSKTKcLFIQMEFCEKGTLESWIEKRNGEKLDkvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 158 skrcLRDDSGRMALSKTFcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIM--VCGSMpYDDSNIKKMLRIQkEHRVNF 235
Cdd:cd14047 164 ----VTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEV-DIYALGLILFELlhVCDSA-FEKSKFWTDLRNG-ILPDIF 235
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 236 PRSKHLTgecKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14047 236 DKRYKIE---KTIIKKMLSKKPEDRPNASEILRT 266
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
17-269 6.74e-14

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: 70.80  E-value: 6.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLKFNVAIKII-DRKKAPADFLEKFlpREI---EILAMlnHCSIIKTYEIFEtSHGKVYIVMEL 92
Cdd:cd14050   8 KLGEGSFGEVFKVRSREDGKLYAVKRSrSRFRGEKDRKRKL--EEVerhEKLGE--HPNCVRFIKAWE-EKGILYIQTEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AvQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrcLRDDSGRMALS 172
Cdd:cd14050  83 C-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFG-----LVVELDKEDIH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTFCGSPAYAAPEVLQGIPyqPKVYDIWSLGVILYIMVCG-SMPyddSNIKKMLRIQKEHrVNFPRSKHLTGECKDLIYH 251
Cdd:cd14050 157 DAQEGDPRYMAPELLQGSF--TKAADIFSLGITILELACNlELP---SGGDGWHQLRQGY-LPEEFTAGLSPELRSIIKL 230
                       250
                ....*....|....*...
gi 14042947 252 MLQPDVNRRLHIDEILSH 269
Cdd:cd14050 231 MMDPDPERRPTAEDLLAL 248
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
59-302 7.29e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 71.78  E-value: 7.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   59 REIEILAMLNHCSIIKTYEIFETShGKVYIVMELAVQGDLleliKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLK 138
Cdd:PLN00034 121 REIEILRDVNHPNVVKCHDMFDHN-GEIQVLLEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  139 CDNLLLDKDFNIKLSDFSFSkRCLrddSGRMALSKTFCGSPAYAAPEVL-----QGIpYQPKVYDIWSLGVILYIMVCGS 213
Cdd:PLN00034 196 PSNLLINSAKNVKIADFGVS-RIL---AQTMDPCNSSVGTIAYMSPERIntdlnHGA-YDGYAGDIWSLGVSILEFYLGR 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  214 MPYDDSN----IKKMLRIQKEHRVNFPRSKhlTGECKDLIYHMLQPDVNRRLHIDEILSHCWMqpkARGSPSvainkEGE 289
Cdd:PLN00034 271 FPFGVGRqgdwASLMCAICMSQPPEAPATA--SREFRHFISCCLQREPAKRWSAMQLLQHPFI---LRAQPG-----QGQ 340
                        250
                 ....*....|...
gi 14042947  290 SSRGTEPLWTPEP 302
Cdd:PLN00034 341 GGPNLHQLLPPPR 353
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
18-271 7.33e-14

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: 71.83  E-value: 7.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrkKAPADFLE--KFlprEIEILAML--------NHCsiIKTYEIFEtSHGKVY 87
Cdd:cd14134  20 LGEGTFGKVLECWDRKRKRYVAVKII---RNVEKYREaaKI---EIDVLETLaekdpngkSHC--VQLRDWFD-YRGHMC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 IVMELAvqG----DLLELIKTRGALHEDeARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLD------------------ 145
Cdd:cd14134  91 IVFELL--GpslyDFLKKNNYGPFPLEH-VQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrqirv 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 146 -KDFNIKLSDF---SFskrclrDDSGRMALSKTfcgsPAYAAPEVLQGIP-YQPKvyDIWSLGVILY------------- 207
Cdd:cd14134 168 pKSTDIKLIDFgsaTF------DDEYHSSIVST----RHYRAPEVILGLGwSYPC--DVWSIGCILVelytgellfqthd 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 208 ------IM--VCGSMPYDdsNIKKMLRIQK-----EHRVNFP-------RSKHLTGECK--------------DLIYHML 253
Cdd:cd14134 236 nlehlaMMerILGPLPKR--MIRRAKKGAKyfyfyHGRLDWPegsssgrSIKRVCKPLKrlmllvdpehrllfDLIRKML 313
                       330
                ....*....|....*...
gi 14042947 254 QPDVNRRLHIDEILSHCW 271
Cdd:cd14134 314 EYDPSKRITAKEALKHPF 331
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
21-237 7.50e-14

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: 70.72  E-value: 7.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  21 GSYAKVKSAYSERLKFNVAIKIIDRKkaPADflEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIvMELAVQGDLLE 100
Cdd:cd14110  14 GRFSVVRQCEEKRSGQMLAAKIIPYK--PED--KQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLI-EELCSGPELLY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 101 LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF----SFS--KRCLRDDSGRMALSKt 174
Cdd:cd14110  89 NLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLgnaqPFNqgKVLMTDKKGDYVETM- 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 175 fcgspayaAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPR 237
Cdd:cd14110 168 --------APELLEGQGAGPQT-DIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSR 221
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
18-272 7.82e-14

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 70.91  E-value: 7.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY----SERLKFNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETShgKVYIVMELA 93
Cdd:cd05057  15 LGSGAFGTVYKGVwipeGEKVKIPVAIKVLREETGPKANEE--ILDEAYVMASVDHPHLVRLLGICLSS--QVQLITQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTrgalHEDEARKKF-----HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDS-- 166
Cdd:cd05057  91 PLGCLLDYVRN----HRDNIGSQLllnwcVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKey 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 ----GRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLR-IQKEHRVNFPRSkh 240
Cdd:cd05057 167 haegGKVPIK--------WMALESIQYRIYTHKS-DVWSYGVTVWeLMTFGAKPYEGIPAVEIPDlLEKGERLPQPPI-- 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 14042947 241 ltgeCKDLIYHmlqpdvnrrlhideILSHCWM 272
Cdd:cd05057 236 ----CTIDVYM--------------VLVKCWM 249
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
7-236 9.32e-14

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: 70.53  E-value: 9.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKV-KSAYS--ERLKFNVAIKIIDRKKAPADfLEKFLpREIEILAMLNHCSIIKTYEIFETSh 83
Cdd:cd05056   3 IQREDITLGRCIGEGQFGDVyQGVYMspENEKIAVAVKTCKNCTSPSV-REKFL-QEAYIMRQFDHPHIVKLIGVITEN- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  84 gKVYIVMELAVQGDLLELIKTRGALHEDEARKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCL 162
Cdd:cd05056  80 -PVWIVMELAPLGELRSYLQVNKYSLDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLS-RYM 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 163 RDDSGRMAlSKTfcGSP-AYAAPEvlqGIPYQ--PKVYDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFP 236
Cdd:cd05056 158 EDESYYKA-SKG--KLPiKWMAPE---SINFRrfTSASDVWMFGVCMWeILMLGVKPFQGvKNNDVIGRIENGERLPMP 230
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
18-273 9.91e-14

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: 71.23  E-value: 9.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME--LAVQ 95
Cdd:cd06635  33 IGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREH-TAWLVMEycLGSA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTrgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrclrdDSGRMALSKTF 175
Cdd:cd06635 112 SDLLEVHKK--PLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG--------SASIASPANSF 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGI---PYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHM 252
Cdd:cd06635 182 VGTPYWMAPEVILAMdegQYDGKV-DVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSC 260
                       250       260
                ....*....|....*....|.
gi 14042947 253 LQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd06635 261 LQKIPQDRPTSEELLKHMFVL 281
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
18-253 1.01e-13

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 70.45  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSA---YSERLKFNVAIKIIDRKK-----APADFLekflpREIEILAMLNHCSIIKTYEIFETShgKVYIV 89
Cdd:cd05040   3 LGDGSFGVVRRGewtTPSGKVIQVAVKCLKSDVlsqpnAMDDFL-----KEVNAMHSLDHPNLIRLYGVVLSS--PLMMV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLEliktrgALHEDEARKKFH-------QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCL 162
Cdd:cd05040  76 TELAPLGSLLD------RLRKDQGHFLIStlcdyavQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLM-RAL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 163 --RDDSGRMALSKTFcgsP-AYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC-GSMPYDDSNIKKML-RIQKEHRvNFPR 237
Cdd:cd05040 149 pqNEDHYVMQEHRKV---PfAWCAPESLKTRKFSHAS-DVWMFGVTLWEMFTyGEEPWLGLNGSQILeKIDKEGE-RLER 223
                       250
                ....*....|....*.
gi 14042947 238 SKHltgeCKDLIYHML 253
Cdd:cd05040 224 PDD----CPQDIYNVM 235
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
18-272 1.15e-13

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: 70.65  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLprEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIM--ELDILHKAVSPYIVDFYGAF-FIEGAVYMCMEYMDAGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELI---KTRGALHEDEARKKFHQLSLAIKYC-HDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRddsgrmALSK 173
Cdd:cd06622  86 LDKLYaggVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVA------SLAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 TFCGSPAYAAPEVLQ-GIPYQPKVY----DIWSLGVILYIMVCGSMPYDD---SNIKKMLR-IQKEHRVNFPRSkhLTGE 244
Cdd:cd06622 160 TNIGCQSYMAPERIKsGGPNQNPTYtvqsDVWSLGLSILEMALGRYPYPPetyANIFAQLSaIVDGDPPTLPSG--YSDD 237
                       250       260
                ....*....|....*....|....*...
gi 14042947 245 CKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd06622 238 AQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
59-272 1.16e-13

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: 70.25  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFETSHgKVYIVMElAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLK 138
Cdd:cd14112  49 REFESLRTLQHENVQRLIAAFKPSN-FAYLVME-KLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQ 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 139 CDNLLLD--KDFNIKLSDFSFSKRCLRddsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPY 216
Cdd:cd14112 127 PDNIMFQsvRSWQVKLVDFGRAQKVSK------LGKVPVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPF 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 217 -----DDSNIKKMLRIQKEHRVNFPrsKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWM 272
Cdd:cd14112 201 tseydDEEETKENVIFVKCRPNLIF--VEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
18-216 1.19e-13

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 70.98  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKK--APADFLEkflpREIEILAMLNHCSIIKTYEIFE--TSHGKVyIVMELA 93
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSfmRPLDVQM----REFEVLKKLNHKNIVKLFAIEEelTTRHKV-LVMELC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDL---LELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL--LDKD-FNI-KLSDFSfSKRCLRDDS 166
Cdd:cd13988  76 PCGSLytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDgQSVyKLTDFG-AARELEDDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 167 GRMALSktfcGSPAYAAPE-----VLQ---GIPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd13988 155 QFVSLY----GTEEYLHPDmyeraVLRkdhQKKYGATV-DLWSIGVTFYHAATGSLPF 207
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
18-212 1.26e-13

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: 70.88  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFlpREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELaVQGD 97
Cdd:cd07869  13 LGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI--REASLLKGLKHANIVLLHDIIHTKE-TLTLVFEY-VHTD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrclrddsGRMALSKTFC 176
Cdd:cd07869  89 LCQYMdKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR-------AKSVPSHTYS 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 14042947 177 GSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCG 212
Cdd:cd07869 162 NEVVtlwYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQG 200
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
60-220 1.41e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 72.08  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    60 EIEILAMLNHCSIIKTYEIF-ETSHGKVYIVMELAVQGDLLELI----KTRGALHEDEARKKFHQLSLAIKYCHDLD--- 131
Cdd:PTZ00266   62 EVNVMRELKHKNIVRYIDRFlNKANQKLYILMEFCDAGDLSRNIqkcyKMFGKIEEHAIVDITRQLLHALAYCHNLKdgp 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   132 ----VVHRDLKCDNLLLD-------------KDFN----IKLSDFSFSKrclrdDSGRMALSKTFCGSPAYAAPEVLQgi 190
Cdd:PTZ00266  142 ngerVLHRDLKPQNIFLStgirhigkitaqaNNLNgrpiAKIGDFGLSK-----NIGIESMAHSCVGTPYYWSPELLL-- 214
                         170       180       190
                  ....*....|....*....|....*....|....
gi 14042947   191 pYQPKVYD----IWSLGVILYIMVCGSMPYDDSN 220
Cdd:PTZ00266  215 -HETKSYDdksdMWALGCIIYELCSGKTPFHKAN 247
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
18-277 2.02e-13

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: 69.62  E-value: 2.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSA---YSERLKFNVAIKIID---RKKAPADFLEkflprEIEILAMLNHCSIIKtYEIFETSHGKVYIVME 91
Cdd:cd05063  13 IGAGEFGEVFRGilkMPGRKEVAVAIKTLKpgyTEKQRQDFLS-----EASIMGQFSHHNIIR-LEGVVTKFKPAMIITE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSgrma 170
Cdd:cd05063  87 YMENGALDKYLRDHdGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLS-RVLEDDP---- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 171 lSKTFCGSPA-----YAAPEvlqGIPYQ--PKVYDIWSLGVILY-IMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRskhl 241
Cdd:cd05063 162 -EGTYTTSGGkipirWTAPE---AIAYRkfTSASDVWSFGIVMWeVMSFGERPYwDMSNHEVMKAINDGFRLPAPM---- 233
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 14042947 242 tgECKDLIYH-MLQpdvnrrlhideilshCWMQPKAR 277
Cdd:cd05063 234 --DCPSAVYQlMLQ---------------CWQQDRAR 253
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
59-246 2.03e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 70.64  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   59 REIEILAMLNHCSIIKTYEIFETshgKVYIVMELAV-QGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDL 137
Cdd:PHA03207 135 REIDILKTISHRAIINLIHAYRW---KSTVCMVMPKyKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  138 KCDNLLLDKDFNIKLSDFSFSkrCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPY- 216
Cdd:PHA03207 212 KTENIFLDEPENAVLGDFGAA--CKLDAHPDTPQCYGWSGTLETNSPELLALDPYCAKT-DIWSAGLVLFEMSVKNVTLf 288
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 14042947  217 ------DDSNIKKMLRIQKEHRVNFPRSKHlTGECK 246
Cdd:PHA03207 289 gkqvksSSSQLRSIIRCMQVHPLEFPQNGS-TNLCK 323
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
18-219 2.16e-13

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: 69.45  E-value: 2.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYsERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd14027   1 LDSGGFGKVSLCF-HRTQGLVVLKTVYTGPNCIEHNEALL-EEGKMMNRLRHSRVVKLLGVI-LEEGKYSLVMEYMEKGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSlAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSD-----FSFSKRCLRDDSGRMALS 172
Cdd:cd14027  78 LMHVLKKVSVPLSVKGRIILEIIE-GMAYLHGKGVIHKDLKPENILVDNDFHIKIADlglasFKMWSKLTKEEHNEQREV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14042947 173 KTFCGSPA----YAAPEVLQGIPYQP-KVYDIWSLGVILYIMVCGSMPYDDS 219
Cdd:cd14027 157 DGTAKKNAgtlyYMAPEHLNDVNAKPtEKSDVYSFAIVLWAIFANKEPYENA 208
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
18-261 2.20e-13

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: 70.48  E-value: 2.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLN--HCSIIKTYEIFETSHGKVYIVMELAVQ 95
Cdd:cd05633  13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVStgDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrClrDDSGRMALSKTf 175
Cdd:cd05633  93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA--C--DFSKKKPHASV- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 cGSPAYAAPEVLQ-GIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQK-EHRVNFPRSKHLTGECKDLIYHML 253
Cdd:cd05633 168 -GTHGYMAPEVLQkGTAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRmTLTVNVELPDSFSPELKSLLEGLL 245

                ....*...
gi 14042947 254 QPDVNRRL 261
Cdd:cd05633 246 QRDVSKRL 253
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
12-269 2.33e-13

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: 69.88  E-value: 2.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPadflEKFLPREIEILAMLN-HCSIIKTYEIFETSHGKVY-IV 89
Cdd:cd14132  20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL--KPVK----KKKIKREIKILQNLRgGPNIVKLLDVVKDPQSKTPsLI 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTrgaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN-IK-----LSDFSFSKrclR 163
Cdd:cd14132  94 FEYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRlidwgLAEFYHPG---Q 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 DDSGRMAlsktfcgSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIM----------------------VCGS-------- 213
Cdd:cd14132 168 EYNVRVA-------SRYYKGPELLVDYQYYDYSLDMWSLGCMLASMifrkepffhghdnydqlvkiakVLGTddlyayld 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 214 ---MPYDDSNIKKMLRIQK---EHRVNfPRSKHL-TGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14132 241 kygIELPPRLNDILGRHSKkpwERFVN-SENQHLvTPEALDLLDKLLRYDHQERITAKEAMQH 302
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
18-269 2.53e-13

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: 69.17  E-value: 2.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSA-------YSERLKFNVAIKIIDRKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHGKVYIVM 90
Cdd:cd14019   9 IGEGTFSSVYKAedklhdlYDRNKGRLVALKHIYPTSSPSRIL-----NELECLERLGGSNNVSGLITAFRNEDQVVAVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDLLELIKTRGALhedEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLldkdFNIK-----LSDFSFSKRcLRDD 165
Cdd:cd14019  84 PYIEHDDFRDFYRKMSLT---DIRIYLRNLFKALKHVHSFGIIHRDVKPGNFL----YNREtgkgvLVDFGLAQR-EEDR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRMAlskTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMP--YDDSNIKKMLRIQkehrvnfprskHLTG 243
Cdd:cd14019 156 PEQRA---PRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPffFSSDDIDALAEIA-----------TIFG 221
                       250       260
                ....*....|....*....|....*...
gi 14042947 244 --ECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14019 222 sdEAYDLLDKLLELDPSKRITAEEALKH 249
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
7-253 2.60e-13

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: 69.75  E-value: 2.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYSERL------KFNVAIKIIDRKKAPADFLEkfLPREIEILAML-NHCSIIKTYEIF 79
Cdd:cd05053   9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLdnkpneVVTVAVKMLKDDATEKDLSD--LVSEMEMMKMIgKHKNIINLLGAC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  80 eTSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLS---------------------LAIKYChdldvVHRDLK 138
Cdd:cd05053  87 -TQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVPEeqltqkdlvsfayqvargmeyLASKKC-----IHRDLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 139 CDNLLLDKDFNIKLSDFSFSKRCLRDDSGRmalsKTFCGS-PA-YAAPEVLQGipyqpKVY----DIWSLGVILY-IMVC 211
Cdd:cd05053 161 ARNVLVTEDNVMKIADFGLARDIHHIDYYR----KTTNGRlPVkWMAPEALFD-----RVYthqsDVWSFGVLLWeIFTL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 14042947 212 GSMPYDDSNIKKMLRIQKE-HRVNFPRSkhltgeCKDLIYHML 253
Cdd:cd05053 232 GGSPYPGIPVEELFKLLKEgHRMEKPQN------CTQELYMLM 268
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-204 2.76e-13

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: 69.29  E-value: 2.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPADFLEkFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVME 91
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII--KLEPGDDFS-LIQQEIFMVKECKHCNIVAYFGSY-LSREKLWICME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrddSGRMAL 171
Cdd:cd06646  87 YCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKI----TATIAK 162
                       170       180       190
                ....*....|....*....|....*....|....*
gi 14042947 172 SKTFCGSPAYAAPEV--LQGIPYQPKVYDIWSLGV 204
Cdd:cd06646 163 RKSFIGTPYWMAPEVaaVEKNGGYNQLCDIWAVGI 197
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
16-271 2.83e-13

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: 69.36  E-value: 2.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVA-IKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETS-HGK--VYIVME 91
Cdd:cd14031  16 IELGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAE--QQRFKEEAEMLKGLQHPNIVRFYDSWESVlKGKkcIVLVTE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDF-NIKLSDFSFSKRClrddsgR 168
Cdd:cd14031  94 LMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLM------R 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVLQgiPYQPKVYDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSKHLTGECKD 247
Cdd:cd14031 168 TSFAKSVIGTPEFMAPEMYE--EHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSGIKPASFNKVTDPEVKE 245
                       250       260
                ....*....|....*....|....
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd14031 246 IIEGCIRQNKSERLSIKDLLNHAF 269
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
7-254 3.01e-13

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 69.66  E-value: 3.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYS---ERLKFN----VAIKIIDRKKAPADFLEkfLPREIEILAML-NHCSIIKTYEI 78
Cdd:cd05098  10 LPRDRLVLGKPLGEGCFGQVVLAEAiglDKDKPNrvtkVAVKMLKSDATEKDLSD--LISEMEMMKMIgKHKNIINLLGA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FeTSHGKVYIVMELAVQGDLLELIKTR---------GALHEDEARKKF-------HQLSLAIKYCHDLDVVHRDLKCDNL 142
Cdd:cd05098  88 C-TQDGPLYVIVEYASKGNLREYLQARrppgmeycyNPSHNPEEQLSSkdlvscaYQVARGMEYLASKKCIHRDLAARNV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 143 LLDKDFNIKLSDFSFSKRCLRDD------SGRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMP 215
Cdd:cd05098 167 LVTEDNVMKIADFGLARDIHHIDyykkttNGRLPVK--------WMAPEALFDRIYTHQS-DVWSFGVLLWeIFTLGGSP 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 14042947 216 YDDSNIKKMLRIQKE-HRVNFPRSkhltgeCKDLIYHMLQ 254
Cdd:cd05098 238 YPGVPVEELFKLLKEgHRMDKPSN------CTNELYMMMR 271
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
19-271 3.30e-13

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: 69.62  E-value: 3.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVKSAYSERLKFN--VAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIF-ETSHGKVYIVMELAvQ 95
Cdd:cd07842   9 GRGTYGRVYKAKRKNGKDGkeYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEVFlEHADKSVYLLFDYA-E 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIK-----TRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN----IKLSDFSFSKRClrdds 166
Cdd:cd07842  88 HDLWQIIKfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDLGLARLF----- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 167 gRMALSKTFCGSPA-----YAAPEVLQGIPYQPKVYDIWSLGVIL------------------------------YIMVC 211
Cdd:cd07842 163 -NAPLKPLADLDPVvvtiwYRAPELLLGARHYTKAIDIWAIGCIFaelltlepifkgreakikksnpfqrdqlerIFEVL 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 212 GsMPYDD--SNIKKM---LRIQKEH-RVNFPRS---------KHLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07842 242 G-TPTEKdwPDIKKMpeyDTLKSDTkASTYPNSllakwmhkhKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
18-271 3.44e-13

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: 69.32  E-value: 3.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKII---DRKKA-PADFLekflpREIEILAMLNHCSIIKTYEIFET-------SHGKV 86
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKKVlmeNEKEGfPITAL-----REIKILQLLKHENVVNLIEICRTkatpynrYKGSI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAvQGDLLELIKTRGA-LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDD 165
Cdd:cd07865  95 YLVFEFC-EHDLAGLLSNKNVkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSLAK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 166 SGRMALSKTFCGSPAYAAPEVLQGI-PYQPKVyDIWSLGVILY-------IM--------------VCGSMP-------- 215
Cdd:cd07865 174 NSQPNRYTNRVVTLWYRPPELLLGErDYGPPI-DMWGAGCIMAemwtrspIMqgnteqhqltlisqLCGSITpevwpgvd 252
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 216 -YDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCW 271
Cdd:cd07865 253 kLELFKKMELPQGQKRKVKERLKPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
59-215 3.55e-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: 69.39  E-value: 3.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHD-LDVVHRDL 137
Cdd:cd06615  48 RELKVLHECNSPYIVGFYGAF-YSDGEISICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREkHKIMHRDV 126
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 138 KCDNLLLDKDFNIKLSDFSFSKRCLrdDSgrMAlsKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP 215
Cdd:cd06615 127 KPSNILVNSRGEIKLCDFGVSGQLI--DS--MA--NSFVGTRSYMSPERLQGTHYTVQS-DIWSLGLSLVEMAIGRYP 197
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
9-236 3.61e-13

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 69.61  E-value: 3.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGINLGEGSYAKVKSAYSERLK-------FNVAIKIIDRKKAPADFLEkfLPREIEILAMLN-HCSIIKTYEIFe 80
Cdd:cd05099  11 RDRLVLGKPLGEGCFGQVVRAEAYGIDksrpdqtVTVAVKMLKDNATDKDLAD--LISEMELMKLIGkHKNIINLLGVC- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  81 TSHGKVYIVMELAVQGDLLELIKTR-----------GALHEDEARKK-----FHQLSLAIKYCHDLDVVHRDLKCDNLLL 144
Cdd:cd05099  88 TQEGPLYVIVEYAAKGNLREFLRARrppgpdytfdiTKVPEEQLSFKdlvscAYQVARGMEYLESRRCIHRDLAARNVLV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 145 DKDFNIKLSDFSFSKRCLRDD------SGRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYD 217
Cdd:cd05099 168 TEDNVMKIADFGLARGVHDIDyykktsNGRLPVK--------WMAPEALFDRVYTHQS-DVWSFGILMWeIFTLGGSPYP 238
                       250       260
                ....*....|....*....|
gi 14042947 218 DSNIKKMLRIQKE-HRVNFP 236
Cdd:cd05099 239 GIPVEELFKLLREgHRMDKP 258
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
18-273 4.29e-13

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 69.28  E-value: 4.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME--LAVQ 95
Cdd:cd06634  23 IGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREH-TAWLVMEycLGSA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTrgALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrclrdDSGRMALSKTF 175
Cdd:cd06634 102 SDLLEVHKK--PLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG--------SASIMAPANSF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 CGSPAYAAPEVLQGI---PYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHM 252
Cdd:cd06634 172 VGTPYWMAPEVILAMdegQYDGKV-DVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSC 250
                       250       260
                ....*....|....*....|.
gi 14042947 253 LQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd06634 251 LQKIPQDRPTSDVLLKHRFLL 271
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
18-206 5.57e-13

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 68.96  E-value: 5.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApadFLEKFLpREIEILAML------NHCSIIKTYEIFeTSHGKVYIVME 91
Cdd:cd14225  51 IGKGSFGQVVKALDHKTNEHVAIKIIRNKKR---FHHQAL-VEVKILDALrrkdrdNSHNVIHMKEYF-YFRNHLCITFE 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LaVQGDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDK--DFNIKLSDFSFSkrCLRDDSg 167
Cdd:cd14225 126 L-LGMNLYELIKKNNfqGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQrgQSSIKVIDFGSS--CYEHQR- 201
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 14042947 168 rmalSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14225 202 ----VYTYIQSRFYRSPEVILGLPYSMAI-DMWSLGCIL 235
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
18-232 5.62e-13

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 68.41  E-value: 5.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGD 97
Cdd:cd14026   5 LSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPE-FLGIVTEYMTNGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKtRGALHEDEA----RKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDFNIKLSDFSFSK-RCLRDDSGRMA 170
Cdd:cd14026  84 LNELLH-EKDIYPDVAwplrLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwRQLSISQSRSS 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 171 LSKTFCGSPAYAAPEvlqgiPYQPKV-------YDIWSLGVILYIMVCGSMPYDDSN--IKKMLRIQKEHR 232
Cdd:cd14026 163 KSAPEGGTIIYMPPE-----EYEPSQkrrasvkHDIYSYAIIMWEVLSRKIPFEEVTnpLQIMYSVSQGHR 228
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
17-267 6.34e-13

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: 68.43  E-value: 6.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAY-SERLkfnVAIKIIDRKKaPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELaVQ 95
Cdd:cd13980   7 SLGSTRFLKVARARhDEGL---VVVKVFVKPD-PALPLRSYKQRLEEIRDRLLELPNVLPFQKVIETDKAAYLIRQY-VK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEarKKF--HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLR---------- 163
Cdd:cd13980  82 YNLYDRISTRPFLNLIE--KKWiaFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTYLpednpadfsy 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 164 --DDSGR----MALSKtFCGSPAYAAPEVLQGIPYQPKVyDIWSLG-VILYIMVCGSMPYDDSNI---KKMlriqkEHRV 233
Cdd:cd13980 160 ffDTSRRrtcyIAPER-FVDALTLDAESERRDGELTPAM-DIFSLGcVIAELFTEGRPLFDLSQLlayRKG-----EFSP 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 14042947 234 NFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEIL 267
Cdd:cd13980 233 EQVLEKIEDPNIRELILHMIQRDPSKRLSAEDYL 266
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
12-225 1.01e-12

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: 68.35  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPAD-----------------------FLEKFLPREIEILAMLN 68
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKI-RCNAPENvelalrefwalssiqrqhpnviqLEECVLQRDGLAQRMSH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  69 HCSIIKTY-EIFETS-HGKV----------YIVMELAVQGDLLELIKTRGAlhEDEARKKF-HQLSLAIKYCHDLDVVHR 135
Cdd:cd13977  81 GSSKSDLYlLLVETSlKGERcfdprsacylWFVMEFCDGGDMNEYLLSRRP--DRQTNTSFmLQLSSALAFLHRNQIVHR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 136 DLKCDNLLLDKDFN---IKLSDFSFSKRCL---RDDSGRMALSKTF----CGSPAYAAPEVLQGiPYQPKVyDIWSLGVI 205
Cdd:cd13977 159 DLKPDNILISHKRGepiLKVADFGLSKVCSgsgLNPEEPANVNKHFlssaCGSDFYMAPEVWEG-HYTAKA-DIFALGII 236
                       250       260
                ....*....|....*....|
gi 14042947 206 LYIMVcGSMPYDDSNIKKML 225
Cdd:cd13977 237 IWAMV-ERITFRDGETKKEL 255
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-220 1.04e-12

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 67.35  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFNVAIKIIDRKKAPADFLEKFlPREIEILAMLNHCSIIkTYEIFETSHGkVYIVMELAVQGD 97
Cdd:cd14150   8 IGTGSFGTV---FRGKWHGDVAVKILKVTEPTPEQLQAF-KNEMQVLRKTRHVNIL-LFMGFMTRPN-FAIITQWCEGSS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 L---LELIKTRGALHE--DEARkkfhQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRdDSGRMALS 172
Cdd:cd14150  82 LyrhLHVTETRFDTMQliDVAR----QTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTR-WSGSQQVE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 14042947 173 KTfCGSPAYAAPEVLQGIPYQPKVY--DIWSLGVILYIMVCGSMPYDDSN 220
Cdd:cd14150 157 QP-SGSILWMAPEVIRMQDTNPYSFqsDVYAYGVVLYELMSGTLPYSNIN 205
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
18-254 1.05e-12

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 67.72  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSER--LKFNVAIKIIDRKKAPADflEKFLPREIEILAML-NHCSIIKTYEIFEtSHGKVYIVMELAV 94
Cdd:cd05089  10 IGEGNFGQVIKAMIKKdgLKMNAAIKMLKEFASEND--HRDFAGELEVLCKLgHHPNIINLLGACE-NRGYLYIAIEYAP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFH----------------QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05089  87 YGNLLDFLRKSRVLETDPAFAKEHgtastltsqqllqfasDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KrclrddSGRMALSKTFCGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKML-RIQKEHRVNF 235
Cdd:cd05089 167 R------GEEVYVKKTMGRLPVrWMAIESLNYSVYTTKS-DVWSFGVLLWeIVSLGGTPYCGMTCAELYeKLPQGYRMEK 239
                       250
                ....*....|....*....
gi 14042947 236 PRSkhltgeCKDLIYHMLQ 254
Cdd:cd05089 240 PRN------CDDEVYELMR 252
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
18-265 1.09e-12

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: 68.07  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQGD 97
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDA-LCLVLTIMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALsktf 175
Cdd:cd05632  89 LKFHIYNMGNPGFEEERALFYaaEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRV---- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 cGSPAYAAPEVLQGIPY--QPkvyDIWSLGVILYIMVCGSMPYDDSNiKKMLRIQKEHRVNFPR---SKHLTGECKDLIY 250
Cdd:cd05632 165 -GTVGYMAPEVLNNQRYtlSP---DYWGLGCLIYEMIEGQSPFRGRK-EKVKREEVDRRVLETEevySAKFSEEAKSICK 239
                       250
                ....*....|....*
gi 14042947 251 HMLQPDVNRRLHIDE 265
Cdd:cd05632 240 MLLTKDPKQRLGCQE 254
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
10-206 1.40e-12

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: 67.72  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEGSYAKVKSAYSERLKFNVAIKII----DRKKAPADFLekflpREIEILAMLNHCSIIKTYE-IFETS-- 82
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKIlmhnEKDGFPITAL-----REIKILKKLKHPNVVPLIDmAVERPdk 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  83 ----HGKVYIVMELAVQgDLLELIKT-RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSF 157
Cdd:cd07866  83 skrkRGSVYMVTPYMDH-DLSGLLENpSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGL 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 158 SKrcLRDDSGRMALSKTFCGSPAYA---------APEVLQGIP-YQPKVyDIWSLGVIL 206
Cdd:cd07866 162 AR--PYDGPPPNPKGGGGGGTRKYTnlvvtrwyrPPELLLGERrYTTAV-DIWGIGCVF 217
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
16-271 1.49e-12

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 67.02  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVA-IKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETS-HGK--VYIVME 91
Cdd:cd14032   7 IELGRGSFKTVYKGLDTETWVEVAwCELQDRKLTKVE--RQRFKEEAEMLKGLQHPNIVRFYDFWESCaKGKrcIVLVTE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDF-NIKLSDFSFSKRclrddsGR 168
Cdd:cd14032  85 LMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATL------KR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVLQgiPYQPKVYDIWSLGVILYIMVCGSMPYDD-SNIKKMLRI-------QKEHRVNFPRSKH 240
Cdd:cd14032 159 ASFAKSVIGTPEFMAPEMYE--EHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKvtcgikpASFEKVTDPEIKE 236
                       250       260       270
                ....*....|....*....|....*....|.
gi 14042947 241 LTGECkdliyhmLQPDVNRRLHIDEILSHCW 271
Cdd:cd14032 237 IIGEC-------ICKNKEERYEIKDLLSHAF 260
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
14-254 1.55e-12

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 67.73  E-value: 1.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAYS-----ERLK--FNVAIKIIDRKKAPADFLEkfLPREIEILAML-NHCSIIKTYEIFeTSHGK 85
Cdd:cd05101  28 LGKPLGEGCFGQVVMAEAvgidkDKPKeaVTVAVKMLKDDATEKDLSD--LVSEMEMMKMIgKHKNIINLLGAC-TQDGP 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 VYIVMELAVQGDLLELIKTRGALHED---------EARKKF-------HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN 149
Cdd:cd05101 105 LYVIVEYASKGNLREYLRARRPPGMEysydinrvpEEQMTFkdlvsctYQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 150 IKLSDFSFSkrclRDDSGRMALSKTFCGS-PA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLR 226
Cdd:cd05101 185 MKIADFGLA----RDINNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQS-DVWSFGVLMWeIFTLGGSPYPGIPVEELFK 259
                       250       260
                ....*....|....*....|....*....
gi 14042947 227 IQKE-HRVNFPrskhltGECKDLIYHMLQ 254
Cdd:cd05101 260 LLKEgHRMDKP------ANCTNELYMMMR 282
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
123-283 1.60e-12

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: 67.06  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 123 AIKYCHD-LDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDDsgrmaLSKTF-CGSPAYAAPEVLQGiPYQPKVY--- 197
Cdd:cd06617 115 ALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGISGY-LVDS-----VAKTIdAGCKPYMAPERINP-ELNQKGYdvk 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 198 -DIWSLGVILYIMVCGSMPYDD--SNIKKMLRIQKEHRVNFPRSKhLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQP 274
Cdd:cd06617 188 sDVWSLGITMIELATGRFPYDSwkTPFQQLKQVVEEPSPQLPAEK-FSPEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266

                ....*....
gi 14042947 275 KARGSPSVA 283
Cdd:cd06617 267 HLSKNTDVA 275
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
7-280 1.61e-12

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: 67.37  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAY-----SERLKFNVAIKIIdrkKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFET 81
Cdd:cd05093   2 IKRHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL---KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHgKVYIVMELAVQGDLLELIKTRGA-------------LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDF 148
Cdd:cd05093  79 GD-PLIMVFEYMKHGDLNKFLRAHGPdavlmaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 149 NIKLSDFSFSKRCLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLRI 227
Cdd:cd05093 158 LVKIGDFGMSRDVYSTDYYRVGGHTML--PIRWMPPESIMYRKFTTES-DVWSLGVVLWeIFTYGKQPWYQLSNNEVIEC 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 14042947 228 QKEHRVnFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEIlsHCWMQPKARGSP 280
Cdd:cd05093 235 ITQGRV-LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEI--HSLLQNLAKASP 284
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
18-227 1.84e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 67.15  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMELaVQGD 97
Cdd:PLN00009  10 IGEGTYGVVYKARDRVTNETIALKKI-RLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVH-SEKRLYLVFEY-LDLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   98 LLELIKTRGALHEDEARKK--FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN-IKLSDFsfskrclrddsgrmALSKT 174
Cdd:PLN00009  87 LKKHMDSSPDFAKNPRLIKtyLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADF--------------GLARA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947  175 FcGSPA-----------YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRI 227
Cdd:PLN00009 153 F-GIPVrtfthevvtlwYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFpGDSEIDELFKI 216
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
18-155 1.89e-12

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: 64.00  E-value: 1.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadfLEKFLPREIEILAML-NHCSIIKTYEIFETSHGKVYIVMELAVQG 96
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNE---EGEDLESEMDILRRLkGLELNIPKVLVTEDVDGPNILLMELVKGG 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947  97 DLLELIkTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDF 155
Cdd:cd13968  78 TLIAYT-QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDF 135
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
3-300 1.98e-12

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: 66.63  E-value: 1.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   3 DAAVLKRRGYLLGINLGEGSYAKV-KSAYSERLKfnVAIKIIDR-KKAPADFLEkflprEIEILAMLNHCSIIKTYEIfe 80
Cdd:cd05070   2 DVWEIPRESLQLIKRLGNGQFGEVwMGTWNGNTK--VAIKTLKPgTMSPESFLE-----EAQIMKKLKHDKLVQLYAV-- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  81 TSHGKVYIVMELAVQGDLLELIKTRG--ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05070  73 VSEEPIYIVTEYMSKGSLLDFLKDGEgrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 kRCLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC-GSMPYDDSNIKKML-RIQKEHRVNFP 236
Cdd:cd05070 153 -RLIEDNEYTARQGAKF--PIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMNNREVLeQVERGYRMPCP 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 237 RskhltgeckdliyhmlqpDVNRRLHidEILSHCWMQ-PKARGSPSVAINKEGESSRGTEPLWTP 300
Cdd:cd05070 229 Q------------------DCPISLH--ELMIHCWKKdPEERPTFEYLQGFLEDYFTATEPQYQP 273
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
59-216 2.56e-12

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: 66.21  E-value: 2.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEI-FETSHgkVYIVMELAVQGDL-LELIKTRGALHEDEARK-KFH-------QLSLAIKYCH 128
Cdd:cd14146  42 QEAKLFSMLRHPNIIKLEGVcLEEPN--LCLVMEFARGGTLnRALAAANAAPGPRRARRiPPHilvnwavQIARGMLYLH 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 129 D---LDVVHRDLKCDN-LLLDK-------DFNIKLSDFSFSKRCLRddSGRMALSKTFcgspAYAAPEVLQGIPYQpKVY 197
Cdd:cd14146 120 EeavVPILHRDLKSSNiLLLEKiehddicNKTLKITDFGLAREWHR--TTKMSAAGTY----AWMAPEVIKSSLFS-KGS 192
                       170
                ....*....|....*....
gi 14042947 198 DIWSLGVILYIMVCGSMPY 216
Cdd:cd14146 193 DIWSYGVLLWELLTGEVPY 211
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
18-261 2.86e-12

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: 66.55  E-value: 2.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGkVYIVMELAVQGD 97
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDA-LCLVLTIMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFH--QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDS--GRMalsk 173
Cdd:cd05631  87 LKFHIYNMGNPGFDEQRAIFYaaELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETvrGRV---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 174 tfcGSPAYAAPEVLQGIPY--QPkvyDIWSLGVILYIMVCGSMPYDDSNiKKMLRIQKEHRVNFPR---SKHLTGECKDL 248
Cdd:cd05631 163 ---GTVGYMAPEVINNEKYtfSP---DWWGLGCLIYEMIQGQSPFRKRK-ERVKREEVDRRVKEDQeeySEKFSEDAKSI 235
                       250
                ....*....|...
gi 14042947 249 IYHMLQPDVNRRL 261
Cdd:cd05631 236 CRMLLTKNPKERL 248
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
16-269 3.54e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 65.79  E-value: 3.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFlPREIEILAMLNHCSIIKTYEIFETS---HGKVYIVMEL 92
Cdd:cd14033   7 IEIGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRF-SEEVEMLKGLQHPNIVRFYDSWKSTvrgHKCIILVTEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDL--DVVHRDLKCDNLLLD-KDFNIKLSDFSFSKrcLRddsgRM 169
Cdd:cd14033  86 MTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGLAT--LK----RA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 170 ALSKTFCGSPAYAAPEVLQGiPYQPKVyDIWSLGVILYIMVCGSMPYDDSN--------IKKMLRIQKEHRVNFPrskhl 241
Cdd:cd14033 160 SFAKSVIGTPEFMAPEMYEE-KYDEAV-DVYAFGMCILEMATSEYPYSECQnaaqiyrkVTSGIKPDSFYKVKVP----- 232
                       250       260
                ....*....|....*....|....*...
gi 14042947 242 tgECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14033 233 --ELKEIIEGCIRTDKDERFTIQDLLEH 258
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
39-216 4.00e-12

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: 65.88  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  39 AIKIIDRKKAP--ADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQ--GDLLE--LIKTRGALHEDE 112
Cdd:cd14001  32 AVKKINSKCDKgqRSLYQERLKEEAKILKSLNHPNIVGFRAFTKSEDGSLCLAMEYGGKslNDLIEerYEAGLGPFPAAT 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 113 ARKKFHQLSLAIKYCH-DLDVVHRDLKCDNLLLDKDFN-IKLSDFSFSKRClrDDSGRMALSKTFC--GSPAYAAPEVL- 187
Cdd:cd14001 112 ILKVALSIARALEYLHnEKKILHGDIKSGNVLIKGDFEsVKLCDFGVSLPL--TENLEVDSDPKAQyvGTEPWKAKEALe 189
                       170       180
                ....*....|....*....|....*....
gi 14042947 188 QGIPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd14001 190 EGGVITDKA-DIFAYGLVLWEMMTLSVPH 217
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
20-269 4.99e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 65.42  E-value: 4.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  20 EGSYAKVKSAYSERLKFNVAIKIIDrkkapadfLEKFLPREIEILAMLNHCSIIKTYEIF---ETSHgkvyIVMELAVQG 96
Cdd:cd13995  14 RGAFGKVYLAQDTKTKKRMACKLIP--------VEQFKPSDVEIQACFRHENIAELYGALlweETVH----LFMEAGEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIkLSDFSFSKRcLRDDsgrMALSKTFC 176
Cdd:cd13995  82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQ-MTED---VYVPKDLR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMP----YDDSNIKKMLRIQKEHRvnfPRSKHLTGEC----KDL 248
Cdd:cd13995 157 GTEIYMSPEVILCRGHNTKA-DIYSLGATIIHMQTGSPPwvrrYPRSAYPSYLYIIHKQA---PPLEDIAQDCspamREL 232
                       250       260
                ....*....|....*....|.
gi 14042947 249 IYHMLQPDVNRRLHIDEILSH 269
Cdd:cd13995 233 LEAALERNPNHRSSAAELLKH 253
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
18-229 6.82e-12

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: 65.24  E-value: 6.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKiidrkKAPADFLEKFLP----REIEILAMLNH----CSIIKTYEIFETSHGKVYIV 89
Cdd:cd07837   9 IGEGTYGKVYKARDKNTGKLVALK-----KTRLEMEEEGVPstalREVSLLQMLSQsiyiVRLLDVEHVEENGKPLLYLV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELaVQGDLLELIKT--RGALHEDEAR--KKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNI-KLSDFSFSKrclr 163
Cdd:cd07837  84 FEY-LDTDLKKFIDSygRGPHNPLPAKtiQSFmYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGR---- 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 164 ddsgrmALS---KTFCGSPA---YAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPY-DDSNIKKMLRIQK 229
Cdd:cd07837 159 ------AFTipiKSYTHEIVtlwYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFpGDSELQQLLHIFR 225
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-254 6.86e-12

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 65.06  E-value: 6.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSER--LKFNVAIKIIDRKKAPADflEKFLPREIEILAML-NHCSIIKTYEIFEtSHGKVYIVMELAV 94
Cdd:cd05047   3 IGEGNFGQVLKARIKKdgLRMDAAIKRMKEYASKDD--HRDFAGELEVLCKLgHHPNIINLLGACE-HRGYLYLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFH----------------QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05047  80 HGNLLDFLRKSRVLETDPAFAIANstastlssqqllhfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KrclrddSGRMALSKTFCGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKML-RIQKEHRVNF 235
Cdd:cd05047 160 R------GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNS-DVWSYGVLLWeIVSLGGTPYCGMTCAELYeKLPQGYRLEK 232
                       250
                ....*....|....*....
gi 14042947 236 PRSkhltgeCKDLIYHMLQ 254
Cdd:cd05047 233 PLN------CDDEVYDLMR 245
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
7-238 8.07e-12

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 65.43  E-value: 8.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYS---ERLKFN----VAIKIIDRKKAPADFLEkfLPREIEILAML-NHCSIIKTYEI 78
Cdd:cd05100   9 LSRTRLTLGKPLGEGCFGQVVMAEAigiDKDKPNkpvtVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLGA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FeTSHGKVYIVMELAVQGDLLELIKTRGA-----------LHEDEARKK-----FHQLSLAIKYCHDLDVVHRDLKCDNL 142
Cdd:cd05100  87 C-TQDGPLYVLVEYASKGNLREYLRARRPpgmdysfdtckLPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLAARNV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 143 LLDKDFNIKLSDFSFSKRCLRDD------SGRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMP 215
Cdd:cd05100 166 LVTEDNVMKIADFGLARDVHNIDyykkttNGRLPVK--------WMAPEALFDRVYTHQS-DVWSFGVLLWeIFTLGGSP 236
                       250       260
                ....*....|....*....|....
gi 14042947 216 YDDSNIKKMLRIQKE-HRVNFPRS 238
Cdd:cd05100 237 YPGIPVEELFKLLKEgHRMDKPAN 260
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
17-224 8.98e-12

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 64.95  E-value: 8.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVK----SAYSERLKFNVAIKII---DRKKAPADflekfLPREIEILAMLNHCSIIKTYEIFETSHGK-VYI 88
Cdd:cd05079  11 DLGEGHFGKVElcryDPEGDNTGEQVAVKSLkpeSGGNHIAD-----LKKEIEILRNLYHENIVKYKGICTEDGGNgIKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrCLRDDSG 167
Cdd:cd05079  86 IMEFLPSGSLKEyLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKE 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14042947 168 RMALsKTFCGSPAY-AAPEVLqgipYQPKVY---DIWSLGVILYIMvcgsMPYDDSNIKKM 224
Cdd:cd05079 165 YYTV-KDDLDSPVFwYAPECL----IQSKFYiasDVWSFGVTLYEL----LTYCDSESSPM 216
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
53-210 1.04e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 65.87  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   53 LEKFLPREIEILAMLNHCSIIKTYEIFEtSHGKVYIVMElAVQGDLLELIKTRGALHED-----EARKKFHQLSLAIKYC 127
Cdd:PHA03210 206 AAIQLENEILALGRLNHENILKIEEILR-SEANTYMITQ-KYDFDLYSFMYDEAFDWKDrpllkQTRAIMKQLLCAVEYI 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  128 HDLDVVHRDLKCDNLLLDKDFNIKLSDF----SFSKRclrddsgRMALSKTFCGSPAYAAPEVLQGIPYqPKVYDIWSLG 203
Cdd:PHA03210 284 HDKKLIHRDIKLENIFLNCDGKIVLGDFgtamPFEKE-------REAFDYGWVGTVATNSPEILAGDGY-CEITDIWSCG 355

                 ....*..
gi 14042947  204 VILYIMV 210
Cdd:PHA03210 356 LILLDML 362
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-231 1.07e-11

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: 64.51  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrkkaPADF---LEKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVME--- 91
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVI-----PLDItveLQKQIMSELEILYKCDSPYIIGFYGAFFVEN-RISICTEfmd 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 ---LAVQGDLLELIKTRGALhedearkkfhQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRddsgr 168
Cdd:cd06619  83 ggsLDVYRKIPEHVLGRIAV----------AVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN----- 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 169 mALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYddsnikkmLRIQKEH 231
Cdd:cd06619 148 -SIAKTYVGTNAYMAPERISGEQYGIHS-DVWSLGISFMELALGRFPY--------PQIQKNQ 200
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
18-217 1.10e-11

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: 64.44  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFN--VAIKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVyIVMELAVQ 95
Cdd:cd14664   1 IGRGGAGTV---YKGVMPNGtlVAVKRLKGEGTQGG--DHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNL-LVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSL----AIKYCHD---LDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGR 168
Cdd:cd14664  75 GSLGELLHSRPESQPPLDWETRQRIALgsarGLAYLHHdcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHV 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 169 MAlskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYD 217
Cdd:cd14664 155 MS---SVAGSYGYIAPEYAYTGKVSEKS-DVYSYGVVLLELITGKRPFD 199
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
18-225 1.19e-11

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 64.34  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFNVAIKIIDRKKAPADFLEKFlPREIEILAMLNHCSIIktyeIFE--TSHGKVYIVME---- 91
Cdd:cd14062   1 IGSGSFGTV---YKGRWHGDVAVKKLNVTDPTPSQLQAF-KNEVAVLRKTRHVNIL----LFMgyMTKPQLAIVTQwceg 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 ---------LAVQGDLLELIktrgalheDEARkkfhQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCL 162
Cdd:cd14062  73 sslykhlhvLETKFEMLQLI--------DIAR----QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKT 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 163 RDDSGRMALSKTfcGSPAYAAPEVLQ---GIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKML 225
Cdd:cd14062 141 RWSGSQQFEQPT--GSILWMAPEVIRmqdENPYSFQS-DVYAFGIVLYELLTGQLPYSHINNRDQI 203
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
118-247 1.59e-11

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: 64.22  E-value: 1.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 118 HQLSLAIKYCHDLDVVHRDLKCDNLLL-----DKDFNIKLSDFSFSKRCLRDdsGRMALSktfcGSPAYAAPEVLQGIPY 192
Cdd:cd14067 121 YQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHE--GALGVE----GTPGYQAPEIRPRIVY 194
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 193 QPKVyDIWSLGVILYIMVCGSMP---YDDSNIKKMLR------IQKEHRVNFPRSKHLTGECKD 247
Cdd:cd14067 195 DEKV-DMFSYGMVLYELLSGQRPslgHHQLQIAKKLSkgirpvLGQPEEVQFFRLQALMMECWD 257
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
18-268 1.60e-11

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: 64.12  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAyseRLK------FNVAIKIID---RKKAPADFLekflpREIEILAMLNHCSIIKtYEIFETSHGKVYI 88
Cdd:cd05066  12 IGAGEFGEVCSG---RLKlpgkreIPVAIKTLKagyTEKQRRDFL-----SEASIMGQFDHPNIIH-LEGVVTRSKPVMI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSg 167
Cdd:cd05066  83 VTEYMENGSLDAFLRKHdGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLS-RVLEDDP- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMALSKTFCGSPA-YAAPEvlqGIPYQ--PKVYDIWSLGVILY-IMVCGSMPY-DDSNIKKMLRIQKEHRVnfPRSKHLT 242
Cdd:cd05066 161 EAAYTTRGGKIPIrWTAPE---AIAYRkfTSASDVWSYGIVMWeVMSYGERPYwEMSNQDVIKAIEEGYRL--PAPMDCP 235
                       250       260
                ....*....|....*....|....*.
gi 14042947 243 GECKDLIYHMLQPDVNRRLHIDEILS 268
Cdd:cd05066 236 AALHQLMLDCWQKDRNERPKFEQIVS 261
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
18-277 1.93e-11

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 63.67  E-value: 1.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK----IIDRKKAPADFLEkflprEIEILAMLNHCSIIKTYEIFETSHGkvyIVMELA 93
Cdd:cd14025   4 VGSGGFGQVYKVRHKHWKTWLAIKcppsLHVDDSERMELLE-----EAKKMEMAKFRHILPVYGICSEPVG---LVMEYM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTrgalHEDEARKKF---HQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLRDDSGR 168
Cdd:cd14025  76 ETGSLEKLLAS----EPLPWELRFriiHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAK--WNGLSHS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSK-TFCGSPAYAAPEVL--QGIPYQPKvYDIWSLGVILYIMVCGSMPYDDSN--IKKMLRIQKEHRVNFPR-SKHLT 242
Cdd:cd14025 150 HDLSRdGLRGTIAYLPPERFkeKNRCPDTK-HDVYSFAIVIWGILTQKKPFAGENniLHIMVKVVKGHRPSLSPiPRQRP 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 14042947 243 GECKDLIYHMLQpdvnrrlhideilshCWMQ-PKAR 277
Cdd:cd14025 229 SECQQMICLMKR---------------CWDQdPRKR 249
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
18-207 2.25e-11

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: 63.88  E-value: 2.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFN----VAIKIIdrKKAPADFLEKFlPREIEILAMLNHCSIIKTYEI-FETSHGKVYIVMEL 92
Cdd:cd14205  12 LGKGNFGSVEMCRYDPLQDNtgevVAVKKL--QHSTEEHLRDF-EREIEILKSLQHDNIVKYKGVcYSAGRRNLRLIMEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAl 171
Cdd:cd14205  89 LPYGSLRDyLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKV- 167
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14042947 172 sKTFCGSPAY-AAPEVLQGIPYQpKVYDIWSLGVILY 207
Cdd:cd14205 168 -KEPGESPIFwYAPESLTESKFS-VASDVWSFGVVLY 202
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
14-220 2.41e-11

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 63.54  E-value: 2.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVksaYSERLKFNVAIKIIDRKKAPADFLEKFlPREIEILAMLNHCSIIktYEIFETSHGKVYIVMELA 93
Cdd:cd14151  12 VGQRIGSGSFGTV---YKGKWHGDVAVKMLNVTAPTPQQLQAF-KNEVGVLRKTRHVNIL--LFMGYSTKPQLAIVTQWC 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDL---LELIKTRGALHE--DEARkkfhQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrcLRDDSGR 168
Cdd:cd14151  86 EGSSLyhhLHIIETKFEMIKliDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG-----LATVKSR 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 169 MALSKTF---CGSPAYAAPEVLQGIPYQPKVY--DIWSLGVILYIMVCGSMPYDDSN 220
Cdd:cd14151 157 WSGSHQFeqlSGSILWMAPEVIRMQDKNPYSFqsDVYAFGIVLYELMTGQLPYSNIN 213
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
18-224 3.56e-11

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: 63.53  E-value: 3.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPA--IRNQIIRELQVLHECNSPYIVGFYGAF-YSDGEISICMEHMDGGS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGALHEDEARKKFHQLSLAIKYCHDL-DVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRddsgrmALSKTFC 176
Cdd:cd06649  90 LDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID------SMANSFV 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 177 GSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSNIKKM 224
Cdd:cd06649 164 GTRSYMSPERLQGTHYSVQS-DIWSMGLSLVELAIGRYPIPPPDAKEL 210
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
18-206 3.79e-11

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: 62.51  E-value: 3.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLekflpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFL-----KEVKLMRRLSHPNILRFIGVC-VKDNKLNFITEYVNGGT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIK---------TRGALHEDEARkkfhqlslAIKYCHDLDVVHRDLKCDNLLL---DKDFNIKLSDFSFSKRC--LR 163
Cdd:cd14065  75 LEELLKsmdeqlpwsQRVSLAKDIAS--------GMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMpdEK 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14042947 164 DDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14065 147 TKKPDRKKRLTVVGSPYWMAPEMLRGESYDEKV-DVFSFGIVL 188
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
18-216 4.71e-11

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: 62.41  E-value: 4.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLkfnVAIKI--IDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEI-FETSHgkVYIVMELA 93
Cdd:cd14061   2 IGVGGFGKVyRGIWRGEE---VAVKAarQDPDEDISVTLENVR-QEARLFWMLRHPNIIALRGVcLQPPN--LCLVMEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 vQGdlleliktrGALHEDEARKKFH---------QLSLAIKYCHD---LDVVHRDLKCDNLLLDKDFN--------IKLS 153
Cdd:cd14061  76 -RG---------GALNRVLAGRKIPphvlvdwaiQIARGMNYLHNeapVPIIHRDLKSSNILILEAIEnedlenktLKIT 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 154 DFSFSKRCLRddSGRMALSKTFcgspAYAAPEVLQGIPYQpKVYDIWSLGVILYIMVCGSMPY 216
Cdd:cd14061 146 DFGLAREWHK--TTRMSAAGTY----AWMAPEVIKSSTFS-KASDVWSYGVLLWELLTGEVPY 201
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
37-277 5.05e-11

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: 62.24  E-value: 5.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  37 NVAIKIIDR-KKAPADFLEkflprEIEILAMLNHCSIIKTYEIfeTSHGKVYIVMELAVQGDLLELIKTRG--ALHEDEA 113
Cdd:cd14203  21 KVAIKTLKPgTMSPEAFLE-----EAQIMKKLRHDKLVQLYAV--VSEEPIYIVTEFMSKGSLLDFLKDGEgkYLKLPQL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 114 RKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQ 193
Cdd:cd14203  94 VDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA-RLIEDNEYTARQGAKF--PIKWTAPEAALYGRFT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 194 PKVyDIWSLGVILYIMVC-GSMPYDDSNIKKML-RIQKEHRVNFPrskhltgeckdliyhmlqPDVNRRLHidEILSHCW 271
Cdd:cd14203 171 IKS-DVWSFGILLTELVTkGRVPYPGMNNREVLeQVERGYRMPCP------------------PGCPESLH--ELMCQCW 229

                ....*..
gi 14042947 272 -MQPKAR 277
Cdd:cd14203 230 rKDPEER 236
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
18-283 5.49e-11

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: 62.19  E-value: 5.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAySERLKFNVAIKIIDR-KKAPADFLEkflprEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQG 96
Cdd:cd05114  12 LGSGLFGVVRLG-KWRAQYKVAIKAIREgAMSEEDFIE-----EAKVMMKLTHPKLVQLYGVC-TQQKPIYIVTEFMENG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLrDDSGRMALSKTF 175
Cdd:cd05114  85 CLLNYLRQRrGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVL-DDQYTSSSGAKF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 176 cgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPrskHLTGEckdliyhml 253
Cdd:cd05114 164 --PVKWSPPEVFNYSKFSSKS-DVWSFGVLMWeVFTEGKMPFESkSNYEVVEMVSRGHRLYRP---KLASK--------- 228
                       250       260       270
                ....*....|....*....|....*....|
gi 14042947 254 qpdvnrrlHIDEILSHCWmQPKARGSPSVA 283
Cdd:cd05114 229 --------SVYEVMYSCW-HEKPEGRPTFA 249
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
18-204 7.89e-11

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: 61.98  E-value: 7.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPAdflEKFLPREIEILAMLN--HCSIIKTYEIFeTSHGKVYIVMELAVQ 95
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELAAIKVI--KLEPG---EDFAVVQQEIIMMKDckHSNIVAYFGSY-LRRDKLWICMEFCGG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRClrddSGRMALSKTF 175
Cdd:cd06645  93 GSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQI----TATIAKRKSF 168
                       170       180       190
                ....*....|....*....|....*....|.
gi 14042947 176 CGSPAYAAPEV--LQGIPYQPKVYDIWSLGV 204
Cdd:cd06645 169 IGTPYWMAPEVaaVERKGGYNQLCDIWAVGI 199
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
38-216 8.01e-11

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: 62.04  E-value: 8.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIDRKKA-PADFLekflpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRG-ALHEDEARK 115
Cdd:cd05068  35 VAVKTLKPGTMdPEDFL-----REAQIMKKLRHPKLIQLYAVC-TLEEPIYIITELMKHGSLLEYLQGKGrSLQLPQLID 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 116 KFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKTFcgsP-AYAAPEVLQGIPYQP 194
Cdd:cd05068 109 MAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREGAKF---PiKWTAPEAANYNRFSI 185
                       170       180
                ....*....|....*....|...
gi 14042947 195 KVyDIWSLGVILY-IMVCGSMPY 216
Cdd:cd05068 186 KS-DVWSFGILLTeIVTYGRIPY 207
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
18-277 8.39e-11

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: 61.83  E-value: 8.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKfNVAIKIIDR-KKAPADFLEkflprEIEILAMLNHCSIIKTYEIfeTSHGKVYIVMELAVQG 96
Cdd:cd05067  15 LGAGQFGEVWMGYYNGHT-KVAIKSLKQgSMSPDAFLA-----EANLMKQLQHQRLVRLYAV--VTQEPIYIITEYMENG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGA--LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMALSKT 174
Cdd:cd05067  87 SLVDFLKTPSGikLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLA-RLIEDNEYTAREGAK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLRiqkehrvNFPRSkhltgeckdliYHML 253
Cdd:cd05067 166 F--PIKWTAPEAINYGTFTIKS-DVWSFGILLTeIVTHGRIPYPGMTNPEVIQ-------NLERG-----------YRMP 224
                       250       260
                ....*....|....*....|....*
gi 14042947 254 QPDvNRRLHIDEILSHCWM-QPKAR 277
Cdd:cd05067 225 RPD-NCPEELYQLMRLCWKeRPEDR 248
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-216 1.02e-10

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: 61.92  E-value: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGINLGEGSYAKVKSAYSERL---------KFN-----VAIKIID---RKKAPADFLekflpREIEILAMLNHCS 71
Cdd:cd05097   4 RQQLRLKEKLGEGQFGEVHLCEAEGLaeflgegapEFDgqpvlVAVKMLRadvTKTARNDFL-----KEIKIMSRLKNPN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  72 IIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRgalhedEARKKFH------------------QLSLAIKYCHDLDVV 133
Cdd:cd05097  79 IIRLLGVC-VSDDPLCMITEYMENGDLNQFLSQR------EIESTFThannipsvsianllymavQIASGMKYLASLNFV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 134 HRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDD----SGR-------MALSKTFCGSPAYAApevlqgipyqpkvyDIWSL 202
Cdd:cd05097 152 HRDLATRNCLVGNHYTIKIADFGMSRNLYSGDyyriQGRavlpirwMAWESILLGKFTTAS--------------DVWAF 217
                       250
                ....*....|....*.
gi 14042947 203 GVILYIM--VCGSMPY 216
Cdd:cd05097 218 GVTLWEMftLCKEQPY 233
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
18-209 1.59e-10

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: 61.13  E-value: 1.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdRKKAPADFLEKFLPREIEILAML---NHCSIIKTYEIFETSHG----KVYIVM 90
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKSV-RVQTNEDGLPLSTVREVALLKRLeafDHPNIVRLMDVCATSRTdretKVTLVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ElAVQGDL---LELIKTRGaLHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrclRDDSG 167
Cdd:cd07863  87 E-HVDQDLrtyLDKVPPPG-LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA----RIYSC 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 14042947 168 RMALSKTFCgSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIM 209
Cdd:cd07863 161 QMALTPVVV-TLWYRAPEVLLQSTYATPV-DMWSVGCIFAEM 200
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
18-268 2.08e-10

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: 60.65  E-value: 2.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLK------FNVAIKIID---RKKAPADFLEkflprEIEILAMLNHCSIIKtYEIFETSHGKVYI 88
Cdd:cd05065  12 IGAGEFGEV---CRGRLKlpgkreIFVAIKTLKsgyTEKQRRDFLS-----EASIMGQFDHPNIIH-LEGVVTKSRPVMI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSG 167
Cdd:cd05065  83 ITEFMENGALDSFLRQNdGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLS-RFLEDDTS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 168 RMALSKTFCGS-PA-YAAPEVLQGIPYQpKVYDIWSLGVILY-IMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRskhltg 243
Cdd:cd05065 162 DPTYTSSLGGKiPIrWTAPEAIAYRKFT-SASDVWSYGIVMWeVMSYGERPYwDMSNQDVINAIEQDYRLPPPM------ 234
                       250       260
                ....*....|....*....|....*....
gi 14042947 244 ECKDLIYHML----QPDVNRRLHIDEILS 268
Cdd:cd05065 235 DCPTALHQLMldcwQKDRNLRPKFGQIVN 263
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
16-273 2.27e-10

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: 60.83  E-value: 2.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSYAKVKSAYSERLKFNVA-IKIIDRKKAPADflEKFLPREIEILAMLNHCSIIKTYEIFE-TSHGK--VYIVME 91
Cdd:cd14030  31 IEIGRGSFKTVYKGLDTETTVEVAwCELQDRKLSKSE--RQRFKEEAGMLKGLQHPNIVRFYDSWEsTVKGKkcIVLVTE 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD--VVHRDLKCDNLLLDKDF-NIKLSDFSFSKRclrddsGR 168
Cdd:cd14030 109 LMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATL------KR 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 169 MALSKTFCGSPAYAAPEVLQGiPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSKHLTGECKD 247
Cdd:cd14030 183 ASFAKSVIGTPEFMAPEMYEE-KYDESV-DVYAFGMCMLEMATSEYPYSEcQNAAQIYRRVTSGVKPASFDKVAIPEVKE 260
                       250       260
                ....*....|....*....|....*.
gi 14042947 248 LIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:cd14030 261 IIEGCIRQNKDERYAIKDLLNHAFFQ 286
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
3-249 2.49e-10

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 60.42  E-value: 2.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   3 DAAVLKRRGYLLGINLGEGSYAKVKSA-YSERLKfnVAIKIIdrkKAPADFLEKFLpREIEILAMLNHCSIIKTYEIfeT 81
Cdd:cd05073   4 DAWEIPRESLKLEKKLGAGQFGEVWMAtYNKHTK--VAVKTM---KPGSMSVEAFL-AEANVMKTLQHDKLVKLHAV--V 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHGKVYIVMELAVQGDLLELIKTrgalheDEARKK--------FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLS 153
Cdd:cd05073  76 TKEPIYIITEFMAKGSLLDFLKS------DEGSKQplpklidfSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 154 DFSFSkRCLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLRiQKEHR 232
Cdd:cd05073 150 DFGLA-RVIEDNEYTAREGAKF--PIKWTAPEAINFGSFTIKS-DVWSFGILLMeIVTYGRIPYPGMSNPEVIR-ALERG 224
                       250
                ....*....|....*..
gi 14042947 233 VNFPRSKHLTGECKDLI 249
Cdd:cd05073 225 YRMPRPENCPEELYNIM 241
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
119-281 2.49e-10

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 60.54  E-value: 2.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 119 QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSK-------RCLRDDSGRmalsktfcgsP-AYAAPEVLQGi 190
Cdd:cd05043 124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRdlfpmdyHCLGDNENR----------PiKWMSLESLVN- 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 191 pyqpKVY----DIWSLGVILY-IMVCGSMPYDDSNIKKMLR-IQKEHRVNFPRSkhltgeCKDLIYhmlqpdvnrrlhid 264
Cdd:cd05043 193 ----KEYssasDVWSFGVLLWeLMTLGQTPYVEIDPFEMAAyLKDGYRLAQPIN------CPDELF-------------- 248
                       170
                ....*....|....*...
gi 14042947 265 EILSHCW-MQPKARGSPS 281
Cdd:cd05043 249 AVMACCWaLDPEERPSFQ 266
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
18-217 3.33e-10

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: 60.81  E-value: 3.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPADFLEKFLprEIEILAML-----NHCSIIKTYEIFE-TSHgkVYIVME 91
Cdd:cd14229   8 LGRGTFGQVVKCWKRGTNEIVAVKIL--KNHPSYARQGQI--EVGILARLsnenaDEFNFVRAYECFQhRNH--TCLVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQgDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRCLRdd 165
Cdd:cd14229  82 MLEQ-NLYDFLKQNkfSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSK-- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 166 sgrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL------YIMVCGSMPYD 217
Cdd:cd14229 159 ----TVCSTYLQSRYYRAPEIILGLPFCEAI-DMWSLGCVIaelflgWPLYPGALEYD 211
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
3-254 3.53e-10

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: 60.09  E-value: 3.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   3 DAAVLKRRGYLLGINLGEGSYAKVKSAyserlKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIfeTS 82
Cdd:cd05069   5 DAWEIPRESLRLDVKLGQGCFGEVWMG-----TWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAV--VS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  83 HGKVYIVMELAVQGDLLELIKTRGALHED--EARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkR 160
Cdd:cd05069  78 EEPIYIVTEFMGKGSLLDFLKEGDGKYLKlpQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLA-R 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 CLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC-GSMPYDDSNIKKML-RIQKEHRVNFPRS 238
Cdd:cd05069 157 LIEDNEYTARQGAKF--PIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMVNREVLeQVERGYRMPCPQG 233
                       250
                ....*....|....*.
gi 14042947 239 khltgeCKDLIYHMLQ 254
Cdd:cd05069 234 ------CPESLHELMK 243
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
119-237 3.76e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.06  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  119 QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVyD 198
Cdd:PHA03211 268 QLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAA--CFARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSV-D 344
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 14042947  199 IWSLGVILYIMVCG-----SMPYD------DSNIKKMLRIQKEHRVNFPR 237
Cdd:PHA03211 345 IWSAGLVIFEAAVHtaslfSASRGderrpyDAQILRIIRQAQVHVDEFPQ 394
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
18-206 4.01e-10

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: 60.53  E-value: 4.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKApadfLEKFLPREIEILAML------NHCSIIKTYEIFeTSHGKVYIVME 91
Cdd:cd14224  73 IGKGSFGQVVKAYDHKTHQHVALKMVRNEKR----FHRQAAEEIRILEHLkkqdkdNTMNVIHMLESF-TFRNHICMTFE 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LaVQGDLLELIKtrgalhedeaRKKFHQLSLAI--KYCHD----LDVVHR------DLKCDNLLLDKD--FNIKLSDFSF 157
Cdd:cd14224 148 L-LSMNLYELIK----------KNKFQGFSLQLvrKFAHSilqcLDALHRnkiihcDLKPENILLKQQgrSGIKVIDFGS 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 158 SkrCLrdDSGRMAlskTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14224 217 S--CY--EHQRIY---TYIQSRFYRAPEVILGARYGMPI-DMWSFGCIL 257
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
38-254 4.28e-10

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 59.74  E-value: 4.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEI-FETShgKVYIVMELAVQGDLLELIktRGALHEDEARKK 116
Cdd:cd05044  29 VAVKTL-RKGATDQEKAEFL-KEAHLMSNFKHPNILKLLGVcLDND--PQYIILELMEGGDLLSYL--RAARPTAFTPPL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 117 F---HQLSLAI------KYCHDLDVVHRDLKCDNLLL-DKDFN---IKLSDFSFSKRCLRDDSGRMALSKTFcgsPA-YA 182
Cdd:cd05044 103 LtlkDLLSICVdvakgcVYLEDMHFVHRDLAARNCLVsSKDYRervVKIGDFGLARDIYKNDYYRKEGEGLL---PVrWM 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 183 APEVL-QGIPYQPKvyDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHRVNFPRSkhltgeCKDLIYHMLQ 254
Cdd:cd05044 180 APESLvDGVFTTQS--DVWAFGVLMWeILTLGQQPYPArNNLEVLHFVRAGGRLDQPDN------CPDDLYELML 246
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
124-214 4.63e-10

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: 59.43  E-value: 4.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 124 IKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRclrddsgRMALSKTFCGSPAYAAPEVLQGiPYQPKVyDIWSLG 203
Cdd:cd13975 115 IRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKP-------EAMMSGSIVGTPIHMAPELFSG-KYDNSV-DVYAFG 185
                        90
                ....*....|.
gi 14042947 204 VILYIMVCGSM 214
Cdd:cd13975 186 ILFWYLCAGHV 196
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
7-266 4.80e-10

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: 59.64  E-value: 4.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGINLGEGSYAKVKSAYSERL-----KFNVAIKIIdrkKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFeT 81
Cdd:cd05094   2 IKRRDIVLKRELGEGAFGKVFLAECYNLsptkdKMLVAVKTL---KDPTLAARKDFQREAELLTNLQHDHIVKFYGVC-G 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHGKVYIVMELAVQGDLLELIKTRGA----LHEDEARKKFHQLSLA------------IKYCHDLDVVHRDLKCDNLLLD 145
Cdd:cd05094  78 DGDPLIMVFEYMKHGDLNKFLRAHGPdamiLVDGQPRQAKGELGLSqmlhiatqiasgMVYLASQHFVHRDLATRNCLVG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 146 KDFNIKLSDFSFSKRCLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKM 224
Cdd:cd05094 158 ANLLVKIGDFGMSRDVYSTDYYRVGGHTML--PIRWMPPESIMYRKFTTES-DVWSFGVILWeIFTYGKQPWFQLSNTEV 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 14042947 225 LRIQKEHRVnFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEI 266
Cdd:cd05094 235 IECITQGRV-LERPRVCPKEVYDIMLGCWQREPQQRLNIKEI 275
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
3-236 5.41e-10

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: 59.70  E-value: 5.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   3 DAAVLKRRGYLLGINLGEGSYAKVksaysERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIfeTS 82
Cdd:cd05071   2 DAWEIPRESLRLEVKLGQGCFGEV-----WMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAV--VS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  83 HGKVYIVMELAVQGDLLELIK--TRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkR 160
Cdd:cd05071  75 EEPIYIVTEYMSKGSLLDFLKgeMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLA-R 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 161 CLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC-GSMPYDDSNIKKML-RIQKEHRVNFP 236
Cdd:cd05071 154 LIEDNEYTARQGAKF--PIKWTAPEAALYGRFTIKS-DVWSFGILLTELTTkGRVPYPGMVNREVLdQVERGYRMPCP 228
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
59-216 6.04e-10

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: 59.29  E-value: 6.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRgALHEDEARKKFHQLSLAIKYCHD---LDVVHR 135
Cdd:cd14145  54 QEAKLFAMLKHPNIIALRGVC-LKEPNLCLVMEFARGGPLNRVLSGK-RIPPDILVNWAVQIARGMNYLHCeaiVPVIHR 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 136 DLKCDNLLL-----DKDFN---IKLSDFSFSKRCLRddSGRMALSKTFcgspAYAAPEVLQGIPYQpKVYDIWSLGVILY 207
Cdd:cd14145 132 DLKSSNILIlekveNGDLSnkiLKITDFGLAREWHR--TTKMSAAGTY----AWMAPEVIRSSMFS-KGSDVWSYGVLLW 204

                ....*....
gi 14042947 208 IMVCGSMPY 216
Cdd:cd14145 205 ELLTGEVPF 213
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
25-269 6.55e-10

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: 59.26  E-value: 6.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  25 KVKSAYSERLKFNVAIKIIDRKKapadfLEKFLPREIEI-----------LAMLNHCSIIKTYEIFETSHGKVYIVMElA 93
Cdd:cd14011  11 KIYNGSKKSTKQEVSVFVFEKKQ-----LEEYSKRDREQilellkrgvkqLTRLRHPRILTVQHPLEESRESLAFATE-P 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLL-ELIKTR-----------GALHEDEARKKFHQLSLAIKYCH-DLDVVHRDLKCDNLLLDKDFNIKLSDFSFS-- 158
Cdd:cd14011  85 VFASLAnVLGERDnmpspppelqdYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCis 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 --------KRCLRDDSGRMALSKTfcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYD--------DSNI 221
Cdd:cd14011 165 seqatdqfPYFREYDPNLPPLAQP---NLNYLAPEYILSKTCDPAS-DMFSLGVLIYaIYNKGKPLFDcvnnllsyKKNS 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 222 KKMLRIQKEHRVNFPrskhltGECKDLIYHMLQPDVNRRLHIDEILSH 269
Cdd:cd14011 241 NQLRQLSLSLLEKVP------EELRDHVKTLLNVTPEVRPDAEQLSKI 282
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
59-206 7.24e-10

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: 59.20  E-value: 7.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQ-LSLAIKYCHDLDVVHRDL 137
Cdd:cd14221  39 KEVKVMRCLEHPNVLKFIGVLYKDK-RLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSFAKdIASGMAYLHSMNIIHRDL 117
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 138 KCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSK----------TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14221 118 NSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSlkkpdrkkryTVVGNPYWMAPEMINGRSYDEKV-DVFSFGIVL 195
PTZ00284 PTZ00284
protein kinase; Provisional
18-286 8.01e-10

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 59.98  E-value: 8.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   18 LGEGSYAKVKSAYSERLKFNVAIKIIDR-------KKAPADFLEKFLPREIEilamlNHCSIIKTYEIFETSHGKVYIVM 90
Cdd:PTZ00284 137 LGEGTFGKVVEAWDRKRKEYCAVKIVRNvpkytrdAKIEIQFMEKVRQADPA-----DRFPLMKIQRYFQNETGHMCIVM 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   91 ElAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCH-DLDVVHRDLKCDNLLLDKdfniklSDFSF---SKRCLRDDS 166
Cdd:PTZ00284 212 P-KYGPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHtELHLMHTDLKPENILMET------SDTVVdpvTNRALPPDP 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  167 GRMAL-----------SKT-FCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDD-SNIKKMLRIQK---- 229
Cdd:PTZ00284 285 CRVRIcdlggccderhSRTaIVSTRHYRSPEVVLGLGWMYST-DMWSMGCIIYELYTGKLLYDThDNLEHLHLMEKtlgr 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  230 ------------EHRVNFPRSKHLTgECK------------------------DLIYHMLQPDVNRRLHIDEILSHCWMQ 273
Cdd:PTZ00284 364 lpsewagrcgteEARLLYNSAGQLR-PCTdpkhlariararpvrevirddllcDLIYGLLHYDRQKRLNARQMTTHPYVL 442
                        330
                 ....*....|....*.
gi 14042947  274 ---PKARGSPSVAINK 286
Cdd:PTZ00284 443 kyyPECRQHPNYPDNR 458
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
18-216 9.56e-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: 58.46  E-value: 9.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKfLPREIEILAMLNHCSIIKTYEI-FETSHgkVYIVMELAvQG 96
Cdd:cd14148   2 IGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTAEN-VRQEARLFWMLQHPNIIALRGVcLNPPH--LCLVMEYA-RG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 dlleliktrGALHEDEARKKFH---------QLSLAIKYCHD---LDVVHRDLKCDNLL-LDK-------DFNIKLSDFS 156
Cdd:cd14148  78 ---------GALNRALAGKKVPphvlvnwavQIARGMNYLHNeaiVPIIHRDLKSSNILiLEPienddlsGKTLKITDFG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 157 FSKRCLRddSGRMALSKTFcgspAYAAPEVLQgIPYQPKVYDIWSLGVILYIMVCGSMPY 216
Cdd:cd14148 149 LAREWHK--TTKMSAAGTY----AWMAPEVIR-LSLFSKSSDVWSFGVLLWELLTGEVPY 201
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
9-226 1.08e-09

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 59.04  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   9 RRGYLLGINLGEGSYAKVKSAYS-----ERLKFNVAIKIIdrkKAPADFLEK-FLPREIEILAML-NHCSIIKTYEIFeT 81
Cdd:cd05055  34 RNNLSFGKTLGAGAFGKVVEATAyglskSDAVMKVAVKML---KPTAHSSEReALMSELKIMSHLgNHENIVNLLGAC-T 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHGKVYIVMELAVQGDLLE-LIKTRGALHEDEARKKF-HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSk 159
Cdd:cd05055 110 IGGPILVITEYCCYGDLLNfLRRKRESFLTLEDLLSFsYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLA- 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 160 RCLRDDSGRMALSKTFCgsPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYD----DSNIKKMLR 226
Cdd:cd05055 189 RDIMNDSNYVVKGNARL--PVkWMAPESIFNCVYTFES-DVWSYGILLWeIFSLGSNPYPgmpvDSKFYKLIK 258
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
59-279 1.19e-09

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 58.26  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLK 138
Cdd:cd14155  37 REVQLMNRLSHPNILRFMGVC-VHQGQLHALTEYINGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLT 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 139 CDNLLLDKD---FNIKLSDFSFSKRCLRDDSGRMALSktFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILyIMVCGSMP 215
Cdd:cd14155 116 SKNCLIKRDengYTAVVGDFGLAEKIPDYSDGKEKLA--VVGSPYWMAPEVLRGEPYNEKA-DVFSYGIIL-CEIIARIQ 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14042947 216 YDdsniKKMLRIQKEHRVNFPRSKHLTGECkdliyhmlqPDVNRRLHIDeilsHCWMQPKARGS 279
Cdd:cd14155 192 AD----PDYLPRTEDFGLDYDAFQHMVGDC---------PPDFLQLAFN----CCNMDPKSRPS 238
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
18-271 1.30e-09

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: 58.06  E-value: 1.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLKfnVAIKIIdrKKA---PADFLEkflprEIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELA 93
Cdd:cd05034   3 LGAGQFGEVwMGVWNGTTK--VAVKTL--KPGtmsPEAFLQ-----EAQIMKKLRHDKLVQLYAVC-SDEEPIYIVTELM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKT-RG-ALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMAL 171
Cdd:cd05034  73 SKGSLLDYLRTgEGrALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLA-RLIEDDEYTARE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 172 SKTFcgsP-AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLR-IQKEHRVNFPRskhltgECKDL 248
Cdd:cd05034 152 GAKF---PiKWTAPEAALYGRFTIKS-DVWSFGILLYeIVTYGRVPYPGMTNREVLEqVERGYRMPKPP------GCPDE 221
                       250       260
                ....*....|....*....|...
gi 14042947 249 IYhmlqpdvnrrlhidEILSHCW 271
Cdd:cd05034 222 LY--------------DIMLQCW 230
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
18-209 1.64e-09

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: 58.12  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVksaYSERLKFNVAiKIIDRKKAPADFLEKFLP----REIEILAMLN---HCSIIKTYEIFETS----HGKV 86
Cdd:cd07862   9 IGEGAYGKV---FKARDLKNGG-RFVALKRVRVQTGEEGMPlstiREVAVLRHLEtfeHPNVVRLFDVCTVSrtdrETKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMElAVQGDL---LELIKTRGALHEdEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrclR 163
Cdd:cd07862  85 TLVFE-HVDQDLttyLDKVPEPGVPTE-TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA----R 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 164 DDSGRMALSKTFCgSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIM 209
Cdd:cd07862 159 IYSFQMALTSVVV-TLWYRAPEVLLQSSYATPV-DLWSVGCIFAEM 202
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-220 1.85e-09

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: 58.15  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIK----IIDRKKapadflEKFLPREIEILAMLNHC-SIIKTY-EIFetSHGKVYIVME 91
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGTIMAVKrirsTVDEKE------QKRLLMDLDVVMRSSDCpYIVKFYgALF--REGDCWICME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 L-AVQGDLLELI---KTRGALHEDEARKKFHQLSLAIKYC-HDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRcLRDds 166
Cdd:cd06616  86 LmDISLDKFYKYvyeVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQ-LVD-- 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947 167 grmALSKTF-CGSPAYAAPEVLQGIPYQPKvYDI----WSLGVILYIMVCGSMPYDDSN 220
Cdd:cd06616 163 ---SIAKTRdAGCRPYMAPERIDPSASRDG-YDVrsdvWSLGITLYEVATGKFPYPKWN 217
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
52-277 2.08e-09

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 57.69  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  52 FLEKFLP----REIEILAMLNHCSIIKTYeifetshgkvYIVMELAVQGDLLELIKT-RGALHEDEARKKFHQLSLAIK- 125
Cdd:cd05087  44 FLEEAQPyralQHTNLLQCLAQCAEVTPY----------LLVMEFCPLGDLKGYLRScRAAESMAPDPLTLQRMACEVAc 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 126 ---YCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSgrMALSKTFCGSPAYAAPEVLQG------IPYQPKV 196
Cdd:cd05087 114 gllHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDY--FVTADQLWVPLRWIAPELVDEvhgnllVVDQTKQ 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 197 YDIWSLGVILY-IMVCGSMPYDDSNIKKMLRIQ-KEHRVNFPRSKhltgeckdliyhmLQPDVNRRLHidEILSHCWMQP 274
Cdd:cd05087 192 SNVWSLGVTIWeLFELGNQPYRHYSDRQVLTYTvREQQLKLPKPQ-------------LKLSLAERWY--EVMQFCWLQP 256

                ...
gi 14042947 275 KAR 277
Cdd:cd05087 257 EQR 259
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
13-216 2.54e-09

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: 57.73  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  13 LLGINLGEGSYAKVksaYSERLKFNVAIKIIDRKKAPADFLEKFlPREIEILAMLNHCSIIktyeIFE--TSHGKVYIVM 90
Cdd:cd14149  15 MLSTRIGSGSFGTV---YKGKWHGDVAVKILKVVDPTPEQFQAF-RNEVAVLRKTRHVNIL----LFMgyMTKDNLAIVT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAVQGDL---LELIKTRGALHE--DEARkkfhQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDD 165
Cdd:cd14149  87 QWCEGSSLykhLHVQETKFQMFQliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWS 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 14042947 166 SGRMALSKTfcGSPAYAAPEVLQGIPYQPKVY--DIWSLGVILYIMVCGSMPY 216
Cdd:cd14149 163 GSQQVEQPT--GSILWMAPEVIRMQDNNPFSFqsDVYSYGIVLYELMTGELPY 213
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
53-269 2.67e-09

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: 57.17  E-value: 2.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  53 LEKFLPREIEILAMLNHCSIIKTYE-IFETSHGKVyiVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLD 131
Cdd:cd05576  56 LRKYIISEESVFLVLQHAEGGKLWSyLSKFLNDKE--IHQLFADLDERLAAASRFYIPEECIQRWAAEMVVALDALHREG 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 132 VVHRDLKCDNLLLDKDFNIKLSDFSfSKRCLRDDSGRMALSKTFCgspayaAPEVlQGIPYQPKVYDIWSLGVILYIMVC 211
Cdd:cd05576 134 IVCRDLNPNNILLNDRGHIQLTYFS-RWSEVEDSCDSDAIENMYC------APEV-GGISEETEACDWWSLGALLFELLT 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 212 GsmpyddsniKKMLR-----IQKEHRVNFPrsKHLTGECKDLIYHMLQPDVNRRL-----HIDEILSH 269
Cdd:cd05576 206 G---------KALVEchpagINTHTTLNIP--EWVSEEARSLLQQLLQFNPTERLgagvaGVEDIKSH 262
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
38-268 3.23e-09

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


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 57.24  E-value: 3.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIdRKKAPADFLEKFLPrEIEILAMLNHCSIIKtYEIFETSHGKVYIVMELAVQGDLLELI-KTRGALHEDEARKK 116
Cdd:cd05064  36 VAIHTL-RAGCSDKQRRGFLA-EALTLGQFDHSNIVR-LEGVITRGNTMMIVTEYMSNGALDSFLrKHEGQLVAGQLMGM 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 117 FHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFsfsKRCLRDDSgrMALSKTFCG-SPA-YAAPEVLQGIPYQP 194
Cdd:cd05064 113 LPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGF---RRLQEDKS--EAIYTTMSGkSPVlWAAPEAIQYHHFSS 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 195 kVYDIWSLGVILY-IMVCGSMPY-DDSNIKKMLRIQKEHRVNFPRSkhltgeCKDLIYHML----QPDVNRR---LHIDE 265
Cdd:cd05064 188 -ASDVWSFGIVMWeVMSYGERPYwDMSGQDVIKAVEDGFRLPAPRN------CPNLLHQLMldcwQKERGERprfSQIHS 260

                ...
gi 14042947 266 ILS 268
Cdd:cd05064 261 ILS 263
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
38-229 4.29e-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: 57.30  E-value: 4.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIDRKKAPADFLeKFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKT------------- 104
Cdd:cd08216  28 VAVKKINLESDSKEDL-KFLQQEILTSRQLQHPNILPYVTSF-VVDNDLYVVTPLMAYGSCRDLLKThfpeglpelaiaf 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 105 --RGALHedearkkfhqlslAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrCLRDDSGRMalSKTFCGSPAYA 182
Cdd:cd08216 106 ilRDVLN-------------ALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYA--YSMVKHGKR--QRVVHDFPKSS 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14042947 183 -------APEVLQ----GipYQPKVyDIWSLGvilyIMVC----GSMPYDDSNIKKMLrIQK 229
Cdd:cd08216 169 eknlpwlSPEVLQqnllG--YNEKS-DIYSVG----ITACelanGVVPFSDMPATQML-LEK 222
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
59-206 4.42e-09

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 56.76  E-value: 4.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELI---------KTRGALHEDEARkkfhqlslAIKYCHD 129
Cdd:cd14156  37 REISLLQKLSHPNIVRYLGIC-VKDEKLHPILEYVSGGCLEELLareelplswREKVELACDISR--------GMVYLHS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 130 LDVVHRDLKCDNLLLDKDFNIK---LSDFSFSKR--CLRDDSGRMALSktFCGSPAYAAPEVLQGIPYQPKVyDIWSLGV 204
Cdd:cd14156 108 KNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREvgEMPANDPERKLS--LVGSAFWMAPEMLRGEPYDRKV-DVFSFGI 184

                ..
gi 14042947 205 IL 206
Cdd:cd14156 185 VL 186
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
14-279 5.71e-09

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: 56.55  E-value: 5.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  14 LGINLGEGSYAKVKSAY--SERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEI-FETSHGKVY--- 87
Cdd:cd05075   4 LGKTLGEGEFGSVMEGQlnQDDSVLKVAVKTMKIAICTRSEMEDFL-SEAVCMKEFDHPNVMRLIGVcLQNTESEGYpsp 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  88 -IVMELAVQGDLLE-LIKTRGA-----LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKR 160
Cdd:cd05075  83 vVILPFMKHGDLHSfLLYSRLGdcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 161 CLRDD---SGRMALSKTfcgspAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPY---DDSNIKKMLRiqKEHRV 233
Cdd:cd05075 163 IYNGDyyrQGRISKMPV-----KWIAIESLADRVYTTKS-DVWSFGVTMWeIATRGQTPYpgvENSEIYDYLR--QGNRL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14042947 234 NFPrskhltGECKDLIYhmlqpdvnrrlhidEILSHCW-MQPKARGS 279
Cdd:cd05075 235 KQP------PDCLDGLY--------------ELMSSCWlLNPKDRPS 261
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
123-236 6.09e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 56.93  E-value: 6.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  123 AIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkrCLRDDsgrMALSKTF--CGSPAYAAPEVLQGIPYQPKVyDIW 200
Cdd:PHA03212 194 AIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAA--CFPVD---INANKYYgwAGTIATNAPELLARDPYGPAV-DIW 267
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 14042947  201 SLGVILYIMVCGSMPY-----------DDSNIKKMLRIQKEHRVNFP 236
Cdd:PHA03212 268 SAGIVLFEMATCHDSLfekdgldgdcdSDRQIKLIIRRSGTHPNEFP 314
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
12-182 7.00e-09

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: 55.93  E-value: 7.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  12 YLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPadfleKFLPREIEILAMLNHCS-IIKTYEiFETSHGKVYIVM 90
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKH-----PQLEYEAKVYKLLQGGPgIPRLYW-FGQEGDYNVMVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  91 ELAvqG-DLLELIKTRGalhedearKKF---------HQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIK---LSDFSF 157
Cdd:cd14016  76 DLL--GpSLEDLFNKCG--------RKFslktvlmlaDQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGL 145
                       170       180
                ....*....|....*....|....*...
gi 14042947 158 SKRCLRDDSGR---MALSKTFCGSPAYA 182
Cdd:cd14016 146 AKKYRDPRTGKhipYREGKSLTGTARYA 173
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
18-206 7.09e-09

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 55.98  E-value: 7.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLKFNVAIKIID-RKKAPADFLekflpREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQ 95
Cdd:cd14154   1 LGKGFFGQAiKVTHRETGEVMVMKELIRfDEEAQRNFL-----KEVKVMRSLDHPNVLKFIGVLYKDK-KLNLITEYIPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  96 GDLLELIKTRGALHEDEARKKFHQ-LSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS------KRCLRDDSGR 168
Cdd:cd14154  75 GTLKDVLKDMARPLPWAQRVRFAKdIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveeRLPSGNMSPS 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 169 MALSK----------TFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14154 155 ETLRHlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKV-DIFSFGIVL 201
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
18-212 9.67e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 56.25  E-value: 9.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPADFLEKFLprEIEILAML-----NHCSIIKTYEIFETSHgKVYIVMEL 92
Cdd:cd14228  23 LGRGTFGQVAKCWKRSTKEIVAIKIL--KNHPSYARQGQI--EVSILSRLssenaDEYNFVRSYECFQHKN-HTCLVFEM 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQgDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRCLRdds 166
Cdd:cd14228  98 LEQ-NLYDFLKQNkfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSK--- 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 167 grmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCG 212
Cdd:cd14228 174 ---AVCSTYLQSRYYRAPEIILGLPFCEAI-DMWSLGCVIAELFLG 215
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
59-216 1.03e-08

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: 55.81  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  59 REIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRgalhedeaRKKFH-------QLSLAIKYCHD-- 129
Cdd:cd14147  51 QEARLFAMLAHPNIIALKAVC-LEEPNLCLVMEYAAGGPLSRALAGR--------RVPPHvlvnwavQIARGMHYLHCea 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 130 -LDVVHRDLKCDNLLLD--------KDFNIKLSDFSFSKRCLRddSGRMALSKTFcgspAYAAPEVLQGIPYQpKVYDIW 200
Cdd:cd14147 122 lVPVIHRDLKSNNILLLqpienddmEHKTLKITDFGLAREWHK--TTQMSAAGTY----AWMAPEVIKASTFS-KGSDVW 194
                       170
                ....*....|....*.
gi 14042947 201 SLGVILYIMVCGSMPY 216
Cdd:cd14147 195 SFGVLLWELLTGEVPY 210
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
18-216 1.06e-08

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 55.84  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSA-----YSERLKFNVAIKIIDRKKAPA---DFLekflpREIEILAMLNHCSIIKTYEIFETSHgKVYIV 89
Cdd:cd05048  13 LGEGAFGKVYKGellgpSSEESAISVAIKTLKENASPKtqqDFR-----REAELMSDLQHPNIVCLLGVCTKEQ-PQCML 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  90 MELAVQGDLLELIKTR------GALHEDEARKKF----HQLSLAIK------YCHDLDVVHRDLKCDNLLLDKDFNIKLS 153
Cdd:cd05048  87 FEYMAHGDLHEFLVRHsphsdvGVSSDDDGTASSldqsDFLHIAIQiaagmeYLSSHHYVHRDLAARNCLVGDGLTVKIS 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 154 DFSFSKRCLRDDSGRMaLSKTFCgsPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPY 216
Cdd:cd05048 167 DFGLSRDIYSSDYYRV-QSKSLL--PVrWMPPEAILYGKFTTES-DVWSFGVVLWeIFSYGLQPY 227
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
18-269 1.11e-08

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 55.47  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-----KSAYSERLKFNVAIKIIDR---KKAPADFLEKFLpreieILAMLNHCSIIKTYEI-FETShgKVYI 88
Cdd:cd05036  14 LGQGAFGEVyegtvSGMPGDPSPLQVAVKTLPElcsEQDEMDFLMEAL-----IMSKFNHPNIVRCIGVcFQRL--PRFI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIK-TRGALHEDEARKKFHQLSLAI---KYCHDLD---VVHRDLKCDNLLLDK---DFNIKLSDFSFS 158
Cdd:cd05036  87 LLELMAGGDLKSFLReNRPRPEQPSSLTMLDLLQLAQdvaKGCRYLEenhFIHRDIAARNCLLTCkgpGRVAKIGDFGMA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KRCLRDD----SGRMALsktfcgsPA-YAAPEV-LQGIpYQPKVyDIWSLGVILY-IMVCGSMPYD-DSNIKKMLRIQKE 230
Cdd:cd05036 167 RDIYRADyyrkGGKAML-------PVkWMPPEAfLDGI-FTSKT-DVWSFGVLLWeIFSLGYMPYPgKSNQEVMEFVTSG 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 14042947 231 HRVNFPRskhltgECKDLIYHML----QPDVNRRLHIDEILSH 269
Cdd:cd05036 238 GRMDPPK------NCPGPVYRIMtqcwQHIPEDRPNFSTILER 274
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
113-261 1.13e-08

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: 55.96  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 113 ARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN----IKLSDFSFskrCLRDDSGRMALSKT-----FCGSPAYAA 183
Cdd:cd14018 140 ARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDgcpwLVIADFGC---CLADDSIGLQLPFSswyvdRGGNACLMA 216
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 184 PEVLQGIPYQPKVY-----DIWSLGVILYIMVCGSMPYdDSNIKKMLRIQKEHRVNFPR-SKHLTGECKDLIYHMLQPDV 257
Cdd:cd14018 217 PEVSTAVPGPGVVInyskaDAWAVGAIAYEIFGLSNPF-YGLGDTMLESRSYQESQLPAlPSAVPPDVRQVVKDLLQRDP 295

                ....
gi 14042947 258 NRRL 261
Cdd:cd14018 296 NKRV 299
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
18-217 1.23e-08

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 55.80  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY----SERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETShgKVYIVMELA 93
Cdd:cd05108  15 LGSGAFGTVYKGLwipeGEKVKIPVAIKELREATSPK--ANKEILDEAYVMASVDNPHVCRLLGICLTS--TVQLITQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTrgalHEDEARKKFH-----QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRD---- 164
Cdd:cd05108  91 PFGCLLDYVRE----HKDNIGSQYLlnwcvQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEekey 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 165 --DSGRMALSktfcgspaYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYD 217
Cdd:cd05108 167 haEGGKVPIK--------WMALESILHRIYTHQS-DVWSYGVTVWeLMTFGSKPYD 213
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
18-220 1.24e-08

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 55.17  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY---SERLKFNVAIKIIDRKKAPADfLEKFLpREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAV 94
Cdd:cd05058   3 IGKGHFGCVYHGTlidSDGQKIHCAVKSLNRITDIEE-VEQFL-KEGIIMKDFSHPNVLSLLGICLPSEGSPLVVLPYMK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIktRGALHEDEARKKFH---QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMAL 171
Cdd:cd05058  81 HGDLRNFI--RSETHNPTVKDLIGfglQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLA-RDIYDKEYYSVH 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14042947 172 SKTFCGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSN 220
Cdd:cd05058 158 NHTGAKLPVkWMALESLQTQKFTTKS-DVWSFGVLLWeLMTRGAPPYPDVD 207
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
10-281 1.37e-08

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


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 55.29  E-value: 1.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  10 RGYLLGINLGEgsyakVKSAYSerlkfnVAIKIIDRKKAPADFLE--KFLpREIEILAMLNHCSIIKTY-EIFETShgKV 86
Cdd:cd05042   5 NGWFGKVLLGE-----IYSGTS------VAQVVVKELKASANPKEqdTFL-KEGQPYRILQHPNILQCLgQCVEAI--PY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  87 YIVMELAVQGDLLELIKT-RGALHEDEARKKFHQLSLAIK----YCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRC 161
Cdd:cd05042  71 LLVMEFCDLGDLKAYLRSeREHERGDSDTRTLQRMACEVAaglaHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 162 LRDDSGRMALSKTFcgsP-AYAAPEVLQGIPY------QPKVYDIWSLGVILY-IMVCGSMPYDD-SNIKKMLRIQKEHR 232
Cdd:cd05042 151 YKEDYIETDDKLWF---PlRWTAPELVTEFHDrllvvdQTKYSNIWSLGVTLWeLFENGAQPYSNlSDLDVLAQVVREQD 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 14042947 233 VNFPRSKhltgeckdliyhmLQPDVNRRLHidEILSHCWMQPKARGSPS 281
Cdd:cd05042 228 TKLPKPQ-------------LELPYSDRWY--EVLQFCWLSPEQRPAAE 261
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
98-260 1.49e-08

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 55.20  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    98 LLELIKTRGALHEDEARKKFHQLSLAI----KYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfskrCLRDDSGRMALSK 173
Cdd:pfam14531 127 LGEVLLSHSSTHKSLVHHARLQLTLQLirlaANLQHYGLVHGQFTVDNFFLDQRGGVFLGGFE----HLVRDGTKVVASE 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   174 TfcgSPAYAAPEVL-QGIPYQPK-------VYDIWSLGVILYIMVCGSMPYDdsnikkmlRIQKEHRVN--FPRSKHLTG 243
Cdd:pfam14531 203 V---PRGFAPPELLgSRGGYTMKnttlmthAFDAWQLGLVIYWIWCLDLPNT--------LDAEEGGIEwkFRLCKNIPE 271
                         170
                  ....*....|....*..
gi 14042947   244 ECKDLIYHMLQPDVNRR 260
Cdd:pfam14531 272 PVRALLKGFLNYSQEDR 288
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
19-210 2.13e-08

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: 54.75  E-value: 2.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  19 GEGSYAKVksaYSERLKF-NVAIKIIDRKKAPADFLEKflprEIEILAMLNHCSIIKTYEIFETSHG---KVYIVMELAV 94
Cdd:cd13998   4 GKGRFGEV---WKASLKNePVAVKIFSSRDKQSWFREK----EIYRTPMLKHENILQFIAADERDTAlrtELWLVTAFHP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIK----------------TRGA--LHEDEARKKFHQLSLAikychdldvvHRDLKCDNLLLDKDFNIKLSDFS 156
Cdd:cd13998  77 NGSL*DYLSlhtidwvslcrlalsvARGLahLHSEIPGCTQGKPAIA----------HRDLKSKNILVKNDGTCCIADFG 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14042947 157 FSkrcLRDDSGRMALSKTF---CGSPAYAAPEVLQG-IPYQP----KVYDIWSLGVILYIMV 210
Cdd:cd13998 147 LA---VRLSPSTGEEDNANngqVGTKRYMAPEVLEGaINLRDfesfKRVDIYAMGLVLWEMA 205
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
18-236 2.16e-08

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: 54.73  E-value: 2.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrkKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGD 97
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTL---KEDTMEVEEFL-KEAAVMKEIKHPNLVQLLGVC-TREPPFYIITEFMPYGN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  98 LLELIKTRGAlHEDEARKKFH---QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSkRCLRDDSGRMALSKT 174
Cdd:cd05052  89 LLDYLRECNR-EELNAVVLLYmatQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLS-RLMTGDTYTAHAGAK 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 175 FcgsP-AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPY---DDSNIKKMLriQKEHRVNFP 236
Cdd:cd05052 167 F---PiKWTAPESLAYNKFSIKS-DVWAFGVLLWeIATYGMSPYpgiDLSQVYELL--EKGYRMERP 227
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
18-216 2.50e-08

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: 54.46  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLkfnVAIKiidRKKAPAdFLEK----FLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMEL 92
Cdd:cd14064   1 IGSGSFGKVyKGRCRNKI---VAIK---RYRANT-YCSKsdvdMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQGDLLELiktrgaLHE-----DEARKKFHQLSLA--IKYCHDLD--VVHRDLKCDNLLLDKDFNIKLSDFSFSK-RCL 162
Cdd:cd14064  74 VSGGSLFSL------LHEqkrviDLQSKLIIAVDVAkgMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRfLQS 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14042947 163 RDDSGrmaLSKTfCGSPAYAAPEVL-QGIPYQPKVyDIWSLGVILYIMVCGSMPY 216
Cdd:cd14064 148 LDEDN---MTKQ-PGNLRWMAPEVFtQCTRYSIKA-DVFSYALCLWELLTGEIPF 197
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
18-207 4.23e-08

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 53.75  E-value: 4.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVkSAY-----SERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETSHGK-VYIVME 91
Cdd:cd05080  12 LGEGHFGKV-SLYcydptNDGTGEMVAVKALKADCGPQ--HRSGWKQEIDILKTLYHENIVKYKGCCSEQGGKsLQLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKtRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRC--------LR 163
Cdd:cd05080  89 YVPLGSLRDYLP-KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVpegheyyrVR 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 164 DDSgrmalsktfcGSPAY-AAPEVLQgipyQPKVY---DIWSLGVILY 207
Cdd:cd05080 168 EDG----------DSPVFwYAPECLK----EYKFYyasDVWSFGVTLY 201
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
11-273 4.27e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.50  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   11 GYLLGINLGEGSYAKVKSAYSERLKFNVAIKIidrKKAPADFLEKFLPREIeilamlNHCSIIKTYEIFetSHGKVYIVM 90
Cdd:PHA03209  67 GYTVIKTLTPGSEGRVFVATKPGQPDPVVLKI---GQKGTTLIEAMLLQNV------NHPSVIRMKDTL--VSGAITCMV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   91 ELAVQGDLLELIKTR-GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSfSKRCLRDDSGRM 169
Cdd:PHA03209 136 LPHYSSDLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPVVAPAFL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  170 ALSktfcGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVC---------GSMPYD-----DSNIKKMLRIQKEHRVNF 235
Cdd:PHA03209 215 GLA----GTVETNAPEVLARDKYNSKA-DIWSAGIVLFEMLAypstifedpPSTPEEyvkscHSHLLKIISTLKVHPEEF 289
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14042947  236 PRSK------------------------------HLTGECkdLIYHMLQPDVNRRLHIDEILSH-CWMQ 273
Cdd:PHA03209 290 PRDPgsrlvrgfieyaslerqpytrypcfqrvnlPIDGEF--LVHKMLTFDAAMRPSAEEILNYpMFAQ 356
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
18-212 4.62e-08

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: 54.33  E-value: 4.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPADFLEKFLprEIEILAMLNHCS-----IIKTYEIFETSHgKVYIVMEL 92
Cdd:cd14227  23 LGRGTFGQVVKCWKRGTNEIVAIKIL--KNHPSYARQGQI--EVSILARLSTESaddynFVRAYECFQHKN-HTCLVFEM 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQgDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSKRCLRdds 166
Cdd:cd14227  98 LEQ-NLYDFLKQNkfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASHVSK--- 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 167 grmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVILYIMVCG 212
Cdd:cd14227 174 ---AVCSTYLQSRYYRAPEIILGLPFCEAI-DMWSLGCVIAELFLG 215
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
7-207 4.78e-08

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: 54.25  E-value: 4.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   7 LKRRGYLLGiNLGEGSYAKVKSAYSE-RLKFNVAIKII-------DRKKAPADFLEKFLPREIEILAMlnhCSIIKTYEI 78
Cdd:cd14214  11 LQERYEIVG-DLGEGTFGKVVECLDHaRGKSQVALKIIrnvgkyrEAARLEINVLKKIKEKDKENKFL---CVLMSDWFN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FetsHGKVYIVMELaVQGDLLELIKTRGALHE--DEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFNIKLSDf 155
Cdd:cd14214  87 F---HGHMCIAFEL-LGKNTFEFLKENNFQPYplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILfVNSEFDTLYNE- 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 156 sfSKRC----LRDDSGRMAL--SKTF--------CGSPAYAAPEVLQGIPY-QPkvYDIWSLGVILY 207
Cdd:cd14214 162 --SKSCeeksVKNTSIRVADfgSATFdhehhttiVATRHYRPPEVILELGWaQP--CDVWSLGCILF 224
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
38-218 4.88e-08

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: 53.88  E-value: 4.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIdRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKF 117
Cdd:cd05051  49 VAVKML-RPDASKNAREDFL-KEVKIMSQLKDPNIVRLLGVC-TRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNS 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 118 HQLSLA------------IKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDD----SGRMALsktfcgsPA- 180
Cdd:cd05051 126 KTLSYGtllymatqiasgMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLYSGDyyriEGRAVL-------PIr 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14042947 181 YAAPEVLQGIPYQPKVyDIWSLGVILY--IMVCGSMPYDD 218
Cdd:cd05051 199 WMAWESILLGKFTTKS-DVWAFGVTLWeiLTLCKEQPYEH 237
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
54-206 5.87e-08

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: 53.41  E-value: 5.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  54 EKFLPREIEILAMLNHCSIIKTYEIFETSHgKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVV 133
Cdd:cd14222  34 QKTFLTEVKVMRSLDHPNVLKFIGVLYKDK-RLNLLTEFIEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSII 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 134 HRDLKCDNLLLDKDFNIKLSDFSFS------------------KRCLRDDSGRMALskTFCGSPAYAAPEVLQGIPYQPK 195
Cdd:cd14222 113 HRDLNSHNCLIKLDKTVVVADFGLSrliveekkkpppdkpttkKRTLRKNDRKKRY--TVVGNPYWMAPEMLNGKSYDEK 190
                       170
                ....*....|.
gi 14042947 196 VyDIWSLGVIL 206
Cdd:cd14222 191 V-DIFSFGIVL 200
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
18-253 7.37e-08

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: 53.46  E-value: 7.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERL-KFN---------------VAIKIID---RKKAPADFLekflpREIEILAMLNHCSIIKTYEI 78
Cdd:cd05095  13 LGEGQFGEVHLCEAEGMeKFMdkdfalevsenqpvlVAVKMLRadaNKNARNDFL-----KEIKIMSRLKDPNIIRLLAV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  79 FETSHgKVYIVMELAVQGDL------------LELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDK 146
Cdd:cd05095  88 CITDD-PLCMITEYMENGDLnqflsrqqpegqLALPSNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 147 DFNIKLSDFSFSKRCLRDD----SGR-------MALSKTFCGSPAYAApevlqgipyqpkvyDIWSLGVILY--IMVCGS 213
Cdd:cd05095 167 NYTIKIADFGMSRNLYSGDyyriQGRavlpirwMSWESILLGKFTTAS--------------DVWAFGVTLWetLTFCRE 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14042947 214 MPYDD-------SNIKKMLRIQKEhRVNFPRSkhltGECKDLIYHML 253
Cdd:cd05095 233 QPYSQlsdeqviENTGEFFRDQGR-QTYLPQP----ALCPDSVYKLM 274
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
18-207 9.85e-08

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: 52.97  E-value: 9.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFN----VAIKIIdrKKAPADFLEKFlPREIEILAMLNHCSIIKtYEIFETSHGK--VYIVME 91
Cdd:cd05081  12 LGKGNFGSVELCRYDPLGDNtgalVAVKQL--QHSGPDQQRDF-QREIQILKALHSDFIVK-YRGVSYGPGRrsLRLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLE-LIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMA 170
Cdd:cd05081  88 YLPSGCLRDfLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVV 167
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 14042947 171 LSKTfcGSPAY-AAPEVLQGIPYQpKVYDIWSLGVILY 207
Cdd:cd05081 168 REPG--QSPIFwYAPESLSDNIFS-RQSDVWSFGVVLY 202
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
17-277 1.35e-07

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 52.39  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  17 NLGEGSYAKVKSAYSERLkfnVAIKIIDRKkapaDFLEKFLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQG 96
Cdd:cd13992  10 HTGEPKYVKKVGVYGGRT---VAIKHITFS----RTEKRTILQELNQLKELVHDNLNKFIGIC-INPPNIAVVTEYCTRG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  97 DLLELIKTRGALHEDEARKKF-HQLSLAIKYCHD-LDVVHRDLKCDNLLLDKDFNIKLSDFSFSKrcLRDDSGRMALSKT 174
Cdd:cd13992  82 SLQDVLLNREIKMDWMFKSSFiKDIVKGMNYLHSsSIGYHGRLKSSNCLVDSRWVVKLTDFGLRN--LLEEQTNHQLDED 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 175 FCGSP-AYAAPEVLQGIPYQPKVY---DIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSkhltgeckDLIY 250
Cdd:cd13992 160 AQHKKlLWTAPELLRGSLLEVRGTqkgDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFRP--------ELAV 231
                       250       260
                ....*....|....*....|....*...
gi 14042947 251 HMLQpdVNRRLHidEILSHCWM-QPKAR 277
Cdd:cd13992 232 LLDE--FPPRLV--LLVKQCWAeNPEKR 255
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
18-206 1.48e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 52.45  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSERLKFNVAIKIIdrKKAPAdfLEKFLPREIEILAMLNH-----CSIIKTYEIFETSHgKVYIVMEL 92
Cdd:cd14211   7 LGRGTFGQVVKCWKRGTNEIVAIKIL--KNHPS--YARQGQIEVSILSRLSQenadeFNFVRAYECFQHKN-HTCLVFEM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  93 AVQgDLLELIKTR--GALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFS----FSKrcl 162
Cdd:cd14211  82 LEQ-NLYDFLKQNkfSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGsashVSK--- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 14042947 163 rddsgrmALSKTFCGSPAYAAPEVLQGIPYQPKVyDIWSLGVIL 206
Cdd:cd14211 158 -------AVCSTYLQSRYYRAPEIILGLPFCEAI-DMWSLGCVI 193
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
18-217 1.62e-07

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: 52.38  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY----SERLKFNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETShgKVYIVMELA 93
Cdd:cd05110  15 LGSGAFGTVYKGIwvpeGETVKIPVAIKILNETTGPKANVE--FMDEALIMASMDHPHLVRLLGVCLSP--TIQLVTQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIKTrgalHEDEARKKFH-----QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRD---- 164
Cdd:cd05110  91 PHGCLLDYVHE----HKDNIGSQLLlnwcvQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDekey 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14042947 165 --DSGRMALSKTfcgspayaapeVLQGIPYQPKVY--DIWSLGVILY-IMVCGSMPYD 217
Cdd:cd05110 167 naDGGKMPIKWM-----------ALECIHYRKFTHqsDVWSYGVTIWeLMTFGGKPYD 213
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
18-216 1.70e-07

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 51.88  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY----SERLKFNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETShgKVYIVMELA 93
Cdd:cd05111  15 LGSGVFGTVHKGIwipeGDSIKIPVAIKVIQDRSGRQSFQA--VTDHMLAIGSLDHAYIVRLLGICPGA--SLQLVTQLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELI-KTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGR---- 168
Cdd:cd05111  91 PLGSLLDHVrQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKKYfyse 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 169 -------MALSKTFCGSPAYAApevlqgipyqpkvyDIWSLGVILY-IMVCGSMPY 216
Cdd:cd05111 171 aktpikwMALESIHFGKYTHQS--------------DVWSYGVTVWeMMTFGAEPY 212
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
16-281 1.70e-07

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 52.08  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  16 INLGEGSY-----AKVKSAYSERLKFNVAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFETS--HgkvYI 88
Cdd:cd05046  11 TTLGRGEFgevflAKAKGIEEEGGETLVLVKALQKTKDENLQSE--FRRELDMFRKLSHKNVVRLLGLCREAepH---YM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  89 VMELAVQGDLLELIKTRGALHEDEARKKF---HQLSLAIKYCHDLD------VVHRDLKCDNLLLDKDFNIKLSDFSFSK 159
Cdd:cd05046  86 ILEYTDLGDLKQFLRATKSKDEKLKPPPLstkQKVALCTQIALGMDhlsnarFVHRDLAARNCLVSSQREVKVSLLSLSK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 160 RCLRDD--SGRMALSKTfcgspAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLRIQKEHRVNFP 236
Cdd:cd05046 166 DVYNSEyyKLRNALIPL-----RWLAPEAVQEDDFSTKS-DVWSFGVLMWeVFTQGELPFYGLSDEEVLNRLQAGKLELP 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 237 rskhLTGECKDLIYhmlqpdvnrrlhidEILSHCWM-QPKARGSPS 281
Cdd:cd05046 240 ----VPEGCPSRLY--------------KLMTRCWAvNPKDRPSFS 267
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
18-207 1.71e-07

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: 51.98  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-KSAYSERLkfnVAIKIIdrkkaPADFLEKFL-PREIEILAMLNHCSIIKTYEIFE--TSHGKV--YIVME 91
Cdd:cd14054   3 IGQGRYGTVwKGSLDERP---VAVKVF-----PARHRQNFQnEKDIYELPLMEHSNILRFIGADErpTADGRMeyLLVLE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIK----------------TRGA--LHEDEARKKFHqlslaiKYChdldVVHRDLKCDNLLLDKDFNIKLS 153
Cdd:cd14054  75 YAPKGSLCSYLRentldwmsscrmalslTRGLayLHTDLRRGDQY------KPA----IAHRDLNSRNVLVKADGSCVIC 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 154 DFSFSKRcLRDDSG-----RMALSKTF--CGSPAYAAPEVLQG------IPYQPKVYDIWSLGVILY 207
Cdd:cd14054 145 DFGLAMV-LRGSSLvrgrpGAAENASIseVGTLRYMAPEVLEGavnlrdCESALKQVDVYALGLVLW 210
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
6-269 2.00e-07

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 52.16  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRgYLLGINLGEGSYAKVKSAYSERLK-FNVAIKII---DRKKAPADflekflpREIEILAMLNHCSIIKTY----- 76
Cdd:cd14213   9 VLRAR-YEIVDTLGEGAFGKVVECIDHKMGgMHVAVKIVknvDRYREAAR-------SEIQVLEHLNTTDPNSTFrcvqm 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  77 -EIFEtSHGKVYIVMELaVQGDLLELIKTRGAL--HEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLL-LDKDFNIKL 152
Cdd:cd14213  81 lEWFD-HHGHVCIVFEL-LGLSTYDFIKENSFLpfPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILfVQSDYVVKY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 153 -SDFSFSKRCLRD------DSGRMALS----KTFCGSPAYAAPEVLQGIPY-QPkvYDIWSLGVILYIMVCGSMPYDDSN 220
Cdd:cd14213 159 nPKMKRDERTLKNpdikvvDFGSATYDdehhSTLVSTRHYRAPEVILALGWsQP--CDVWSIGCILIEYYLGFTVFQTHD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 221 IKKMLR-------------IQKEHRVNF------------PRSKHLTGECK-----------------DLIYHMLQPDVN 258
Cdd:cd14213 237 SKEHLAmmerilgplpkhmIQKTRKRKYfhhdqldwdehsSAGRYVRRRCKplkefmlsqdvdheqlfDLIQKMLEYDPA 316
                       330
                ....*....|.
gi 14042947 259 RRLHIDEILSH 269
Cdd:cd14213 317 KRITLDEALKH 327
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
6-279 2.83e-07

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: 51.46  E-value: 2.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRGYLLGINLGEGSYAKVKSAY--SERLKF-NVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEIFETS 82
Cdd:cd05074   5 LIQEQQFTLGRMLGKGEFGSVREAQlkSEDGSFqKVAVKMLKADIFSSSDIEEFL-REAACMKEFDHPNVIKLIGVSLRS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  83 HGK-----VYIVMELAVQGDLLE-LIKTRGA-----LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIK 151
Cdd:cd05074  84 RAKgrlpiPMVILPFMKHGDLHTfLLMSRIGeepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 152 LSDFSFSKRCLRDDSGRMAlsktfCGSP---AYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPY---DDSNIKKM 224
Cdd:cd05074 164 VADFGLSKKIYSGDYYRQG-----CASKlpvKWLALESLADNVYTTHS-DVWAFGVTMWeIMTRGQTPYagvENSEIYNY 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14042947 225 LriQKEHRVNFPRskhltgECKDLIYhmlqpdvnrrlhidEILSHCWM-QPKARGS 279
Cdd:cd05074 238 L--IKGNRLKQPP------DCLEDVY--------------ELMCQCWSpEPKCRPS 271
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
18-226 3.25e-07

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 51.12  E-value: 3.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-----KSAYSERLKFNVAIKIIDRKKApadflekfLPREIEilaMLNHCSIIKTYEIFET-------SHGK 85
Cdd:cd05061  14 LGQGSFGMVyegnaRDIIKGEAETRVAVKTVNESAS--------LRERIE---FLNEASVMKGFTCHHVvrllgvvSKGQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  86 -VYIVMELAVQGDLLELIKT----------RGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSD 154
Cdd:cd05061  83 pTLVVMELMAHGDLKSYLRSlrpeaennpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGD 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14042947 155 FSFSKRCLRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLR 226
Cdd:cd05061 163 FGMTRDIYETDYYRKGGKGLL--PVRWMAPESLKDGVFTTSS-DMWSFGVVLWeITSLAEQPYQGLSNEQVLK 232
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
18-254 3.26e-07

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


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 51.54  E-value: 3.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAYSER--LKFNVAIKIIDRKKAPADflEKFLPREIEILAMLN-HCSIIKTYEIFEtSHGKVYIVMELAV 94
Cdd:cd05088  15 IGEGNFGQVLKARIKKdgLRMDAAIKRMKEYASKDD--HRDFAGELEVLCKLGhHPNIINLLGACE-HRGYLYLAIEYAP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  95 QGDLLELIKTRGALHEDEARKKFHQ----------------LSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFS 158
Cdd:cd05088  92 HGNLLDFLRKSRVLETDPAFAIANStastlssqqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 159 KrclrddSGRMALSKTFCGSPA-YAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKML-RIQKEHRVNF 235
Cdd:cd05088 172 R------GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNS-DVWSYGVLLWeIVSLGGTPYCGMTCAELYeKLPQGYRLEK 244
                       250
                ....*....|....*....
gi 14042947 236 PRSkhltgeCKDLIYHMLQ 254
Cdd:cd05088 245 PLN------CDDEVYDLMR 257
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
96-270 5.19e-07

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 49.32  E-value: 5.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947     96 GDLLELIKTRGA-LHEDEARKKFHQLSLAIKYCHDLDvvhrdlKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALskt 174
Cdd:smart00750   1 VSLADILEVRGRpLNEEEIWAVCLQCLGALRELHRQA------KSGNILLTWDGLLKLDGSVAFKTPEQSRPDPYFM--- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947    175 fcgspayaAPEVLQGIPYQPKVyDIWSLGVILYIMVCGSMPYDDSN---------IKKMLRIQKEHRVN---FPRSKHLT 242
Cdd:smart00750  72 --------APEVIQGQSYTEKA-DIYSLGITLYEALDYELPYNEERelsaileilLNGMPADDPRDRSNlegVSAARSFE 142
                          170       180
                   ....*....|....*....|....*...
gi 14042947    243 GECKDLIYHMLQpdvnRRLHIDEILSHC 270
Cdd:smart00750 143 DFMRLCASRLPQ----RREAANHYLAHC 166
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
15-206 6.50e-07

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 50.45  E-value: 6.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  15 GINLGEGSYAKVksaYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFET-SHGKVYIVMELA 93
Cdd:cd07867   7 GCKVGRGTYGHV---YKAKRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLShSDRKVWLLFDYA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 vQGDLLELIKTRGA---------LHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL----DKDFNIKLSDFSFSkR 160
Cdd:cd07867  84 -EHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-R 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14042947 161 CLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVIL 206
Cdd:cd07867 162 LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIF 207
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
18-217 6.63e-07

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 50.41  E-value: 6.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKVKSAY----SERLKFNVAIKIIDRKKAPAdfLEKFLPREIEILAMLNHCSIIKTYEIFETShgKVYIVMELA 93
Cdd:cd05109  15 LGSGAFGTVYKGIwipdGENVKIPVAIKVLRENTSPK--ANKEILDEAYVMAGVGSPYVCRLLGICLTS--TVQLVTQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  94 VQGDLLELIK-TRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMAls 172
Cdd:cd05109  91 PYGCLLDYVReNKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHA-- 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14042947 173 ktfCGSPAYAAPEVLQGIPYQPKVY--DIWSLGVILY-IMVCGSMPYD 217
Cdd:cd05109 169 ---DGGKVPIKWMALESILHRRFTHqsDVWSYGVTVWeLMTFGAKPYD 213
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
114-283 8.90e-07

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: 50.13  E-value: 8.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 114 RKKFHQLSLAIKYCHDLDVVHRDLKCDNLLL-DKDFNIKLSDFSFSKRcLRddSGRMALSKTFCGSPAYAAPE------- 185
Cdd:cd14013 123 KSIMRQILVALRKLHSTGIVHRDVKPQNIIVsEGDGQFKIIDLGAAAD-LR--IGINYIPKEFLLDPRYAPPEqyimstq 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 186 -----------VLQGIPYQ---PKVYDIWSLGVILYIMVCGSMpYDDSNIKKMLRIQKEHRVNFPRSKHLTGE--CKDLI 249
Cdd:cd14013 200 tpsappapvaaALSPVLWQmnlPDRFDMYSAGVILLQMAFPNL-RSDSNLIAFNRQLKQCDYDLNAWRMLVEPraSADLR 278
                       170       180       190
                ....*....|....*....|....*....|....
gi 14042947 250 YHMLQPDVNRRLHIDeiLSHCWMQPKARGSPSVA 283
Cdd:cd14013 279 EGFEILDLDDGAGWD--LVTKLIRYKPRGRLSAS 310
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
18-230 9.81e-07

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 49.65  E-value: 9.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  18 LGEGSYAKV-----KSAYSERLKFNVAIKIIDRKKAPADFLEkFLpREIEILAMLNHCSIIKTYEIfeTSHGK-VYIVME 91
Cdd:cd05062  14 LGQGSFGMVyegiaKGVVKDEPETRVAIKTVNEAASMRERIE-FL-NEASVMKEFNCHHVVRLLGV--VSQGQpTLVIME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  92 LAVQGDLLELIKTRGALHEDEARKKFHQLSLAIK----------YCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRC 161
Cdd:cd05062  90 LMTRGDLKSYLRSLRPEMENNPVQAPPSLKKMIQmageiadgmaYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDI 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 162 LRDDSGRMALSKTFcgSPAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKMLRIQKE 230
Cdd:cd05062 170 YETDYYRKGGKGLL--PVRWMSPESLKDGVFTTYS-DVWSFGVVLWeIATLAEQPYQGMSNEQVLRFVME 236
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
120-279 1.04e-06

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: 49.46  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 120 LSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMA-LSKTfcgsPA-YAAPEVLQGIPYQPKVy 197
Cdd:cd05035 122 IAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIYSGDYYRQGrISKM----PVkWIALESLADNVYTSKS- 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 198 DIWSLGVILY-IMVCGSMPY---DDSNIKKMLRiqKEHRVNFPRskhltgECKDLIYhmlqpdvnrrlhidEILSHCW-M 272
Cdd:cd05035 197 DVWSFGVTMWeIATRGQTPYpgvENHEIYDYLR--NGNRLKQPE------DCLDEVY--------------FLMYFCWtV 254

                ....*..
gi 14042947 273 QPKARGS 279
Cdd:cd05035 255 DPKDRPT 261
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
38-226 1.16e-06

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: 49.62  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  38 VAIKIIDRKKAPADFLEkfLPREIEILAMLNHCSIIKTYEIFeTSHGKVYIVMELAVQGDLLELIKTRG-------ALHE 110
Cdd:cd05090  37 VAIKTLKDYNNPQQWNE--FQQEASLMTELHHPNIVCLLGVV-TQEQPVCMLFEFMNQGDLHEFLIMRSphsdvgcSSDE 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 111 DEARKK-------FH---QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDsgrmalskTFCGSPA 180
Cdd:cd05090 114 DGTVKSsldhgdfLHiaiQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSD--------YYRVQNK 185
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14042947 181 YAAPevLQGIPYQPKVY-------DIWSLGVILYIMVC-GSMPY---DDSNIKKMLR 226
Cdd:cd05090 186 SLLP--IRWMPPEAIMYgkfssdsDIWSFGVVLWEIFSfGLQPYygfSNQEVIEMVR 240
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
6-271 1.30e-06

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


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 49.55  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947   6 VLKRRGYLLGINLGEGSYAKVKSA---YSERLKFNVAIKIIDRKKAPADFLEKFLpREIEILAMLNHCSIIKTYEI-FET 81
Cdd:cd14204   3 MIDRNLLSLGKVLGEGEFGSVMEGelqQPDGTNHKVAVKTMKLDNFSQREIEEFL-SEAACMKDFNHPNVIRLLGVcLEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947  82 SHG---KVYIVMELAVQGDLLE-LIKTRgalHEDEARK-------KFH-QLSLAIKYCHDLDVVHRDLKCDNLLLDKDFN 149
Cdd:cd14204  82 GSQripKPMVILPFMKYGDLHSfLLRSR---LGSGPQHvplqtllKFMiDIALGMEYLSSRNFLHRDLAARNCMLRDDMT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14042947 150 IKLSDFSFSKRCLRDD---SGRMALSKTfcgspAYAAPEVLQGIPYQPKVyDIWSLGVILY-IMVCGSMPYDDSNIKKML 225
Cdd:cd14204 159 VCVADFGLSKKIYSGDyyrQGRIAKMPV-----KWIAVESLADRVYTVKS-DVWAFGVTMWeIATRGMTPYPGVQNHEIY 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 14042947 226 R-IQKEHRVNFPRskhltgECKDLIYhmlqpdvnrrlhidEILSHCW 271
Cdd:cd14204 233 DyLLHGHRLKQPE------DCLDELY--------------DIMYSCW 259
 
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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