NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1774959464|ref|NP_001363220|]
View 

serine/threonine-protein kinase PAK 1 isoform 6 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase PAK( domain architecture ID 10466534)

serine/threonine-protein kinase PAK (p21-activated kinase) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and it functions as a key effector of RHO-family GTPases involved in cell motility, survival, and proliferation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
249-503 2.68e-175

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


The actual alignment was detected with superfamily member cd06654:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 296  Bit Score: 494.63  E-value: 2.68e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 249 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV 328
Cdd:cd06654     1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 329 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRE------------------------------------ 372
Cdd:cd06654    81 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCREclqaleflhsnqvihrdiksdnillgmdgsvkltdf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 -----ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 447
Cdd:cd06654   161 gfcaqITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774959464 448 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 503
Cdd:cd06654   241 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 296
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
74-132 1.78e-26

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


:

Pssm-ID: 395634  Cd Length: 59  Bit Score: 101.62  E-value: 1.78e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464  74 EISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYN 132
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFYS 59
 
Name Accession Description Interval E-value
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
249-503 2.68e-175

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: 494.63  E-value: 2.68e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 249 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV 328
Cdd:cd06654     1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 329 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRE------------------------------------ 372
Cdd:cd06654    81 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCREclqaleflhsnqvihrdiksdnillgmdgsvkltdf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 -----ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 447
Cdd:cd06654   161 gfcaqITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774959464 448 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 503
Cdd:cd06654   241 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 296
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
270-480 5.60e-70

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 223.95  E-value: 5.60e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  349 GGSLTDVVTET-CMDEGQIAAVCREIT-----------------PE-----------------------QSKRSTMVGTP 387
Cdd:smart00220  81 GGDLFDLLKKRgRLSEDEARFYLRQILsaleylhskgivhrdlkPEnilldedghvkladfglarqldpGEKLTTFVGTP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE-KLSAIFRDFLNRCLEMDVE 466
Cdd:smart00220 161 EYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKDPE 240
                          250
                   ....*....|....
gi 1774959464  467 KRGSAKELLQHQFL 480
Cdd:smart00220 241 KRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
270-480 4.03e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 217.88  E-value: 4.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVTE-TCMDEGQIAAVCREIT---PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:pfam00069  81 EGGSLFDLLSEkGAFSEREAKFIMKQILeglESGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 424 LNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:pfam00069 161 PGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
269-476 5.93e-36

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 139.38  E-value: 5.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:COG0515     8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpeLAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVVTET-CMDEGQIAAVCREI------------------------------------------TPEQSKRST 382
Cdd:COG0515    88 YVEGESLADLLRRRgPLPPAEALRILAQLaealaaahaagivhrdikpanilltpdgrvklidfgiaralgGATLTQTGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQ--NPEkLSAIFRDFLNRC 460
Cdd:COG0515   168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSelRPD-LPPALDAIVLRA 246
                         250
                  ....*....|....*..
gi 1774959464 461 LEMDVEKR-GSAKELLQ 476
Cdd:COG0515   247 LAKDPEERyQSAAELAA 263
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
74-132 1.78e-26

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 101.62  E-value: 1.78e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464  74 EISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYN 132
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFYS 59
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
73-118 1.12e-23

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 93.49  E-value: 1.12e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464  73 PEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQK 118
Cdd:cd01093     1 PEISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSGITKEEQK 46
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
186-485 1.71e-20

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 92.96  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 186 PPPVIAPRPEHTKSVYTRSVIEP---LPVtPTRDVATS---PISPTENNTTPPDALTRNTEKQKKKPKMSDeeiLEKLRs 259
Cdd:PLN00034    6 PPPGVPLPSTARHTTKSRPRRRPdltLPL-PQRDPSLAvplPLPPPSSSSSSSSSSSASGSAPSAAKSLSE---LERVN- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 260 ivsvgdpkkkytrfeKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVG 337
Cdd:PLN00034   81 ---------------RIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHN 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 DELWVVMEYLAGGSLTDvvtETCMDEGQIAAVCRE-----------------ITPEQ----SKRS--------------T 382
Cdd:PLN00034  145 GEIQVLLEFMDGGSLEG---THIADEQFLADVARQilsgiaylhrrhivhrdIKPSNllinSAKNvkiadfgvsrilaqT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 M------VGTPYWMAPEVV----TRKAY-GPKVDIWSLGIMAIEMIEGEPPY-LNENPLRALYLIATNGTPELQNPEKLS 450
Cdd:PLN00034  222 MdpcnssVGTIAYMSPERIntdlNHGAYdGYAGDIWSLGVSILEFYLGRFPFgVGRQGDWASLMCAICMSQPPEAPATAS 301
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFlkIAKP 485
Cdd:PLN00034  302 REFRHFISCCLQREPAKRWSAMQLLQHPF--ILRA 334
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
75-110 2.21e-14

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 66.85  E-value: 2.21e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1774959464   75 ISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTS 110
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFTGLPTEWKSLLKTS 36
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
274-428 1.37e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 57.11  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEILVMR---ENKN------PNIVNYLDsylVGDE---LW 341
Cdd:NF033483   13 ERIGRGGMAEVYLAKDTRLDRDVAVKVL------RPDLARDPEFVARfrrEAQSaaslshPNIVSVYD---VGEDggiPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVTE-------TCMD-EGQIAA----------VCREITPE--------------------------- 376
Cdd:NF033483   84 IVMEYVDGRTLKDYIREhgplspeEAVEiMIQILSalehahrngiVHRDIKPQnilitkdgrvkvtdfgiaralssttmt 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 377 QSkrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP 428
Cdd:NF033483  164 QT--NSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSP 213
 
Name Accession Description Interval E-value
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
249-503 2.68e-175

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: 494.63  E-value: 2.68e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 249 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV 328
Cdd:cd06654     1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 329 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRE------------------------------------ 372
Cdd:cd06654    81 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCREclqaleflhsnqvihrdiksdnillgmdgsvkltdf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 -----ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 447
Cdd:cd06654   161 gfcaqITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774959464 448 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 503
Cdd:cd06654   241 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 296
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
250-503 1.50e-169

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: 479.99  E-value: 1.50e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 250 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 329
Cdd:cd06656     1 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 330 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRE------------------------------------- 372
Cdd:cd06656    81 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCREclqaldflhsnqvihrdiksdnillgmdgsvkltdfg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 ----ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEK 448
Cdd:cd06656   161 fcaqITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 503
Cdd:cd06656   241 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNS 295
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
262-481 2.39e-164

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: 465.56  E-value: 2.39e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 262 SVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 341
Cdd:cd06647     1 SVGDPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRE-----------------------------------------ITPEQSKR 380
Cdd:cd06647    81 VVMEYLAGGSLTDVVTETCMDEGQIAAVCREclqaleflhsnqvihrdiksdnillgmdgsvkltdfgfcaqITPEQSKR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRC 460
Cdd:cd06647   161 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRC 240
                         250       260
                  ....*....|....*....|.
gi 1774959464 461 LEMDVEKRGSAKELLQHQFLK 481
Cdd:cd06647   241 LEMDVEKRGSAKELLQHPFLK 261
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
250-503 4.44e-159

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: 453.41  E-value: 4.44e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 250 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 329
Cdd:cd06655     1 DEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 330 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRE------------------------------------- 372
Cdd:cd06655    81 FLDSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCREclqaleflhanqvihrdiksdnvllgmdgsvkltdfg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 ----ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEK 448
Cdd:cd06655   161 fcaqITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 503
Cdd:cd06655   241 LSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSN 295
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
269-481 4.54e-128

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: 372.70  E-value: 4.54e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQ-NKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTET--CMDEGQIAAVCREI-----------------------------------------TPEQSKRSTMVG 385
Cdd:cd06614    80 GGSLTDIITQNpvRMNESQIAYVCREVlqgleylhsqnvihrdiksdnillskdgsvkladfgfaaqlTKEKSKRNSVVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd06614   160 TPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFLNKCLVKDP 239
                         250
                  ....*....|....*.
gi 1774959464 466 EKRGSAKELLQHQFLK 481
Cdd:cd06614   240 EKRPSAEELLQHPFLK 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
269-480 2.74e-103

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: 309.52  E-value: 2.74e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTETC--MDEGQIAAVCREI-----------------------------------------TPEQSkRSTMVG 385
Cdd:cd05122    81 GGSLKDLLKNTNktLTEQQIAYVCKEVlkgleylhshgiihrdikaanilltsdgevklidfglsaqlSDGKT-RNTFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd05122   160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFKDFLKKCLQKDP 239
                         250
                  ....*....|....*
gi 1774959464 466 EKRGSAKELLQHQFL 480
Cdd:cd05122   240 EKRPTAEQLLKHPFI 254
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
262-481 1.99e-96

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: 292.42  E-value: 1.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 262 SVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 341
Cdd:cd06648     1 SPGDPRSDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVTETCMDEGQIAAVCR-----------------------------------------EITPEQSKR 380
Cdd:cd06648    81 VVMEFLEGGALTDIVTHTRMNEEQIATVCRavlkalsflhsqgvihrdiksdsilltsdgrvklsdfgfcaQVSKEVPRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRC 460
Cdd:cd06648   161 KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRM 240
                         250       260
                  ....*....|....*....|.
gi 1774959464 461 LEMDVEKRGSAKELLQHQFLK 481
Cdd:cd06648   241 LVRDPAQRATAAELLNHPFLA 261
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
248-500 2.52e-80

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: 252.21  E-value: 2.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 248 MSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNI 327
Cdd:cd06659     1 VTHEQFKAALRMVVDQGDPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 328 VNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAV-------------------------------------- 369
Cdd:cd06659    81 VEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVceavlqalaylhsqgvihrdiksdsilltldgrvklsd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 370 ---CREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP 446
Cdd:cd06659   161 fgfCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1774959464 447 EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEAT 500
Cdd:cd06659   241 HKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVPLIQQYRKRT 294
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
268-493 5.41e-77

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: 242.92  E-value: 5.41e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEiEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTETCMDEGQIAAVCREI-----------------------------------------TPEQSKRSTMVG 385
Cdd:cd06609    81 CGGGSVLDLLKPGPLDETYIAFILREVllgleylhsegkihrdikaanillseegdvkladfgvsgqlTSTMSKRNTFVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQnPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd06609   161 TPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLE-GNKFSKPFKDFVELCLNKDP 239
                         250       260
                  ....*....|....*....|....*...
gi 1774959464 466 EKRGSAKELLQHQFLKIAKPLSSLTPLI 493
Cdd:cd06609   240 KERPSAKELLKHKFIKKAKKTSYLTLLI 267
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
247-493 1.07e-76

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: 242.64  E-value: 1.07e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 247 KMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPN 326
Cdd:cd06658     1 RVSHEQFRAALQLVVSPGDPREYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 327 IVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVC------------------------------------ 370
Cdd:cd06658    81 VVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVClsvlralsylhnqgvihrdiksdsilltsdgrikls 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 371 -----REITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQN 445
Cdd:cd06658   161 dfgfcAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1774959464 446 PEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLI 493
Cdd:cd06658   241 SHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLKLAGPPSCIVPLM 288
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
249-493 2.19e-74

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: 236.84  E-value: 2.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 249 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV 328
Cdd:cd06657     1 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 329 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVC-------------------------------------- 370
Cdd:cd06657    81 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVClavlkalsvlhaqgvihrdiksdsillthdgrvklsdf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 371 ---REITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 447
Cdd:cd06657   161 gfcAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLH 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464 448 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLI 493
Cdd:cd06657   241 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVPLM 286
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
269-479 1.39e-71

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: 228.34  E-value: 1.39e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTETC-MDEGQIAAVCRE-----------------------------------------ITPEQSKRSTMVGT 386
Cdd:cd06613    81 GGSLQDIYQVTGpLSELQIAYVCREtlkglaylhstgkihrdikganilltedgdvkladfgvsaqLTATIAKRKSFIGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEV--VTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSAIFRDFLNRCL 461
Cdd:cd06613   161 PYWMAPEVaaVERKGgYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNfdPPKLKDKEKWSPDFHDFIKKCL 240
                         250
                  ....*....|....*...
gi 1774959464 462 EMDVEKRGSAKELLQHQF 479
Cdd:cd06613   241 TKNPKKRPTATKLLQHPF 258
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
266-480 1.57e-70

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: 225.61  E-value: 1.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQqqPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd06612     1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVE--EDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVVTETC--MDEGQIAAVCR-----------------------------------------EITPEQSKRST 382
Cdd:cd06612    79 YCGAGSVSDIMKITNktLTEEEIAAILYqtlkgleylhsnkkihrdikagnillneegqakladfgvsgQLTDTMAKRNT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLE 462
Cdd:cd06612   159 VIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLV 238
                         250
                  ....*....|....*...
gi 1774959464 463 MDVEKRGSAKELLQHQFL 480
Cdd:cd06612   239 KDPEERPSAIQLLQHPFI 256
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
270-480 5.60e-70

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 223.95  E-value: 5.60e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  349 GGSLTDVVTET-CMDEGQIAAVCREIT-----------------PE-----------------------QSKRSTMVGTP 387
Cdd:smart00220  81 GGDLFDLLKKRgRLSEDEARFYLRQILsaleylhskgivhrdlkPEnilldedghvkladfglarqldpGEKLTTFVGTP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE-KLSAIFRDFLNRCLEMDVE 466
Cdd:smart00220 161 EYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKDPE 240
                          250
                   ....*....|....
gi 1774959464  467 KRGSAKELLQHQFL 480
Cdd:smart00220 241 KRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
270-480 4.03e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 217.88  E-value: 4.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVTE-TCMDEGQIAAVCREIT---PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:pfam00069  81 EGGSLFDLLSEkGAFSEREAKFIMKQILeglESGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 424 LNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:pfam00069 161 PGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
269-480 5.98e-64

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: 208.53  E-value: 5.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELeaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVV-TETCMDEGQIAAVCREI------------------------TPE---------QSKR----------ST 382
Cdd:cd06606    81 VPGGSLASLLkKFGKLPEPVVRKYTRQIlegleylhsngivhrdikganilvDSDgvvkladfgCAKRlaeiatgegtKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGT-PELqnPEKLSAIFRDFLNRC 460
Cdd:cd06606   161 LRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEpPPI--PEHLSEEAKDFLRKC 238
                         250       260
                  ....*....|....*....|
gi 1774959464 461 LEMDVEKRGSAKELLQHQFL 480
Cdd:cd06606   239 LQRDPKKRPTADELLQHPFL 258
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
268-479 6.22e-59

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: 195.65  E-value: 6.22e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKcQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDV----VTETCMDEGQIAAVCREI------------------------------------------TPEQSK- 379
Cdd:cd06610    81 LSGGSLLDImkssYPRGGLDEAIIATVLKEVlkgleylhsngqihrdvkagnillgedgsvkiadfgvsaslaTGGDRTr 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 --RSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQN---PEKLSAIF 453
Cdd:cd06610   161 kvRKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETgadYKKYSKSF 240
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd06610   241 RKMISLCLQKDPSKRPTAEELLKHKF 266
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
265-480 1.07e-57

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: 192.52  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKElIINEILVMRENKN-PNIVNYLDSYL------VG 337
Cdd:cd06608     3 DPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEE-IKLEINILRKFSNhPNIATFYGAFIkkdppgGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 DELWVVMEYLAGGSLTDVVTET-----CMDEGQIAAVCREI--------------------------------------- 373
Cdd:cd06608    82 DQLWLVMEYCGGGSVTDLVKGLrkkgkRLKEEWIAYILRETlrglaylhenkvihrdikgqnillteeaevklvdfgvsa 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 --TPEQSKRSTMVGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP 446
Cdd:cd06608   162 qlDSTLGRRNTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSP 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774959464 447 EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06608   242 EKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
269-480 3.36e-55

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: 185.51  E-value: 3.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLksVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVT------ETCM---------------DEGQI-----AA----------------VCREITPEQSKRSTMV 384
Cdd:cd06627    81 VENGSLASIIKkfgkfpESLVavyiyqvleglaylhEQGVIhrdikGAnilttkdglvkladfgVATKLNEVEKDENSVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMD 464
Cdd:cd06627   161 GTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPL--PENISPELRDFLLQCFQKD 238
                         250
                  ....*....|....*.
gi 1774959464 465 VEKRGSAKELLQHQFL 480
Cdd:cd06627   239 PTLRPSAKELLKHPWL 254
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
270-494 9.49e-55

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: 184.99  E-value: 9.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQqPKKEL--IINEILVM---RENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT-DDDDVsdIQKEVALLsqlKLGQPKNIIKYYGSYLKGPSLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVTETCMDEGQIAAVCRE------------------------ITPE-----------------QSKRSTM 383
Cdd:cd06917    82 DYCEGGSIRTLMRAGPIAERYIAVIMREvlvalkfihkdgiihrdikaanilVTNTgnvklcdfgvaaslnqnSSKRSTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqNPEKLSAIFRDFLNRCLE 462
Cdd:cd06917   162 VGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRL-EGNGYSPLLKEFVAACLD 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774959464 463 MDVEKRGSAKELLQHQFLKI--AKPLSSLTPLIA 494
Cdd:cd06917   241 EEPKDRLSADELLKSKWIKQhsKTPTSVLKELIS 274
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
276-489 1.71e-52

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: 179.17  E-value: 1.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALDSI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 V--TETCMDEGQIAAVCREI-----------------------------------------TPEQSKRSTMVGTPYWMAP 392
Cdd:cd06611    93 MleLERGLTEPQIRYVCRQMlealnflhshkvihrdlkagnilltldgdvkladfgvsaknKSTLQKRDTFIGTPYWMAP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 393 EVV---TRK--AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd06611   173 EVVaceTFKdnPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSKWSSSFNDFLKSCLVKDPDD 252
                         250       260
                  ....*....|....*....|....*
gi 1774959464 468 RGSAKELLQHQFLKIA---KPLSSL 489
Cdd:cd06611   253 RPTAAELLKHPFVSDQsdnKAIKDL 277
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
265-497 3.61e-52

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: 178.33  E-value: 3.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd06642     1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTETCMDEGQIAAVCREI-----------------------------------------TPEQSKRST 382
Cdd:cd06642    81 MEYLGGGSALDLLKPGPLEETYIATILREIlkgldylhserkihrdikaanvllseqgdvkladfgvagqlTDTQIKRNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNpeKLSAIFRDFLNRCLE 462
Cdd:cd06642   161 FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEG--QHSKPFKEFVEACLN 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1774959464 463 MDVEKRGSAKELLQHQFL-KIAKPLSSLTPLIAAAK 497
Cdd:cd06642   239 KDPRFRPTAKELLKHKFItRYTKKTSFLTELIDRYK 274
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
265-493 1.39e-50

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: 174.09  E-value: 1.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd06640     1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTETCMDEGQIAAVCREI-----------------------------------------TPEQSKRST 382
Cdd:cd06640    81 MEYLGGGSALDLLRAGPFDEFQIATMLKEIlkgldylhsekkihrdikaanvllseqgdvkladfgvagqlTDTQIKRNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNpeKLSAIFRDFLNRCLE 462
Cdd:cd06640   161 FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVG--DFSKPFKEFIDACLN 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1774959464 463 MDVEKRGSAKELLQHQFL-KIAKPLSSLTPLI 493
Cdd:cd06640   239 KDPSFRPTAKELLKHKFIvKNAKKTSYLTELI 270
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
265-493 1.16e-48

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: 169.10  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd06641     1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTETCMDEGQIAAVCREI-----------------------------------------TPEQSKRST 382
Cdd:cd06641    81 MEYLGGGSALDLLEPGPLDETQIATILREIlkgldylhsekkihrdikaanvllsehgevkladfgvagqlTDTQIKRN* 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNpeKLSAIFRDFLNRCLE 462
Cdd:cd06641   161 FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEG--NYSKPLKEFVEACLN 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1774959464 463 MDVEKRGSAKELLQHQF-LKIAKPLSSLTPLI 493
Cdd:cd06641   239 KEPSFRPTAKELLKHKFiLRNAKKTSYLTELI 270
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
268-480 1.74e-48

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: 168.01  E-value: 1.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd06607     1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYsgkQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGgSLTDV--VTETCMDEGQIAAVC-----------------REI--------TPEQSK------------RSTMVG 385
Cdd:cd06607    81 EYCLG-SASDIveVHKKPLQEVEIAAIChgalqglaylhshnrihRDVkagnilltEPGTVKladfgsaslvcpANSFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEkLSAIFRDFLNRCLE 462
Cdd:cd06607   160 TPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLSSGE-WSDDFRNFVDSCLQ 238
                         250
                  ....*....|....*...
gi 1774959464 463 MDVEKRGSAKELLQHQFL 480
Cdd:cd06607   239 KIPQDRPSAEDLLKHPFV 256
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
265-497 1.63e-46

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: 163.27  E-value: 1.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd06643     2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVTE--TCMDEGQIAAVCREI-----------------------------------------TPEQSKRS 381
Cdd:cd06643    82 EFCAGGAVDAVMLEleRPLTEPQIRVVCKQTlealvylhenkiihrdlkagnilftldgdikladfgvsaknTRTLQRRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDF 456
Cdd:cd06643   162 SFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSPEFKDF 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAK 497
Cdd:cd06643   242 LRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLRELIAEAK 282
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
269-479 4.11e-46

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: 161.49  E-value: 4.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEdeEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTD-VVTETCMDEGQIAAVCREIT-----------------PE--------------------------QSKRST 382
Cdd:cd05117    81 CTGGELFDrIVKKGSFSEREAAKIMKQILsavaylhsqgivhrdlkPEnillaskdpdspikiidfglakifeeGEKLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPE--KLSAIFRDFLNRC 460
Cdd:cd05117   161 VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKI-LKGKYSFDSPEwkNVSEEAKDLIKRL 239
                         250
                  ....*....|....*....
gi 1774959464 461 LEMDVEKRGSAKELLQHQF 479
Cdd:cd05117   240 LVVDPKKRLTAAEALNHPW 258
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
265-501 8.23e-46

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: 162.51  E-value: 8.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 341
Cdd:cd06633    18 DPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYsgkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAW 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGgSLTDV--VTETCMDEGQIAAVC-----------------REIT--------PEQ------------SKRST 382
Cdd:cd06633    98 LVMEYCLG-SASDLleVHKKPLQEVEIAAIThgalqglaylhshnmihRDIKagnilltePGQvkladfgsasiaSPANS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEkLSAIFRDFLNR 459
Cdd:cd06633   177 FVGTPYWMAPEVIlamDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNE-WTDSFRGFVDY 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATK 501
Cdd:cd06633   256 CLQKIPQERPSSAELLRHDFVRRERPPRVLIDLIQRTKDAVR 297
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
265-480 2.03e-45

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: 160.19  E-value: 2.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd06646     6 NPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVTETC-MDEGQIAAVCRE-----------------------------------------ITPEQSKRST 382
Cdd:cd06646    86 EYCGGGSLQDIYHVTGpLSELQIAYVCREtlqglaylhskgkmhrdikganilltdngdvkladfgvaakITATIAKRKS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSAIFRDFL 457
Cdd:cd06646   166 FIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNfqPPKLKDKTKWSSTFHNFV 245
                         250       260
                  ....*....|....*....|...
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06646   246 KISLTKNPKKRPTAERLLTHLFV 268
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
265-480 1.59e-43

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: 155.20  E-value: 1.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd06645     8 NPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVTETC-MDEGQIAAVCRE-----------------------------------------ITPEQSKRST 382
Cdd:cd06645    88 EFCGGGSLQDIYHVTGpLSESQIAYVSREtlqglyylhskgkmhrdikganilltdnghvkladfgvsaqITATIAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEV--VTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSAIFRDFL 457
Cdd:cd06645   168 FIGTPYWMAPEVaaVERKGgYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNfqPPKLKDKMKWSNSFHHFV 247
                         250       260
                  ....*....|....*....|...
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06645   248 KMALTKNPKKRPTAEKLLQHPFV 270
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
269-480 1.91e-43

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 154.54  E-value: 1.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEreEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTETCMDEG------------QIAA----------------------------------VCREITPEQSKR 380
Cdd:cd08215    81 ADGGDLAQKIKKQKKKGQpfpeeqildwfvQICLalkylhsrkilhrdlktqnifltkdgvvklgdfgISKVLESTTDLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPElQNPEKLSAIFRDFLNRC 460
Cdd:cd08215   161 KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANN-LPALVYKIVKGQYP-PIPSQYSSELRDLVNSM 238
                         250       260
                  ....*....|....*....|
gi 1774959464 461 LEMDVEKRGSAKELLQHQFL 480
Cdd:cd08215   239 LQKDPEKRPSANEILSSPFI 258
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
258-480 3.27e-43

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: 154.78  E-value: 3.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 258 RSIV--SVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYL 335
Cdd:cd06638     6 KTIIfdSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 336 -----VGDELWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRE--------------------------------- 372
Cdd:cd06638    86 kkdvkNGDQLWLVLELCNGGSVTDLVKGFLkrgerMEEPIIAYILHEalmglqhlhvnktihrdvkgnnilltteggvkl 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 --------ITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG 439
Cdd:cd06638   166 vdfgvsaqLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNP 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1774959464 440 TPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06638   246 PPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
265-501 4.48e-42

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: 152.51  E-value: 4.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 341
Cdd:cd06635    22 DPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYsgkQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAW 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGgSLTDV--VTETCMDEGQIAAVC-----------------REIT--------PEQ------------SKRST 382
Cdd:cd06635   102 LVMEYCLG-SASDLleVHKKPLQEIEIAAIThgalqglaylhshnmihRDIKagnilltePGQvkladfgsasiaSPANS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEkLSAIFRDFLNR 459
Cdd:cd06635   181 FVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNE-WSDYFRNFVDS 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATK 501
Cdd:cd06635   260 CLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVR 301
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
276-479 6.14e-42

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: 150.58  E-value: 6.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQ---QPKKELII--NEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPintEASKEVKAleCEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDVVTET-CMDEG-------QI----------AAVCREITPEQ----------------SKR----------STMVGT 386
Cdd:cd06625    88 SVKDEIKAYgALTENvtrkytrQIleglaylhsnMIVHRDIKGANilrdsngnvklgdfgaSKRlqticsstgmKSVTGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd06625   168 PYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTnPQL--PPHVSEDARDFLSLIFVRNK 245
                         250
                  ....*....|....
gi 1774959464 466 EKRGSAKELLQHQF 479
Cdd:cd06625   246 KQRPSAEELLSHSF 259
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
265-497 7.81e-42

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: 151.34  E-value: 7.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd06644     9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVTEtcMDEG----QIAAVCREI-----------------------------------------TPEQSK 379
Cdd:cd06644    89 EFCPGGAVDAIMLE--LDRGltepQIQVICRQMlealqylhsmkiihrdlkagnvlltldgdikladfgvsaknVKTLQR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 RSTMVGTPYWMAPEVV---TRK--AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFR 454
Cdd:cd06644   167 RDSFIGTPYWMAPEVVmceTMKdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPSKWSMEFR 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAK 497
Cdd:cd06644   247 DFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPLRELVAEAK 289
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
260-480 8.37e-42

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: 150.93  E-value: 8.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 260 IVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV--- 336
Cdd:cd06636     8 LSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKksp 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 337 ---GDELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCREITPEQS-------------------------------- 378
Cdd:cd06636    88 pghDDQLWLVMEFCGAGSVTDLVKNTkgnALKEDWIAYICREILRGLAhlhahkvihrdikgqnvlltenaevklvdfgv 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 ---------KRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQ 444
Cdd:cd06636   168 saqldrtvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLK 247
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1774959464 445 NpEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06636   248 S-KKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
275-480 9.52e-42

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: 150.15  E-value: 9.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQ--QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd06626     7 KIGEGTFGKVYTAVNLDTGELMAMKEIRFQdnDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTETCM-DEGQIAA-----------------VCREITPEQ--------------------SKRSTM---------VG 385
Cdd:cd06626    87 EELLRHGRIlDEAVIRVytlqlleglaylhengiVHRDIKPANifldsngliklgdfgsavklKNNTTTmapgevnslVG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCL 461
Cdd:cd06626   167 TPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWSElDNEWAIMYHVGMGHKPPIPDSLQLSPEGKDFLSRCL 246
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd06626   247 ESDPKKRPTASELLDHPFI 265
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
276-477 1.21e-40

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: 145.49  E-value: 1.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 354
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKlLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 VVTE--TCMDE-------GQIA----------------------------------AVCREITPEQSKRSTMVG--TPYW 389
Cdd:cd00180    81 LLKEnkGPLSEeealsilRQLLsaleylhsngiihrdlkpenilldsdgtvkladfGLAKDLDSDDSLLKTTGGttPPYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEgeppylnenplralyliatngtpelqnpeklsaiFRDFLNRCLEMDVEKRG 469
Cdd:cd00180   161 APPELLGGRYYGPKVDIWSLGVILYELEE----------------------------------LKDLIRRMLQYDPKKRP 206

                  ....*...
gi 1774959464 470 SAKELLQH 477
Cdd:cd00180   207 SAKELLEH 214
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
265-501 8.00e-40

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: 146.32  E-value: 8.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 341
Cdd:cd06634    12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYsgkQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGgSLTDV--VTETCMDEGQIAAVC-----------------REIT--------PEQSK------------RST 382
Cdd:cd06634    92 LVMEYCLG-SASDLleVHKKPLQEVEIAAIThgalqglaylhshnmihRDVKagnilltePGLVKlgdfgsasimapANS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNpEKLSAIFRDFLNR 459
Cdd:cd06634   171 FVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQS-GHWSEYFRNFVDS 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATK 501
Cdd:cd06634   250 CLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLIQRTKDAVR 291
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
262-481 5.29e-39

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: 143.59  E-value: 5.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 262 SVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKElIINEILVMRENKN-PNIVN-----YLDSYL 335
Cdd:cd06639    16 SLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEE-IEAEYNILRSLPNhPNVVKfygmfYKADQY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 336 VGDELWVVMEYLAGGSLTDVVTETC-----MDEGQIA-----------------------------------------AV 369
Cdd:cd06639    95 VGGQLWLVLELCNGGSVTELVKGLLkcgqrLDEAMISyilygallglqhlhnnriihrdvkgnnilltteggvklvdfGV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 370 CREITPEQSKRSTMVGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQ 444
Cdd:cd06639   175 SAQLTSARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLL 254
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1774959464 445 NPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd06639   255 NPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
273-481 1.38e-38

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: 141.07  E-value: 1.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FE---KIGQGASGTVYTAMDVATGQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14007     2 FEigkPLGKGKFGNVYLAREKKSGFIVALKVIsksQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSL-TDVVTETCMDEGQ----IAAVC-------------REITPE----------------------QSKRSTMVGT 386
Cdd:cd14007    82 APNGELyKELKKQKRFDEKEaakyIYQLAlaldylhskniihRDIKPEnillgsngelkladfgwsvhapSNRRKTFCGT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEKLSAIFRDFLNRCLEMDVE 466
Cdd:cd14007   162 LDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQ---NVDIKFPSSVSPEAKDLISKLLQKDPS 238
                         250
                  ....*....|....*
gi 1774959464 467 KRGSAKELLQHQFLK 481
Cdd:cd14007   239 KRLSLEQVLNHPWIK 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
269-480 9.59e-38

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: 139.21  E-value: 9.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL------QQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd06628     1 KWIKGALIGSGSFGSVYLGMNASSGELMAVKQVELpsvsaeNKDRKKSMLdalQREIALLRELQHENIVQYLGSSSDANH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCREI--------------------------------------------- 373
Cdd:cd06628    81 LNIFLEYVPGGSVATLLNNyGAFEESLVRNFVRQIlkglnylhnrgiihrdikganilvdnkggikisdfgiskkleans 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 --TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSA 451
Cdd:cd06628   161 lsTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTI--PSNISS 238
                         250       260
                  ....*....|....*....|....*....
gi 1774959464 452 IFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06628   239 EARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
269-476 3.17e-37

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: 137.72  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRerfLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVVTE-TCMDEGQIAAVCREI------------------------------------------TPEQSKRST 382
Cdd:cd14014    81 YVEGGSLADLLRErGPLPPREALRILAQIadalaaahragivhrdikpanilltedgrvkltdfgiaralgDSGLTQTGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN-GTPELQNPEKLSAIFRDFLNRCL 461
Cdd:cd14014   161 VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEaPPPPSPLNPDVPPALDAIILRAL 240
                         250
                  ....*....|....*.
gi 1774959464 462 EMDVEKR-GSAKELLQ 476
Cdd:cd14014   241 AKDPEERpQSAAELLA 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
275-481 6.01e-37

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 136.95  E-value: 6.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQP-KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd06623     8 VLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEeFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTET-CMDEGQIAAVCREI------------------------------------------TPEQSKRSTMVGTPYWM 390
Cdd:cd06623    88 DLLKKVgKIPEPVLAYIARQIlkgldylhtkrhiihrdikpsnllinskgevkiadfgiskvlENTLDQCNTFVGTVTYM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLR--ALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd06623   168 SPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSffELMQAICDGPPPSLPAEEFSPEFRDFISACLQKDPKKR 247
                         250
                  ....*....|...
gi 1774959464 469 GSAKELLQHQFLK 481
Cdd:cd06623   248 PSAAELLQHPFIK 260
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
350-488 6.14e-37

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: 134.06  E-value: 6.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  350 GSLTDVVT--ETCMDEGQIAAVCRE---------------------------------ITPEQSKrstmvGTPYWMAPEV 394
Cdd:smart00750   1 VSLADILEvrGRPLNEEEIWAVCLQclgalrelhrqaksgnilltwdgllkldgsvafKTPEQSR-----PDPYFMAPEV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  395 VTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPEL-----QNPEKLSA--IFRDFLNRCLEMDVEK 467
Cdd:smart00750  76 IQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADdprdrSNLEGVSAarSFEDFMRLCASRLPQR 155
                          170       180
                   ....*....|....*....|.
gi 1774959464  468 RGSAKELLQHQFLKIAKPLSS 488
Cdd:smart00750 156 REAANHYLAHCRALFAETLEL 176
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
274-477 9.91e-37

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: 136.11  E-value: 9.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd14003     6 KTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEieEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTD-VVTETCMDEGQ--------IAAVC---------REITPE-----------------------QSKRSTMVGTPYWM 390
Cdd:cd14003    86 LFDyIVNNGRLSEDEarrffqqlISAVDychsngivhRDLKLEnilldkngnlkiidfglsnefrgGSLLKTFCGTPAYA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEKRG 469
Cdd:cd14003   166 APEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDN-DSKLFRKILKGKYPI--PSHLSPDARDLIRRMLVVDPSKRI 242

                  ....*...
gi 1774959464 470 SAKELLQH 477
Cdd:cd14003   243 TIEEILNH 250
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
269-480 1.71e-36

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: 135.61  E-value: 1.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK-----ELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd06632     1 RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKsresvKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTE-TCMDEGQIAAVCREI----------------------------------------TPEQSKRST 382
Cdd:cd06632    81 LEYVPGGSIHKLLQRyGAFEEPVIRLYTRQIlsglaylhsrntvhrdikganilvdtngvvkladfgmakhVEAFSFAKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRK--AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG-TPELqnPEKLSAIFRDFLNR 459
Cdd:cd06632   161 FKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGeLPPI--PDHLSPDAKDFIRL 238
                         250       260
                  ....*....|....*....|.
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06632   239 CLQRDPEDRPTASQLLEHPFV 259
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
265-481 2.34e-36

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: 136.39  E-value: 2.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYL------VGD 338
Cdd:cd06637     3 DPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIkknppgMDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCREITPEQS------------------------------------- 378
Cdd:cd06637    83 QLWLVMEFCGAGSVTDLIKNTkgnTLKEEWIAYICREILRGLShlhqhkvihrdikgqnvlltenaevklvdfgvsaqld 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 ----KRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNpEKL 449
Cdd:cd06637   163 rtvgRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKS-KKW 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1774959464 450 SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd06637   242 SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
270-480 2.64e-36

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: 135.26  E-value: 2.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMdVATGQEVAIKQMNL--------QQQPKKelIINEILVMRENKNPNIVNYLDSYLVGDELW 341
Cdd:cd06631     3 WKKGNVLGKGAYGTVYCGL-TSTGQLIAVKQVELdtsdkekaEKEYEK--LQEEVDLLKTLKHVNIVGYLGTCLEDNVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVT-------------------------ETC-------------MDEGQIAAV---C-REITPEQSK 379
Cdd:cd06631    80 IFMEFVPGGSIASILArfgaleepvfcrytkqilegvaylhNNNvihrdikgnnimlMPNGVIKLIdfgCaKRLCINLSS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 RS------TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIF 453
Cdd:cd06631   160 GSqsqllkSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLPDKFSPEA 239
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06631   240 RDFVHACLTRDQDERPSAEQLLKHPFI 266
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
269-476 5.93e-36

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 139.38  E-value: 5.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:COG0515     8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpeLAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVVTET-CMDEGQIAAVCREI------------------------------------------TPEQSKRST 382
Cdd:COG0515    88 YVEGESLADLLRRRgPLPPAEALRILAQLaealaaahaagivhrdikpanilltpdgrvklidfgiaralgGATLTQTGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQ--NPEkLSAIFRDFLNRC 460
Cdd:COG0515   168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSelRPD-LPPALDAIVLRA 246
                         250
                  ....*....|....*..
gi 1774959464 461 LEMDVEKR-GSAKELLQ 476
Cdd:COG0515   247 LAKDPEERyQSAAELAA 263
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
276-479 1.16e-35

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: 133.03  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNlqqqpKKELI--------INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLR-----KKEIIkrkevehtLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVV-TETCMDEGQI---AA--------------VCREITPE------------------------QSKRSTMVG 385
Cdd:cd05123    76 PGGELFSHLsKEGRFPEERArfyAAeivlaleylhslgiIYRDLKPEnilldsdghikltdfglakelssdGDRTYTFCG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd05123   156 TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKS---PLKFPEYVSPEAKSLISGLLQKDP 232
                         250
                  ....*....|....*..
gi 1774959464 466 EKR---GSAKELLQHQF 479
Cdd:cd05123   233 TKRlgsGGAEEIKAHPF 249
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
269-480 3.22e-33

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: 127.11  E-value: 3.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL------QQQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGD 338
Cdd:cd06629     2 KWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVELpktssdRADSRQKTVVDalksEIDTLKDLDHPNIVQYLGFEETED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYLAGGSLTDV----------VTETCMD---EG---------------------QIAAVCREITPEQSKRS--- 381
Cdd:cd06629    82 YFSIFLEYVPGGSIGSClrkygkfeedLVRFFTRqilDGlaylhskgilhrdlkadnilvDLEGICKISDFGISKKSddi 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 -------TMVGTPYWMAPEVV--TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSA 451
Cdd:cd06629   162 ygnngatSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgNKRSAPPVPEDVNLSP 241
                         250       260
                  ....*....|....*....|....*....
gi 1774959464 452 IFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd06629   242 EALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
276-480 8.34e-33

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: 125.98  E-value: 8.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQM---NLQQ-QPKKEliinEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIperDSREvQPLHE----EIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTET----CMDEGQIAAVCREITP------EQ----------------------------SKR--------STMVG 385
Cdd:cd06624    92 LSALLRSKwgplKDNENTIGYYTKQILEglkylhDNkivhrdikgdnvlvntysgvvkisdfgtSKRlaginpctETFTG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPYLNE-NPLRALYLIATNGT-PELqnPEKLSAIFRDFLNRCL 461
Cdd:cd06624   172 TLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKVGMFKIhPEI--PESLSEEAKSFILRCF 249
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd06624   250 EPDPDKRATASDLLQDPFL 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
276-476 1.43e-32

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: 124.57  E-value: 1.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAmdVATGQEVAIKQMNLQ--QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd13999     1 IGSGSFGEVYKG--KWRGTDVAIKKLKVEddNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTETC--------------------------------------MDEGQIAAVC-----REITPEQSKRSTMVGTPYWM 390
Cdd:cd13999    79 DLLHKKKiplswslrlkialdiargmnylhsppiihrdlkslnilLDENFTVKIAdfglsRIKNSTTEKMTGVVGTPRWM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT-PELQN--PEKLSAIfrdfLNRCLEMDVEK 467
Cdd:cd13999   159 APEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLrPPIPPdcPPELSKL----IKRCWNEDPEK 234

                  ....*....
gi 1774959464 468 RGSAKELLQ 476
Cdd:cd13999   235 RPSFSEIVK 243
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
269-480 4.87e-32

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: 123.81  E-value: 4.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSYLVGDE--LWVVM 344
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKmsEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVV-------------------TETC---------------------------MDEGQIA-----AVCREI 373
Cdd:cd08217    81 EYCEGGDLAQLIkkckkenqyipeefiwkifTQLLlalyechnrsvgggkilhrdlkpanifLDSDNNVklgdfGLARVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIF 453
Cdd:cd08217   161 SHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRI--PSRYSSEL 238
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd08217   239 NEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
270-477 1.57e-29

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: 116.76  E-value: 1.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL------IINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd06630     2 WLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSL----------TDVVT---------------ETCM----------------------DEGQIAAVCREITPE 376
Cdd:cd06630    82 VEWMAGGSVasllskygafSENVIinytlqilrglaylhDNQIihrdlkganllvdstgqrlriaDFGAAARLASKGTGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE---NPLRALYLIAT-NGTPELqnPEKLSAI 452
Cdd:cd06630   162 GEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEkisNHLALIFKIASaTTPPPI--PEHLSPG 239
                         250       260
                  ....*....|....*....|....*
gi 1774959464 453 FRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd06630   240 LRDVTLRCLELQPEDRPPARELLKH 264
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
269-480 1.70e-29

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: 116.20  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14002     2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELrnLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 lAGGSLTDVVT-ETCMDEGQIAAVC-----------------REITPE--------QSK-------RS----TMV----- 384
Cdd:cd14002    82 -AQGELFQILEdDGTLPEEEVRSIAkqlvsalhylhsnriihRDMKPQniligkggVVKlcdfgfaRAmscnTLVltsik 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd14002   161 GTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKD---PVKWPSNMSPEFKSFLQGLLNKD 237
                         250
                  ....*....|....*.
gi 1774959464 465 VEKRGSAKELLQHQFL 480
Cdd:cd14002   238 PSKRLSWPDLLEHPFV 253
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
276-372 3.44e-29

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: 111.77  E-value: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNP--NIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLelNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90
                  ....*....|....*....
gi 1774959464 354 DVVTETCMDEGQIAAVCRE 372
Cdd:cd13968    81 AYTQEEELDEKDVESIMYQ 99
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
269-477 1.10e-28

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: 114.34  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKcKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVTET---------CM--DEGQIAA-------VCREITPEQ---------SKR----------------STMV 384
Cdd:cd14095    81 KGGDLFDAITSStkfterdasRMvtDLAQALKylhslsiVHRDIKPENllvvehedgSKSlkladfglatevkeplFTVC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA-LYLIATNGTPELQNP--EKLSAIFRDFLNRCL 461
Cdd:cd14095   161 GTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEeLFDLILAGEFEFLSPywDNISDSAKDLISRML 240
                         250
                  ....*....|....*.
gi 1774959464 462 EMDVEKRGSAKELLQH 477
Cdd:cd14095   241 VVDPEKRYSAGQVLDH 256
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
276-481 1.52e-28

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: 113.98  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE-LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 354
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQkQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLDK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 VVTET-CMDE---GQIA-AVC--------------REITPEQ----------------------SKRSTMVGTPYWMAPE 393
Cdd:cd06605    89 ILKEVgRIPErilGKIAvAVVkgliylhekhkiihRDVKPSNilvnsrgqvklcdfgvsgqlvdSLAKTFVGTRSYMAPE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 394 VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN------PLRALYLIATNGTPELQNpEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd06605   169 RISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNakpsmmIFELLSYIVDEPPPLLPS-GKFSPDFQDFVSQCLQKDPTE 247
                         250
                  ....*....|....
gi 1774959464 468 RGSAKELLQHQFLK 481
Cdd:cd06605   248 RPSYKELMEHPFIK 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
269-480 1.92e-28

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: 114.34  E-value: 1.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd07833     2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEdvKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 L-----------AGGSLTDVVTETCMDEGQIAAVC-------REITPE----------------------QSKRS---TM 383
Cdd:cd07833    82 VertllelleasPGGLPPDAVRSYIWQLLQAIAYChshniihRDIKPEnilvsesgvlklcdfgfaraltARPASpltDY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEV-VTRKAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI---------------------ATNGT 440
Cdd:cd07833   162 VATRWYRAPELlVGDTNYGKPVDVWAIGcIMA-ELLDGEPLFPGDSDIDQLYLIqkclgplppshqelfssnprfAGVAF 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1774959464 441 PELQNPEKLSAIFR--------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07833   241 PEPSQPESLERRYPgkvsspalDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
274-480 4.17e-28

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: 112.50  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd08529     6 NKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRkmREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVV-----------------TETCM-------------------------DEGQIA--AVCREITPEQSKRSTMVGTP 387
Cdd:cd08529    86 LHSLIksqrgrplpedqiwkffIQTLLglshlhskkilhrdiksmnifldkgDNVKIGdlGVAKILSDTTNFAQTIVGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd08529   166 YYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPI--SASYSQDLSQLIDSCLTKDYRQ 243
                         250
                  ....*....|...
gi 1774959464 468 RGSAKELLQHQFL 480
Cdd:cd08529   244 RPDTTELLRNPSL 256
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
269-480 4.41e-28

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: 112.32  E-value: 4.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRF-EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVM- 344
Cdd:cd13983     1 RYLKFnEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERqrFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 -EYLAGGSLTDVVTE-TCMDEGQIAAVCREI----------TP--------------------------------EQSKR 380
Cdd:cd13983    81 tELMTSGTLKQYLKRfKRLKLKVIKSWCRQIleglnylhtrDPpiihrdlkcdnifingntgevkigdlglatllRQSFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKaYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPelqnPEKLSAI----FRDF 456
Cdd:cd13983   161 KSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIK----PESLSKVkdpeLKDF 235
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEmDVEKRGSAKELLQHQFL 480
Cdd:cd13983   236 IEKCLK-PPDERPSARELLEHPFF 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
274-476 3.71e-27

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 109.93  E-value: 3.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  274 EKIGQGASGTVY----TAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:smart00219   5 KKLGEGAFGEVYkgklKGKGGKKKVEVAVKTLKEDASEQqIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  349 GGSLTDVVTET----CMDE-----GQIAA----------------------------------VCREITPEQSKRSTMVG 385
Cdd:smart00219  85 GGDLLSYLRKNrpklSLSDllsfaLQIARgmeylesknfihrdlaarnclvgenlvvkisdfgLSRDLYDDDYYRKRGGK 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  386 TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEM 463
Cdd:smart00219 165 LPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLPQ--PPNCPPELYDLMLQCWAE 242
                          250
                   ....*....|...
gi 1774959464  464 DVEKRGSAKELLQ 476
Cdd:smart00219 243 DPEDRPTFSELVE 255
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
267-477 5.27e-27

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 109.38  E-value: 5.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKAlKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTD-VVTETCMDE-------GQI----------AAVCREITPE---------QSK----------------RST 382
Cdd:cd14083    82 LVTGGELFDrIVEKGSYTEkdashliRQVleavdylhslGIVHRDLKPEnllyyspdeDSKimisdfglskmedsgvMST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP-------LRALYliatngtpELQNP--EKLSAIF 453
Cdd:cd14083   162 ACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDsklfaqiLKAEY--------EFDSPywDDISDSA 233
                         250       260
                  ....*....|....*....|....
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14083   234 KDFIRHLMEKDPNKRYTCEQALEH 257
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
276-479 1.05e-26

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 108.46  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKlqENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DV------VTETC----MdeGQIAA----------VCREITPE--------------------------QSKRSTMVGTP 387
Cdd:cd14009    81 QYirkrgrLPEAVarhfM--QQLASglkflrskniIHRDLKPQnlllstsgddpvlkiadfgfarslqpASMAETLCGSP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFLNRCLEMDVE 466
Cdd:cd14009   159 LYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIeRSDAVIPFPIAAQLSPDCKDLLRRLLRRDPA 238
                         250
                  ....*....|...
gi 1774959464 467 KRGSAKELLQHQF 479
Cdd:cd14009   239 ERISFEEFFAHPF 251
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
74-132 1.78e-26

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 101.62  E-value: 1.78e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464  74 EISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYN 132
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFYS 59
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
274-476 2.91e-26

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 107.25  E-value: 2.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  274 EKIGQGASGTVY----TAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:smart00221   5 KKLGEGAFGEVYkgtlKGKGDGKEVEVAVKTLKEDASEQqIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  349 GGSLTDVV-----TETCMDE-----GQIAA----------------------------------VCREITPEQSKRSTMV 384
Cdd:smart00221  85 GGDLLDYLrknrpKELSLSDllsfaLQIARgmeylesknfihrdlaarnclvgenlvvkisdfgLSRDLYDDDYYKVKGG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  385 GTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLE 462
Cdd:smart00221 165 KLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLPK--PPNCPPELYKLMLQCWA 242
                          250
                   ....*....|....
gi 1774959464  463 MDVEKRGSAKELLQ 476
Cdd:smart00221 243 EDPEDRPTFSELVE 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
276-479 3.39e-26

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: 107.44  E-value: 3.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQ-QQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYLA 348
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKQVQFDpESPETSKEVNalecEIQLLKNLLHERIVQYYGCLRDPQErtLSIFMEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTD------VVTETCMD-------EG--------------QIAAVCREITPE-------QSKR-----------STM 383
Cdd:cd06652    90 GGSIKDqlksygALTENVTRkytrqilEGvhylhsnmivhrdiKGANILRDSVGNvklgdfgASKRlqticlsgtgmKSV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSAIFRDFLNRCLe 462
Cdd:cd06652   170 TGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTnPQL--PAHVSDHCRDFLKRIF- 246
                         250
                  ....*....|....*..
gi 1774959464 463 MDVEKRGSAKELLQHQF 479
Cdd:cd06652   247 VEAKLRPSADELLRHTF 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
267-480 1.41e-25

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: 105.49  E-value: 1.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLVGDEL 340
Cdd:cd14167     2 RDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCI-----AKKALegketsIENEIAVLHKIKHPNIVALDDIYESGGHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLTDVVTE----TCMDEGQI--------------AAVCREITPEQ------------------------- 377
Cdd:cd14167    77 YLIMQLVSGGELFDRIVEkgfyTERDASKLifqildavkylhdmGIVHRDLKPENllyysldedskimisdfglskiegs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 -SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNP--EKLSAIFR 454
Cdd:cd14167   157 gSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAK-LFEQILKAEYEFDSPywDDISDSAK 235
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14167   236 DFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
275-480 2.36e-25

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: 104.64  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd14081     8 TLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVlmkVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTD-VVTETCMDEGQ--------IAAV--------C-REITPEQ-----------------------SKRSTMVGTPYWM 390
Cdd:cd14081    88 LFDyLVKKGRLTEKEarkffrqiISALdychshsiChRDLKPENllldeknnikiadfgmaslqpegSLLETSCGSPHYA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEKRG 469
Cdd:cd14081   168 CPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDN-LRQLLEKVKRGVFHI--PHFISPDAQDLLRRMLEVNPEKRI 244
                         250
                  ....*....|.
gi 1774959464 470 SAKELLQHQFL 480
Cdd:cd14081   245 TIEEIKKHPWF 255
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
275-495 3.47e-25

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: 105.84  E-value: 3.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASG--TVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd08216     5 EIGKCFKGggVVHLAKHKPTNTLVAVKKINLESDSKEDLkfLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDVVTETCMD---EGQIAAVCRE------------------------ITP----------------EQSKRST-MVGT 386
Cdd:cd08216    85 SCRDLLKTHFPEglpELAIAFILRDvlnaleyihskgyihrsvkashilISGdgkvvlsglryaysmvKHGKRQRvVHDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 P-------YWMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGTP--------------EL 443
Cdd:cd08216   165 PksseknlPWLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPF-SDMPATQMLLEKVRGTTpqlldcstypleedSM 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 444 QNPE-------------------KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLS-SLTPLIAA 495
Cdd:cd08216   244 SQSEdsstehpnnrdtrdipyqrTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQCRRSNtSLLDLLKP 315
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
275-478 3.57e-25

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 104.40  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNL--QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd08530     7 KLGKGSYGSVYKVKRLSDNQVYALKEVNLgsLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTET------------------------CMDEGQIaaVCREITPEQSKRS----------------------TMVGT 386
Cdd:cd08530    87 SKLISKRkkkrrlfpeddiwrifiqmlrglkALHDQKI--LHRDLKSANILLSagdlvkigdlgiskvlkknlakTQIGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGT-PELqnPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd08530   165 PLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPF-EARTMQELRYKVCRGKfPPI--PPVYSQDLQQIIRSLLQVNP 241
                         250
                  ....*....|...
gi 1774959464 466 EKRGSAKELLQHQ 478
Cdd:cd08530   242 KKRPSCDKLLQSP 254
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
269-477 5.34e-25

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: 104.09  E-value: 5.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkrkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVtetcMDEGQIAA-VCREIT---------------------PEQ------------------------- 377
Cdd:cd14098    81 EYVEGGDLMDFI----MAWGAIPEqHARELTkqileamaythsmgithrdlkPENilitqddpvivkisdfglakvihtg 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRK------AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPelQNPEK--- 448
Cdd:cd14098   157 TFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYT--QPPLVdfn 234
                         250       260
                  ....*....|....*....|....*....
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14098   235 ISEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
276-479 5.38e-25

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: 103.95  E-value: 5.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQ---QQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYLA 348
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVPFDpdsQETSKEVnaLECEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTD------VVTETCM----------------------------------------DEG---QIAAVCREITPEQSk 379
Cdd:cd06653    90 GGSVKDqlkaygALTENVTrrytrqilqgvsylhsnmivhrdikganilrdsagnvklgDFGaskRIQTICMSGTGIKS- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 rstMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSAIFRDFLN 458
Cdd:cd06653   169 ---VTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTkPQL--PDGVSDACRDFLR 243
                         250       260
                  ....*....|....*....|.
gi 1774959464 459 RcLEMDVEKRGSAKELLQHQF 479
Cdd:cd06653   244 Q-IFVEEKRRPTAEFLLRHPF 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
268-477 7.35e-25

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 103.57  E-value: 7.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE-LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTE-TCMDEGQIAA-----------------VCREITPE-------------------------QSKRSTM 383
Cdd:cd14184    81 VKGGDLFDAITSsTKYTERDASAmvynlasalkylhglciVHRDIKPEnllvceypdgtkslklgdfglatvvEGPLYTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA-LYLIATNGTPELQNP--EKLSAIFRDFLNRC 460
Cdd:cd14184   161 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEdLFDQILLGKLEFPSPywDNITDSAKELISHM 240
                         250
                  ....*....|....*..
gi 1774959464 461 LEMDVEKRGSAKELLQH 477
Cdd:cd14184   241 LQVNVEARYTAEQILSH 257
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
270-480 2.47e-24

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: 101.54  E-value: 2.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnLQQQPKKELIINEILVMRE----NKNPNIVNYLDSYL--VGDELWVV 343
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI-KNDFRHPKAALREIKLLKHlndvEGHPNIVKLLDVFEhrGGNHLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLaGGSLTDVV--TETCMDEGQIAAVC-----------------REITPE-----------------------QSKRS 381
Cdd:cd05118    80 FELM-GMNLYELIkdYPRGLPLDLIKSYLyqllqaldflhsngiihRDLKPEnilinlelgqlkladfglarsftSPPYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPElqnpeklsaiFRDFLNR 459
Cdd:cd05118   159 PYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIvRLLGTPE----------ALDLLSK 228
                         250       260
                  ....*....|....*....|.
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFL 480
Cdd:cd05118   229 MLKYDPAKRITASQALAHPYF 249
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
268-480 3.48e-24

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: 102.09  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQP--------KKELIINEILVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd14084     6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTigsrreinKPRNIETEIEILKKLSHPCIIKIEDFFDAEDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTETCMDEGQIA-----------------AVC-REITPE-------------------QSKRS- 381
Cdd:cd14084    86 YYIVLELMEGGELFDRVVSNKRLKEAICklyfyqmllavkylhsnGIIhRDLKPEnvllssqeeeclikitdfgLSKILg 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 ------TMVGTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQNPEKLS 450
Cdd:cd14084   166 etslmkTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILSGkyTFIPKAWKNVS 245
                         250       260       270
                  ....*....|....*....|....*....|
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14084   246 EEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
276-481 4.30e-24

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: 101.52  E-value: 4.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQM--------NLQQQPKKEliiNEILVMreNKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIkkrdmirkNQVDSVLAE---RNILSQ--AQNPFVVKLYYSFQGKKNLYLVMEYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGG---SLTDVVTetCMDEG-------QIAA----------VCREITPE------------------------------- 376
Cdd:cd05579    76 PGGdlySLLENVG--ALDEDvariyiaEIVLaleylhshgiIHRDLKPDnilidanghlkltdfglskvglvrrqiklsi 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 --------QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELQNPEK 448
Cdd:cd05579   154 qkksngapEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETP-EEIFQNILNGKIEWPEDPE 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKR---GSAKELLQHQFLK 481
Cdd:cd05579   233 VSDEAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFK 268
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
276-480 5.82e-24

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: 101.09  E-value: 5.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN-----------LQQQPKK---ELIINEILVMRENKNPNIVN-Y--LDSyLVGD 338
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkrregkNDRGKIKnalDDVRREIAIMKKLDHPNIVRlYevIDD-PESD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRE-----------------ITPE---QSKR----------STMV- 384
Cdd:cd14008    80 KLYLVLEYCEGGPVMELDSGDrvpPLPEETARKYFRDlvlgleylhengivhrdIKPEnllLTADgtvkisdfgvSEMFe 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 ----------GTPYWMAPEV--VTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLrALYLIATNGTPELQNPEKLSA 451
Cdd:cd14008   160 dgndtlqktaGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNIL-ELYEAIQNQNDEFPIPPELSP 238
                         250       260
                  ....*....|....*....|....*....
gi 1774959464 452 IFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14008   239 ELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
270-480 9.74e-24

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: 100.63  E-value: 9.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNE--EEGIpstaLREISLLKELKHPNIVKLLDVIHTENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAggslTDV-----VTETCMDEGQI--------AAVC---------------------------------REITPEQSK 379
Cdd:cd07829    79 YCD----QDLkkyldKRPGPLPPNLIksimyqllRGLAychshrilhrdlkpqnllinrdgvlkladfglaRAFGIPLRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 RSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI-ATNGTPELQN----------- 445
Cdd:cd07829   155 YTHEVVTLWYRAPEILLGsKHYSTAVDIWSVGcIFA-ELITGKPLFPGDSEIDQLFKIfQILGTPTEESwpgvtklpdyk 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 446 -------PEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07829   234 ptfpkwpKNDLEKVLprldpegIDLLSKMLQYNPAKRISAKEALKHPYF 282
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
73-118 1.12e-23

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 93.49  E-value: 1.12e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464  73 PEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQK 118
Cdd:cd01093     1 PEISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSGITKEEQK 46
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
270-482 1.27e-23

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: 100.16  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQ-QQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDE--LWV 342
Cdd:cd06651     9 WRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDpESPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDRAEktLTI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEYLAGGSLTD------VVTETCMDE--GQI----------AAVCREITPEQ----------------SKR-------- 380
Cdd:cd06651    89 FMEYMPGGSVKDqlkaygALTESVTRKytRQIlegmsylhsnMIVHRDIKGANilrdsagnvklgdfgaSKRlqticmsg 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 ---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSAIFRDF 456
Cdd:cd06651   169 tgiRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHARDF 246
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 457 LnRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd06651   247 L-GCIFVEARHRPSAEELLRHPFAQL 271
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
276-478 2.12e-23

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: 98.88  E-value: 2.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQqPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD- 354
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD-KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 -----VVTETC-------------------------------MDEGQIAAV-------CREITPEQSKRSTMvGTPYWMA 391
Cdd:cd14006    80 laergSLSEEEvrtymrqlleglqylhnhhilhldlkpenilLADRPSPQIkiidfglARKLNPGEELKEIF-GTPEFVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 392 PEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELQNPEK--LSAIFRDFLNRCLEMDVEKRG 469
Cdd:cd14006   159 PEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDD-QETLANISACRVDFSEEYFssVSQEAKDFIRKLLVKEPRKRP 237

                  ....*....
gi 1774959464 470 SAKELLQHQ 478
Cdd:cd14006   238 TAQEALQHP 246
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
268-484 2.20e-23

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 99.80  E-value: 2.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN------LQQQPKKELIINeilvmRENKNPNIVNYLDSYLvgDE-- 339
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITtdpnpdVQKQILRELEIN-----KSCASPYIVKYYGAFL--DEqd 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 --LWVVMEYLAGGSLTDVVTETCMDEGQIAA----------------------VCREITPE------------------- 376
Cdd:cd06621    74 ssIGIAMEYCEGGSLDSIYKKVKKKGGRIGEkvlgkiaesvlkglsylhsrkiIHRDIKPSnilltrkgqvklcdfgvsg 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 ---QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN-----PLRALYLIATNGTPELQNPEK 448
Cdd:cd06621   154 elvNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGepplgPIELLSYIVNMPNPELKDEPE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1774959464 449 L----SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAK 484
Cdd:cd06621   234 NgikwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQE 273
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
276-477 3.53e-23

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: 98.48  E-value: 3.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 354
Cdd:cd14185     8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKlKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 VVTETCMDEGQIAAV-----C-------------REITPEQ------SKRS-------------------TMVGTPYWMA 391
Cdd:cd14185    88 AIIESVKFTEHDAALmiidlCealvyihskhivhRDLKPENllvqhnPDKSttlkladfglakyvtgpifTVCGTPTYVA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 392 PEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGTPELQNP--EKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd14185   168 PEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQLGHYEFLPPywDNISEAAKDLISRLLVVDPEKR 247

                  ....*....
gi 1774959464 469 GSAKELLQH 477
Cdd:cd14185   248 YTAKQVLQH 256
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
270-479 4.30e-23

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: 98.52  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKkelIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPE---VLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTE-TCMDEGQIAAVCREI------------------------------------------------------- 373
Cdd:cd14010    79 GDLETLLRQdGNLPESSVRKFGRDLvrglhyihskgiiycdlkpsnilldgngtlklsdfglarregeilkelfgqfsde 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 --TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP--EKL 449
Cdd:cd14010   159 gnVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKvsSKP 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1774959464 450 SAIFRDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd14010   239 SPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
276-480 9.13e-23

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: 97.30  E-value: 9.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD- 354
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFEr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 ------VVTET---------C-----MDEGQIA--------AVC----------------REITPEQSKRsTMVGTPYWM 390
Cdd:cd14103    81 vvdddfELTERdcilfmrqiCegvqyMHKQGILhldlkpenILCvsrtgnqikiidfglaRKYDPDKKLK-VLFGTPEFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd14103   160 APEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANV-TRAKWDFDDEafDDISDEAKDFISKLLVKDPRKR 238
                         250
                  ....*....|..
gi 1774959464 469 GSAKELLQHQFL 480
Cdd:cd14103   239 MSAAQCLQHPWL 250
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
267-480 9.37e-23

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: 98.14  E-value: 9.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14166     2 RETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTET-CMDEGQIAAVCREI-------------------------TPEQSKR-----------------STM 383
Cdd:cd14166    82 VSGGELFDRILERgVYTEKDASRVINQVlsavkylhengivhrdlkpenllylTPDENSKimitdfglskmeqngimSTA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNP--EKLSAIFRDFLNRCL 461
Cdd:cd14166   162 CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESR-LFEKIKEGYYEFESPfwDDISESAKDFIRHLL 240
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd14166   241 EKNPSKRYTCEKALSHPWI 259
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
268-480 9.75e-23

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: 97.24  E-value: 9.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKvvpKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVV-TETCMDEGQIAAVCREI-----------------------------------------TPEQSKRST 382
Cdd:cd14099    81 ELCSNGSLMELLkRRKALTEPEVRYFMRQIlsgvkylhsnriihrdlklgnlfldenmnvkigdfglaarlEYDGERKKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRK-AYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYL-IATNgtpELQNPEKL--SAIFRDFLN 458
Cdd:cd14099   161 LCGTPNYIAPEVLEKKkGHSFEVDIWSLGVILYTLLVGKPPF-ETSDVKETYKrIKKN---EYSFPSHLsiSDEAKDLIR 236
                         250       260
                  ....*....|....*....|..
gi 1774959464 459 RCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14099   237 SMLQPDPTKRPSLDEILSHPFF 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
268-480 1.11e-22

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: 97.73  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIK-------QMNLQQ-QPKKELIINEILVMRENKN-PNIVNYLDSYLVGD 338
Cdd:cd14181    10 QKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKiievtaeRLSPEQlEEVRSSTLKEIHILRQVSGhPSIITLIDSYESST 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYLAGGSLTDVVTET---------CMDEGQIAAVC---------REITPEQ----------------------- 377
Cdd:cd14181    90 FIFLVFDLMRRGELFDYLTEKvtlseketrSIMRSLLEAVSylhannivhRDLKPENillddqlhiklsdfgfschlepg 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVV------TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPE--KL 449
Cdd:cd14181   170 EKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI-MEGRYQFSSPEwdDR 248
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1774959464 450 SAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14181   249 SSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
275-483 1.12e-22

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: 97.90  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLV-GDELWVVMEYLAGGSL 352
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSvRKQILRELQILHECHSPYIVSFYGAFLNeNNNIIICMEYMDCGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 -------TDVVTETCmdeGQIA-AVC--------------REITPEQ----------------------SKRSTMVGTPY 388
Cdd:cd06620    92 dkilkkkGPFPEEVL---GKIAvAVLegltylynvhriihRDIKPSNilvnskgqiklcdfgvsgelinSIADTFVGTST 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYL-----------IATNGTPELQNPEKLSAIFRDFL 457
Cdd:cd06620   169 YMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNgpmgildllqrIVNEPPPRLPKDRIFPKDLRDFV 248
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFLKIA 483
Cdd:cd06620   249 DRCLLKDPRERPSPQLLLDHDPFIQA 274
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
270-468 1.14e-22

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: 97.57  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEV-AIKQMNLQQ----QPKKEL------IINEILVMREN-KNPNIVNYLDSYLVG 337
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGQTLlALKEINMTNpafgRTEQERdksvgdIISEVNIIKEQlRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 DELWVVMEYLAGGSLTD-------------------VVTETCM------DEGQIaaVCREITP----------------- 375
Cdd:cd08528    82 DRLYIVMELIEGAPLGEhfsslkeknehftedriwnIFVQMVLalrylhKEKQI--VHRDLKPnnimlgeddkvtitdfg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 376 -------EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPEK 448
Cdd:cd08528   160 lakqkgpESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKI-VEAEYEPLPEGM 238
                         250       260
                  ....*....|....*....|
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKR 468
Cdd:cd08528   239 YSDDITFVIRSCLTPDPEAR 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
274-481 1.32e-22

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: 97.22  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAM---DVATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd00192     1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDaSESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMDEG-----------------QIAA----------------------------------VCREITPEQS 378
Cdd:cd00192    81 GDLLDFLRKSRPVFPspepstlslkdllsfaiQIAKgmeylaskkfvhrdlaarnclvgedlvvkisdfgLSRDIYDDDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 KRSTMvGTP---YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIaTNGTpELQNPEKLSAIFR 454
Cdd:cd00192   161 YRKKT-GGKlpiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYL-RKGY-RLPKPENCPDELY 237
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELlqHQFLK 481
Cdd:cd00192   238 ELMLSCWQLDPEDRPTFSEL--VERLE 262
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
273-481 1.62e-22

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: 98.51  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FEK---IGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05573     3 FEVikvIGRGAFGEVWLVRDKDTGQVYAMKILRksdMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLT------DVVTET----------------------------------------------CMD------------ 362
Cdd:cd05573    83 MPGGDLMnllikyDVFPEEtarfyiaelvlaldslhklgfihrdikpdnilldadghikladfglCTKmnksgdresyln 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 363 EGQIAAVCREITPEQSKRS-------TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAlYLI 435
Cdd:cd05573   163 DSVNTLFQDNVLARRRPHKqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVET-YSK 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 436 ATNGTPELQNP--EKLSAIFRDFLNRCLeMDVEKR-GSAKELLQHQFLK 481
Cdd:cd05573   242 IMNWKESLVFPddPDVSPEAIDLIRRLL-CDPEDRlGSAEEIKAHPFFK 289
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
269-480 4.66e-22

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: 95.57  E-value: 4.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQmnLQQQPKKELIINE-ILVMRENK------NPNIVNYLDSYLVGDELW 341
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKV--LKEISVGELQPDEtVDANREAKllskldHPAIVKFHDSFVEKESFC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVTE-----TCMDEGQIAA----------------------------------------VCREITPE 376
Cdd:cd08222    79 IVTEYCEGGDLDDKISEykksgTTIDENQILDwfiqlllavqymherrilhrdlkakniflknnvikvgdfgISRILMGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDF 456
Cdd:cd08222   159 SDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSL--PDKYSKELNAI 236
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd08222   237 YSRMLNKDPALRPSAAEILKIPFI 260
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
270-477 5.74e-22

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: 95.73  E-value: 5.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELII-NEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVeNEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTE----TCMDEGQI--------------AAVCREITPE-------------------------QSKRSTMVG 385
Cdd:cd14169    85 GGELFDRIIErgsyTEKDASQLigqvlqavkylhqlGIVHRDLKPEnllyatpfedskimisdfglskieaQGMLSTACG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNP--EKLSAIFRDFLNRCLEM 463
Cdd:cd14169   165 TPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSE-LFNQILKAEYEFDSPywDDISESAKDFIRHLLER 243
                         250
                  ....*....|....
gi 1774959464 464 DVEKRGSAKELLQH 477
Cdd:cd14169   244 DPEKRFTCEQALQH 257
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
274-479 6.72e-22

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: 95.36  E-value: 6.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDkrhIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDVVTE-TCMDE-------GQIAAVC----------REITPE------------------------------------ 376
Cdd:cd05581    87 DLLEYIRKyGSLDEkctrfytAEIVLALeylhskgiihRDLKPEnilldedmhikitdfgtakvlgpdsspestkgdads 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 -----QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGtpELQNPEKLSA 451
Cdd:cd05581   167 qiaynQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKI-VKL--EYEFPENFPP 243
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774959464 452 IFRDFLNRCLEMDVEKR------GSAKELLQHQF 479
Cdd:cd05581   244 DAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
269-477 8.54e-22

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: 94.80  E-value: 8.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEErqAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTETC---MDEGQIAAVCREIT-----------------------------------------PEQSKRST 382
Cdd:cd08220    81 APGGTLFEYIQQRKgslLSEEEILHFFVQILlalhhvhskqilhrdlktqnillnkkrtvvkigdfgiskilSSKSKAYT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGT--PElqnPEKLSAIFRDFLNRC 460
Cdd:cd08220   161 VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAAN-LPALVLKIMRGTfaPI---SDRYSEELRHLILSM 236
                         250
                  ....*....|....*..
gi 1774959464 461 LEMDVEKRGSAKELLQH 477
Cdd:cd08220   237 LHLDPNKRPTLSEIMAQ 253
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
276-480 1.11e-21

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: 94.25  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd05578     8 IGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDsvrNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 -----TDVVtetcMDEGQIA--AVC---------------REITPE-----------------------QSKRSTMVGTP 387
Cdd:cd05578    88 ryhlqQKVK----FSEETVKfyICEivlaldylhskniihRDIKPDnilldeqghvhitdfniatkltdGTLATSTSGTK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-----ENPLRALYLIATNGTPELQNPEklsaiFRDFLNRCLE 462
Cdd:cd05578   164 PYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIhsrtsIEEIRAKFETASVLYPAGWSEE-----AIDLINKLLE 238
                         250
                  ....*....|....*....
gi 1774959464 463 MDVEKR-GSAKELLQHQFL 480
Cdd:cd05578   239 RDPQKRlGDLSDLKNHPYF 257
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
269-481 1.39e-21

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: 94.95  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIIN-----EILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGINftalrEIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAgGSLTDVVTETCMD--EGQIAA----------VC-------REITPE--------QSK-----RSTMVGTP-YWM 390
Cdd:cd07841    81 FEFME-TDLEKVIKDKSIVltPADIKSymlmtlrgleYLhsnwilhRDLKPNnlliasdgVLKladfgLARSFGSPnRKM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTR-----------KAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI-ATNGTPELQN------------ 445
Cdd:cd07841   160 THQVVTRwyrapellfgaRHYGVGVDMWSVGcIFA-ELLLRVPFLPGDSDIDQLGKIfEALGTPTEENwpgvtslpdyve 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1774959464 446 -----PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07841   239 fkpfpPTPLKQIFPaasddalDLLQRLLTLNPNKRITARQALEHPYFS 286
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
268-480 1.43e-21

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: 94.20  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDvATGQEVAIKQMNLQ---QQPKKELIiNEI-LVMRENKNPNIVNYLDsYLVGDE---L 340
Cdd:cd14131     1 KPYEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEgadEQTLQSYK-NEIeLLKKLKGSDRIIQLYD-YEVTDEddyL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEY----------------LAGGSLTDVVTE------TCMDEGQIAA--------------------VCREITPEQS 378
Cdd:cd14131    78 YMVMECgeidlatilkkkrpkpIDPNFIRYYWKQmleavhTIHEEGIVHSdlkpanfllvkgrlklidfgIAKAIQNDTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 --KRSTMVGTPYWMAPEVVTRKAY----------GPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIaTNGTPELQN 445
Cdd:cd14131   158 siVRDSQVGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAI-IDPNHEIEF 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1774959464 446 PEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14131   237 PDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
270-480 1.53e-21

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: 94.52  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMnLREVKSLRKlNEHPNIVKLKEVFRENDELYFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AgGSLTDVVTE---TCMDEGQIAAVC-----------------REITPE---------------------QSKR--STMV 384
Cdd:cd07830    81 E-GNLYQLMKDrkgKPFSESVIRSIIyqilqglahihkhgffhRDLKPEnllvsgpevvkiadfglareiRSRPpyTDYV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQN-PE--KLSAI--FR--- 454
Cdd:cd07830   160 STRWYRAPEILLRsTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKIcSVLGTPTKQDwPEgyKLASKlgFRfpq 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 455 ------------------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07830   240 faptslhqlipnaspeaiDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
273-468 1.90e-21

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: 94.18  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd05580     6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiikLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSL-TDVVTETCMDEGQI---AA--------------VCREITPEQ----------------SKR-----STMVGTPYWM 390
Cdd:cd05580    86 GELfSLLRRSGRFPNDVAkfyAAevvlaleylhsldiVYRDLKPENllldsdghikitdfgfAKRvkdrtYTLCGTPEYL 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774959464 391 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd05580   166 APEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMK-IYEKILEG--KIRFPSFFDPDAKDLIKRLLVVDLTKR 240
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
269-480 2.39e-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: 93.93  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLqqqPKKE-----LIINEILVMRENK-NPNIVNYLDSYLVGDELWV 342
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVAL---RKLEggipnQALREIKALQACQgHPYVVKLRDVFPHGTGFVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEYLaGGSLTDVV--TETCMDEGQI----------AAVC-------REITP-----------------------EQSKR 380
Cdd:cd07832    78 VFEYM-LSSLSEVLrdEERPLTEAQVkrymrmllkgVAYMhanrimhRDLKPanllisstgvlkiadfglarlfsEEDPR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 --STMVGTPYWMAPEVV--TRKaYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRAL-YLIATNGTPELQN--------- 445
Cdd:cd07832   157 lySHQVATRWYRAPELLygSRK-YDEGVDLWAVGcIFA-ELLNGSPLFPGENDIEQLaIVLRTLGTPNEKTwpeltslpd 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 446 ----------PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07832   235 ynkitfpeskGIRLEEIFPdcspeaiDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
275-476 2.85e-21

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 93.10  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd08224     7 KIGKGQFSVVYRARCLLDGRLVALKKVQifeMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTE-----TCMDEGQI----AAVC-------------REITPEQ--------------------SKRST----MVG 385
Cdd:cd08224    87 LSRLIKHfkkqkRLIPERTIwkyfVQLCsalehmhskrimhRDIKPANvfitangvvklgdlglgrffSSKTTaahsLVG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN-PLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd08224   167 TPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKmNLYSLCKKIEKCEYPPLPADLYSQELRDLVAACIQPD 246
                         250
                  ....*....|..
gi 1774959464 465 VEKRGSAKELLQ 476
Cdd:cd08224   247 PEKRPDISYVLD 258
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
274-479 4.39e-21

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: 92.35  E-value: 4.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAM-DVATGQEVAIKQMNlqqqpKKEL-------IINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14121     1 EKLGSGTYATVYKAYrKSGAREVVAVKCVS-----KSSLnkastenLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVV-TETCMDEG-------QIAA---VCRE---------------------------------ITPEQSKRS 381
Cdd:cd14121    76 YCSGGDLSRFIrSRRTLPEStvrrflqQLASalqFLREhnishmdlkpqnlllssrynpvlkladfgfaqhLKPNDEAHS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 tMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY----LNENPLRalylIATNGTPEL-QNPEkLSAIFRDF 456
Cdd:cd14121   156 -LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFasrsFEELEEK----IRSSKPIEIpTRPE-LSADCRDL 229
                         250       260
                  ....*....|....*....|...
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd14121   230 LLRLLQRDPDRRISFEEFFAHPF 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
186-485 1.71e-20

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 92.96  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 186 PPPVIAPRPEHTKSVYTRSVIEP---LPVtPTRDVATS---PISPTENNTTPPDALTRNTEKQKKKPKMSDeeiLEKLRs 259
Cdd:PLN00034    6 PPPGVPLPSTARHTTKSRPRRRPdltLPL-PQRDPSLAvplPLPPPSSSSSSSSSSSASGSAPSAAKSLSE---LERVN- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 260 ivsvgdpkkkytrfeKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVG 337
Cdd:PLN00034   81 ---------------RIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHN 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 DELWVVMEYLAGGSLTDvvtETCMDEGQIAAVCRE-----------------ITPEQ----SKRS--------------T 382
Cdd:PLN00034  145 GEIQVLLEFMDGGSLEG---THIADEQFLADVARQilsgiaylhrrhivhrdIKPSNllinSAKNvkiadfgvsrilaqT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 M------VGTPYWMAPEVV----TRKAY-GPKVDIWSLGIMAIEMIEGEPPY-LNENPLRALYLIATNGTPELQNPEKLS 450
Cdd:PLN00034  222 MdpcnssVGTIAYMSPERIntdlNHGAYdGYAGDIWSLGVSILEFYLGRFPFgVGRQGDWASLMCAICMSQPPEAPATAS 301
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFlkIAKP 485
Cdd:PLN00034  302 REFRHFISCCLQREPAKRWSAMQLLQHPF--ILRA 334
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
269-479 1.83e-20

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: 91.28  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQ-MNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd07847     2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKfVESEDDPViKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTET-CMDEGQIAAVC-----------------REITPEQ---SKRSTM---------------------V 384
Cdd:cd07847    82 CDHTVLNELEKNPrGVPEHLIKKIIwqtlqavnfchkhncihRDVKPENiliTKQGQIklcdfgfariltgpgddytdyV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI---------------ATNG------TPE 442
Cdd:cd07847   162 ATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIrktlgdliprhqqifSTNQffkglsIPE 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 443 LQNPEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07847   242 PETREPLESKFPnisspalSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
269-477 2.61e-20

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: 90.16  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTD-VVTETCMDEGQ--------IAAV--C-------REITPE---------------------QSKRS----- 381
Cdd:cd14663    81 LVTGGELFSkIAKNGRLKEDKarkyfqqlIDAVdyChsrgvfhRDLKPEnllldedgnlkisdfglsalsEQFRQdgllh 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDFLNRC 460
Cdd:cd14663   161 TTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDEN-LMALYRKIMKGEFEY--PRWFSPGAKSLIKRI 237
                         250
                  ....*....|....*..
gi 1774959464 461 LEMDVEKRGSAKELLQH 477
Cdd:cd14663   238 LDPNPSTRITVEQIMAS 254
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
276-476 3.08e-20

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: 90.47  E-value: 3.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGD----ELWVVMEYlAGG 350
Cdd:cd13985     8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRlCGHPNIVQYYDSAILSSegrkEVLLLMEY-CPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDVVTETC---MDEGQIA----AVC---------------REITPE---------------------------QSKRS 381
Cdd:cd13985    87 SLVDILEKSPpspLSEEEVLrifyQICqavghlhsqsppiihRDIKIEnilfsntgrfklcdfgsattehyplerAEEVN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 T------MVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALyliatNGTPELQNPEKLSAI 452
Cdd:cd13985   167 IieeeiqKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIV-----AGKYSIPEQPRYSPE 241
                         250       260
                  ....*....|....*....|....
gi 1774959464 453 FRDFLNRCLEMDVEKRGSAKELLQ 476
Cdd:cd13985   242 LHDLIRHMLTPDPAERPDIFQVIN 265
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
267-480 3.08e-20

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: 90.13  E-value: 3.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlqqqpKKEL------IINEILVMRENKNPNIVNYLDSYLVGDEL 340
Cdd:cd14078     2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMD-----KKALgddlprVKTEIEALKNLSHQHICRLYHVIETDNKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLTD-VVTETCMDEGQ--------IAAVC---------REITPE-------------------------Q 377
Cdd:cd14078    77 FMVLEYCPGGELFDyIVAKDRLSEDEarvffrqiVSAVAyvhsqgyahRDLKPEnllldedqnlklidfglcakpkggmD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGtpELQNPEKLSAIFRDF 456
Cdd:cd14078   157 HHLETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDN-VMALYRKIQSG--KYEEPEWLSPSSKLL 233
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14078   234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
268-481 4.09e-20

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: 90.56  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHqkLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSL-TDVVTETCMDEG-------QI----------AAVCREITPE---------------------------QSKR 380
Cdd:cd14086    81 LVTGGELfEDIVAREFYSEAdashciqQIlesvnhchqnGIVHRDLKPEnlllaskskgaavkladfglaievqgdQQAW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNPE--KLSAIFRDFLN 458
Cdd:cd14086   161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHR-LYAQIKAGAYDYPSPEwdTVTPEAKDLIN 239
                         250       260
                  ....*....|....*....|...
gi 1774959464 459 RCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14086   240 QMLTVNPAKRITAAEALKHPWIC 262
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
269-480 4.36e-20

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: 90.11  E-value: 4.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--------KELIINEILVMRE-NKNPNIVNYLDSYLVGDE 339
Cdd:cd14093     4 KYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSseneaeelREATRREIEILRQvSGHPNIIELHDVFESPTF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTETC-MDEGQ--------IAAVC---------REITPEQ-----------------------S 378
Cdd:cd14093    84 IFLVFELCRKGELFDYLTEVVtLSEKKtrrimrqlFEAVEflhslnivhRDLKPENillddnlnvkisdfgfatrldegE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 KRSTMVGTPYWMAPEVVTRK------AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPE--KLS 450
Cdd:cd14093   164 KLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI-MEGKYEFGSPEwdDIS 242
                         250       260       270
                  ....*....|....*....|....*....|
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14093   243 DTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
276-480 4.46e-20

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: 89.70  E-value: 4.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14069     9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTETC-MDEGQ--------IAAVC---------REITPE--------QSKRS------------------TMVGTPYW 389
Cdd:cd14069    89 DKIEPDVgMPEDVaqfyfqqlMAGLKylhscgithRDIKPEnllldendNLKISdfglatvfrykgkerllnKMCGTLPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP-EKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd14069   169 VAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTYLTPwKKIDTAALSLLRKILTENPNK 248
                         250
                  ....*....|...
gi 1774959464 468 RGSAKELLQHQFL 480
Cdd:cd14069   249 RITIEDIKKHPWY 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
270-480 4.54e-20

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 89.57  E-value: 4.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTET--CMDEGQIAAVCRE-----------------ITPE----QSKRSTMV---------------------G 385
Cdd:cd14114    84 GELFERIAAEhyKMSEAEVINYMRQvceglchmhennivhldIKPEnimcTTKRSNEVklidfglathldpkesvkvttG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd14114   164 TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVkSCDWNFDDSAFSGISEEAKDFIRKLLLAD 243
                         250
                  ....*....|....*.
gi 1774959464 465 VEKRGSAKELLQHQFL 480
Cdd:cd14114   244 PNKRMTIHQALEHPWL 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
270-488 4.89e-20

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: 90.39  E-value: 4.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQM-NLQQQPKKELiinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIdKSKRDPSEEI---EIL-LRYGQHPNIITLRDVYDDGNSVYLVTELLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTD-VVTETCMDEGQIAAVCREIT-------------------------PEQSKRST----------------MVGT 386
Cdd:cd14091    78 GGELLDrILRQKFFSEREASAVMKTLTktveylhsqgvvhrdlkpsnilyadESGDPESLricdfgfakqlraengLLMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 P-Y---WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN---ENPLRALYLIaTNGTPELQNP--EKLSAIFRDFL 457
Cdd:cd14091   158 PcYtanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARI-GSGKIDLSGGnwDHVSDSAKDLV 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFLKIAKPLSS 488
Cdd:cd14091   237 RKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQ 267
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
274-477 9.78e-20

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: 88.71  E-value: 9.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVY----TAMDVATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:pfam07714   5 EKLGEGAFGEVYkgtlKGEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTET----CMDE-----GQIAA----------------------------------VCREITPEQSKRSTMVG 385
Cdd:pfam07714  85 GGDLLDFLRKHkrklTLKDllsmaLQIAKgmeylesknfvhrdlaarnclvsenlvvkisdfgLSRDIYDDDYYRKRGGG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 -TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGtpELQNPEKLSAIFRDFLNRCLE 462
Cdd:pfam07714 165 kLPIkWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGY--RLPQPENCPDELYDLMKQCWA 242
                         250
                  ....*....|....*
gi 1774959464 463 MDVEKRGSAKELLQH 477
Cdd:pfam07714 243 YDPEDRPTFSELVED 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
269-480 1.21e-19

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: 88.48  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPvkEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTE---TCMDEGQIAA------------------------------------------VCREITPEQSKRS 381
Cdd:cd08225    81 CDGGDLMKRINRqrgVLFSEDQILSwfvqislglkhihdrkilhrdiksqniflskngmvaklgdfgIARQLNDSMELAY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGTPELQNPEkLSAIFRDFLNRCL 461
Cdd:cd08225   161 TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF-EGNNLHQLVLKICQGYFAPISPN-FSRDLRSLISQLF 238
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd08225   239 KVSPRDRPSITSILKRPFL 257
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
267-480 1.52e-19

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: 88.53  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQ-EVAIKQMNLQQQPKKE-LIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd14202     1 KFEFSRKDLIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQtLLGKEIKILKELKHENIVALYDFQEIANSVYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVV-TETCMDEG-------QIAA----------VCREITPEQ-------SKRS------------------ 381
Cdd:cd14202    81 EYCNGGDLADYLhTMRTLSEDtirlflqQIAGamkmlhskgiIHRDLKPQNillsysgGRKSnpnnirikiadfgfaryl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 -------TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP--LRALYLIATNGTPELqnPEKLSAI 452
Cdd:cd14202   161 qnnmmaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPqdLRLFYEKNKSLSPNI--PRETSSH 238
                         250       260
                  ....*....|....*....|....*...
gi 1774959464 453 FRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14202   239 LRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
276-479 1.92e-19

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: 87.81  E-value: 1.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVA-TGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKsQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTE-TCMDE-------GQIAA----------VCREITPEQ------SKRS--------------------------TM 383
Cdd:cd14120    81 DYLQAkGTLSEdtirvflQQIAAamkalhskgiVHRDLKPQNillshnSGRKpspndirlkiadfgfarflqdgmmaaTL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP--LRALYLIATNGTPELqnPEKLSAIFRDFLNRCL 461
Cdd:cd14120   161 CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPqeLKAFYEKNANLRPNI--PSGTSPALKDLLLGLL 238
                         250
                  ....*....|....*...
gi 1774959464 462 EMDVEKRGSAKELLQHQF 479
Cdd:cd14120   239 KRNPKDRIDFEDFFSHPF 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
276-479 1.97e-19

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: 88.05  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQM------NLQQQpkkELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVkkrhivQTRQQ---EHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTE-------------TCMDEG-------QIaaVCREITPE---------------------QSKRS--TMVGT 386
Cdd:cd05572    78 GELWTILRDrglfdeytarfytACVVLAfeylhsrGI--IYRDLKPEnllldsngyvklvdfgfakklGSGRKtwTFCGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENPLRaLYLIATNGTPELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd05572   156 PEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFggDDEDPMK-IYNIILKGIDKIEFPKYIDKNAKNLIKQLLRRN 234
                         250       260
                  ....*....|....*....|
gi 1774959464 465 VEKR-----GSAKELLQHQF 479
Cdd:cd05572   235 PEERlgylkGGIRDIKKHKW 254
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
274-480 2.23e-19

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: 87.67  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS-- 351
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGElf 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 ---------LTDV-----VTETCmdEG-----QIAAVCREITPE-------------------------QSKRSTMVGTP 387
Cdd:cd14190    90 erivdedyhLTEVdamvfVRQIC--EGiqfmhQMRVLHLDLKPEnilcvnrtghqvkiidfglarrynpREKLKVNFGTP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-YLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVE 466
Cdd:cd14190   168 EFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLnNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERS 247
                         250
                  ....*....|....
gi 1774959464 467 KRGSAKELLQHQFL 480
Cdd:cd14190   248 ARMSATQCLKHPWL 261
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
269-476 2.78e-19

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 87.79  E-value: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQM---NLQQQPKKELIIN----EI-LVMRENKNPNIVNYLDSYLVGDEL 340
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksGPNSKDGNDFQKLpqlrEIdLHRRVSRHPNIITLHDVFETEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLTDVVTETCMDEGQ-----------IAAV--C-------REITPE--------------------QSKR 380
Cdd:cd13993    81 YIVLEYCPNGDLFEAITENRIYVGKteliknvflqlIDAVkhChslgiyhRDIKPEnillsqdegtvklcdfglatTEKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 ST--MVGTPYWMAPEVVT-----RKAYGPK-VDIWSLGIMAIEMIEGEPPYLNENPLRALYL-IATNGTPELQNPEKLSA 451
Cdd:cd13993   161 SMdfGVGSEFYMAPECFDevgrsLKGYPCAaGDIWSLGIILLNLTFGRNPWKIASESDPIFYdYYLNSPNLFDVILPMSD 240
                         250       260
                  ....*....|....*....|....*
gi 1774959464 452 IFRDFLNRCLEMDVEKRGSAKELLQ 476
Cdd:cd13993   241 DFYNLLRQIFTVNPNNRILLPELQL 265
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
270-480 5.00e-19

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: 86.55  E-value: 5.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNrqkIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTD-VVTETCMDEGQ--------IAAV--C-------REITPEQ----SKRS-------------------TMVG 385
Cdd:cd14079    84 VSGGELFDyIVQKGRLSEDEarrffqqiISGVeyChrhmvvhRDLKPENllldSNMNvkiadfglsnimrdgeflkTSCG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMD 464
Cdd:cd14079   164 SPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEH-IPNLFKKIKSGIYTI--PSHLSPGARDLIKRMLVVD 240
                         250
                  ....*....|....*.
gi 1774959464 465 VEKRGSAKELLQHQFL 480
Cdd:cd14079   241 PLKRITIPEIRQHPWF 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
266-481 5.69e-19

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: 87.17  E-value: 5.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlQQQPK---KELIIneilvMRENKNPNIVNYLDSYLVGDE--- 339
Cdd:cd14137     2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV--LQDKRyknRELQI-----MRRLKHPNIVKLKYFFYSSGEkkd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 ---LWVVMEYLAgGSLTDVV-----TETCMDEG-------QIAA---------VC-REITPEQ--SKRSTMV-------- 384
Cdd:cd14137    75 evyLNLVMEYMP-ETLYRVIrhyskNKQTIPIIyvklysyQLFRglaylhslgIChRDIKPQNllVDPETGVlklcdfgs 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 ------GTP--------YWMAPEVVTR-KAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLIA-TNGTPELQ--- 444
Cdd:cd14137   154 akrlvpGEPnvsyicsrYYRAPELIFGaTDYTTAIDIWSAGcVLA-ELLLGQPLFPGESSVDQLVEIIkVLGTPTREqik 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464 445 --NPEK------------LSAIFR--------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14137   233 amNPNYtefkfpqikphpWEKVFPkrtppdaiDLLSKILVYNPSKRLTALEALAHPFFD 291
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
270-468 7.21e-19

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: 86.69  E-value: 7.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLkqvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVV--------TETCMDEGQIAAVC----------REITPE---------------------QSKRSTMVGTP 387
Cdd:cd14209    83 VPGGEMFSHLrrigrfsePHARFYAAQIVLAFeylhsldliyRDLKPEnllidqqgyikvtdfgfakrvKGRTWTLCGTP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd14209   163 EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQVDLTK 239

                  .
gi 1774959464 468 R 468
Cdd:cd14209   240 R 240
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
268-480 7.71e-19

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: 86.20  E-value: 7.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKcRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTETCMDEGQIAA------------------VCREITPEQ---------SKR----------------STM 383
Cdd:cd14183    86 VKGGDLFDAITSTNKYTERDASgmlynlasaikylhslniVHRDIKPENllvyehqdgSKSlklgdfglatvvdgplYTV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE-NPLRALYLIATNGTPELQNP--EKLSAIFRDFLNRC 460
Cdd:cd14183   166 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSgDDQEVLFDQILMGQVDFPSPywDNVSDSAKELITMM 245
                         250       260
                  ....*....|....*....|
gi 1774959464 461 LEMDVEKRGSAKELLQHQFL 480
Cdd:cd14183   246 LQVDVDQRYSALQVLEHPWV 265
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
263-480 9.63e-19

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: 86.64  E-value: 9.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 263 VGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLV 336
Cdd:cd14168     5 VEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCI-----PKKALkgkessIENEIAVLRKIKHENIVALEDIYES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 337 GDELWVVMEYLAGGSLTDVVTETCMDEGQIAA------------------VCREITPE---------QSK---------- 379
Cdd:cd14168    80 PNHLYLVMQLVSGGELFDRIVEKGFYTEKDAStlirqvldavyylhrmgiVHRDLKPEnllyfsqdeESKimisdfglsk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 -------RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNP--EKLS 450
Cdd:cd14168   160 megkgdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKADYEFDSPywDDIS 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14168   239 DSAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
274-472 1.37e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 86.80  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SL-----------TDVVTETCMdEGQIA--------AVCREITPEQ----------------SKRS-----TMVGTPYWM 390
Cdd:PTZ00263  104 ELfthlrkagrfpNDVAKFYHA-ELVLAfeylhskdIIYRDLKPENllldnkghvkvtdfgfAKKVpdrtfTLCGTPEYL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKR-G 469
Cdd:PTZ00263  183 APEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG---RLKFPNWFDGRARDLVKGLLQTDHTKRlG 259

                  ...
gi 1774959464 470 SAK 472
Cdd:PTZ00263  260 TLK 262
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
263-481 1.47e-18

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: 85.45  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 263 VGDpkKKYTRFEKIGQGASGTVYTAMD-VATGQEVAIKQMNLQQQPKKELII-NEILVMRENKNPNIVNYLDSYLVGDEL 340
Cdd:cd14201     3 VGD--FEYSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLTDVV-TETCMDEG-------QIAA----------VCREITPEQ------SKR---------------- 380
Cdd:cd14201    81 FLVMEYCNGGDLADYLqAKGTLSEDtirvflqQIAAamrilhskgiIHRDLKPQNillsyaSRKkssvsgirikiadfgf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 ----------STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP--LRALYLIATNGTPELqnPEK 448
Cdd:cd14201   161 arylqsnmmaATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPqdLRMFYEKNKNLQPSI--PRE 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14201   239 TSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
272-487 1.69e-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: 85.89  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 272 RFEKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAg 349
Cdd:cd06618    19 NLGEIGSGTCGQVYKMRHKKTGHVMAVKQMrrSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELMS- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 gsltdvvteTCMDE--------------GQIAA---------------VCREITP-----------------------EQ 377
Cdd:cd06618    98 ---------TCLDKllkriqgpipedilGKMTVsivkalhylkekhgvIHRDVKPsnilldesgnvklcdfgisgrlvDS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMIEGEPPY-LNENPLRALYLIATNGTPELQNPEKLSAIF 453
Cdd:cd06618   169 KAKTRSAGCAAYMAPERIDPPdnpKYDIRADVWSLGISLVELATGQFPYrNCKTEFEVLTKILNEEPPSLPPNEGFSPDF 248
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLS 487
Cdd:cd06618   249 CSFVDLCLTKDHRYRPKYRELLQHPFIRRYETAE 282
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
274-484 2.24e-18

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: 85.17  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEylaggs 351
Cdd:cd06617     7 EELGRGAYGVVDKMRHVPTGTIMAVKRIraTVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICME------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 ltdvVTETCMDE-----------------GQIA-AVCREITPEQSKRS-------------------------------- 381
Cdd:cd06617    81 ----VMDTSLDKfykkvydkgltipedilGKIAvSIVKALEYLHSKLSvihrdvkpsnvlinrngqvklcdfgisgylvd 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGT------PYwMAPEVV----TRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGTPELQNpEKLS 450
Cdd:cd06617   157 SVAKTidagckPY-MAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDSwKTPFQQLKQVVEEPSPQLPA-EKFS 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAK 484
Cdd:cd06617   235 PEFQDFVNKCLKKNYKERPNYPELLQHPFFELHL 268
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
276-481 2.86e-18

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: 84.45  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNvkaeRAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVV---------------TETCM---DEGQIAAVCREITPE-------------------------QSKRstMVGTPY 388
Cdd:cd05611    84 CASLIktlgglpedwakqyiAEVVLgveDLHQRGIIHRDIKPEnllidqtghlkltdfglsrnglekrHNKK--FVGTPD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN--GTPELQNpEKLSAIFRDFLNRCLEMDVE 466
Cdd:cd05611   162 YLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRriNWPEEVK-EFCSPEAVDLINRLLCMDPA 240
                         250
                  ....*....|....*...
gi 1774959464 467 KRGSAK---ELLQHQFLK 481
Cdd:cd05611   241 KRLGANgyqEIKSHPFFK 258
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
274-481 2.96e-18

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: 84.90  E-value: 2.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd06622     7 DELGKGNYGSVYKVLHRPTGVTMAMKEIRLElDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTETC----MDEGQIAAVC------------------REITP----------------------EQSKRSTMVGTPY 388
Cdd:cd06622    87 DKLYAGGVategIPEDVLRRITyavvkglkflkeehniihRDVKPtnvlvngngqvklcdfgvsgnlVASLAKTNIGCQS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVT------RKAYGPKVDIWSLGIMAIEMIEGEPPYLNE---NPLRALYLIATNGTPELqnPEKLSAIFRDFLNR 459
Cdd:cd06622   167 YMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGRYPYPPEtyaNIFAQLSAIVDGDPPTL--PSGYSDDAQDFVAK 244
                         250       260
                  ....*....|....*....|..
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd06622   245 CLNKIPNRRPTYAQLLEHPWLV 266
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
270-480 3.31e-18

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: 85.18  E-value: 3.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDV-ATGQEVAIK--------QMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDEL 340
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVPLrNTGKPVAIKvvrkadlsSDNLKGSSRAN-ILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLTD-VVTETCMDEG-------QIAA----------VCREITPEQ------------------------- 377
Cdd:cd14096    82 YIVLELADGGEIFHqIVRLTYFSEDlsrhvitQVASavkylheigvVHRDIKPENllfepipfipsivklrkadddetkv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 ------------------------------SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 427
Cdd:cd14096   162 degefipgvggggigivkladfglskqvwdSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDES 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774959464 428 pLRALYLIATNGTPELQNP--EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14096   242 -IETLTEKISRGDYTFLSPwwDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
269-480 6.36e-18

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: 83.35  E-value: 6.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIE-TKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTD-VVTETCMDEGQIAAVC-----------------REITPE----------------------QSKRS------T 382
Cdd:cd14087    81 GGELFDrIIAKGSFTERDATRVLqmvldgvkylhglgithRDLKPEnllyyhpgpdskimitdfglasTRKKGpnclmkT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEK-LSAIFRDFLNRCL 461
Cdd:cd14087   161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPsVSNLAKDFIDRLL 240
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd14087   241 TVNPGERLSATQALKHPWI 259
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
270-493 1.24e-17

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: 83.25  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvirLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSL------------------------------------TDVVTETCM--DEGQIAAVCREITPEQSKRS-TMVGTP 387
Cdd:cd05612    83 VPGGELfsylrnsgrfsnstglfyaseivcaleylhskeivyRDLKPENILldKEGHIKLTDFGFAKKLRDRTwTLCGTP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLrALYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd05612   163 EYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPF-GIYEKILAG--KLEFPRHLDLYAKDLIKKLLVVDRTR 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1774959464 468 R-GSAK----ELLQHQFLKI----AKPLSSLTPLI 493
Cdd:cd05612   240 RlGNMKngadDVKNHRWFKSvdwdDVPQRKLKPPI 274
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
276-481 2.91e-17

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: 82.65  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELII---------NEILVMR-ENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVL------KKEVIIedddvectmTEKRVLAlANRHPFLTGLHACFQTEDRLYFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSL----------TDVVT-----ETC-----------------MD------EGQIA----AVCREITPEQSKRSTM 383
Cdd:cd05570    77 YVNGGDLmfhiqrarrfTEERArfyaaEIClalqflhergiiyrdlkLDnvlldaEGHIKiadfGMCKEGIWGGNTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY------------LNENPlraLYliatngtpelqnPEKLSA 451
Cdd:cd05570   157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFegddedelfeaiLNDEV---LY------------PRWLSR 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1774959464 452 IFRDFLNRCLEMDVEKR-----GSAKELLQHQFLK 481
Cdd:cd05570   222 EAVSILKGLLTKDPARRlgcgpKGEADIKAHPFFR 256
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
274-480 3.52e-17

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: 81.85  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVElQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 tDV---VTETCMdeGQIAAVC--------------REITPEQ----------------------SKRSTMVGTPYWMAPE 393
Cdd:cd06619    87 -DVyrkIPEHVL--GRIAVAVvkgltylwslkilhRDVKPSNmlvntrgqvklcdfgvstqlvnSIAKTYVGTNAYMAPE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 394 VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL----NEN---PLRALYLIATNGTPELQNPEkLSAIFRDFLNRCLEMDVE 466
Cdd:cd06619   164 RISGEQYGIHSDVWSLGISFMELALGRFPYPqiqkNQGslmPLQLLQCIVDEDPPVLPVGQ-FSEKFVHFITQCMRKQPK 242
                         250
                  ....*....|....
gi 1774959464 467 KRGSAKELLQHQFL 480
Cdd:cd06619   243 ERPAPENLMDHPFI 256
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
276-480 4.88e-17

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: 81.98  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKIL------RKEVIIakdevahtvTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSL------------------------------------TDVVTETCM--DEGQIA----AVCREITPEQSKRSTMV 384
Cdd:cd05595    77 ANGGELffhlsrervftedrarfygaeivsaleylhsrdvvyRDIKLENLMldKDGHIKitdfGLCKEGITDGATMKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd05595   157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILME---EIRFPRTLSPEAKSLLAGLLKKD 233
                         250       260
                  ....*....|....*....|.
gi 1774959464 465 VEKR-----GSAKELLQHQFL 480
Cdd:cd05595   234 PKQRlgggpSDAKEVMEHRFF 254
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
269-482 5.02e-17

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: 82.19  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL----QQQPKKelIINEILVMRENKNPNIVNYLD-----SYLVGDE 339
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfddLIDAKR--ILREIKILRHLKHENIIGLLDilrppSPEEFND 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYL---------AGGSLTD--------------------------------VVTETCMdegqiAAVC-----REI 373
Cdd:cd07834    79 VYIVTELMetdlhkvikSPQPLTDdhiqyflyqilrglkylhsagvihrdlkpsniLVNSNCD-----LKICdfglaRGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 TPEQSKRsTM---VGTPYWMAPEVV-TRKAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI-ATNGTPELQN-- 445
Cdd:cd07834   154 DPDEDKG-FLteyVVTRWYRAPELLlSSKKYTKAIDIWSVGcIFA-ELLTRKPLFPGRDYIDQLNLIvEVLGTPSEEDlk 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 446 ------------------PEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd07834   232 fissekarnylkslpkkpKKPLSEVFpgaspeaIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
274-476 5.09e-17

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: 81.23  E-value: 5.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd08228     8 KKIGRGQFSEVYRATCLLDRKPVALKKVQifeMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDVVT-----ETCMDEGQI----AAVC-------------REITP------------------------EQSKRSTMV 384
Cdd:cd08228    88 DLSQMIKyfkkqKRLIPERTVwkyfVQLCsavehmhsrrvmhRDIKPanvfitatgvvklgdlglgrffssKTTAAHSLV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE--NPLRALYLIATNGTPELQNpEKLSAIFRDFLNRCLE 462
Cdd:cd08228   168 GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLFSLCQKIEQCDYPPLPT-EHYSEKLRELVSMCIY 246
                         250
                  ....*....|....
gi 1774959464 463 MDVEKRGSAKELLQ 476
Cdd:cd08228   247 PDPDQRPDIGYVHQ 260
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
269-479 5.67e-17

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: 81.31  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd07846     2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKmvKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDV-VTETCMDEG-------QI---AAVC-------REITPE-----QSKRSTM-------------------V 384
Cdd:cd07846    82 VDHTVLDDLeKYPNGLDESrvrkylfQIlrgIDFChshniihRDIKPEnilvsQSGVVKLcdfgfartlaapgevytdyV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI---------------------ATNGTPE 442
Cdd:cd07846   162 ATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIikclgnliprhqelfqknplfAGVRLPE 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 443 LQNPE-------KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07846   242 VKEVEplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
270-500 6.50e-17

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: 81.23  E-value: 6.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEI--EIL-LRYGQHPNIITLKDVYDDGKHVYLVTELMRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTD-VVTETCMDEGQIAAVCREIT-----------------------------PEQSK------------RSTMVGTP 387
Cdd:cd14175    80 GELLDkILRQKFFSEREASSVLHTICktveylhsqgvvhrdlkpsnilyvdesgnPESLRicdfgfakqlraENGLLMTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YW----MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN---ENPLRALYLIATNG-TPELQNPEKLSAIFRDFLNR 459
Cdd:cd14175   160 CYtanfVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsDTPEEILTRIGSGKfTLSGGNWNTVSDAAKDLVSK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFL--KIAKPLSSLT----PLIAAAKEAT 500
Cdd:cd14175   240 MLHVDPHQRLTAKQVLQHPWItqKDKLPQSQLNhqdvQLVKGAMAAT 286
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
274-480 7.57e-17

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 80.39  E-value: 7.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTETCMDEGQIAAV------CR-------------EITPE-------------------------QSKRSTMVGTPYW 389
Cdd:cd14192    90 DRITDESYQLTELDAIlftrqiCEgvhylhqhyilhlDLKPEnilcvnstgnqikiidfglarrykpREKLKVNFGTPEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-YLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd14192   170 LAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMnNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCR 249
                         250
                  ....*....|..
gi 1774959464 469 GSAKELLQHQFL 480
Cdd:cd14192   250 MSATQCLKHEWL 261
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
269-480 7.58e-17

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: 80.12  E-value: 7.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIIN--------------EILVM---RENKNPNIVNYL 331
Cdd:cd14004     1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFI------FKERILVdtwvrdrklgtvplEIHILdtlNKRSHPNIVKLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 332 DSYLVGDELWVVMEYLAGG-SLTDVV-TETCMDE-------GQIAA----------VCREITPE---------------- 376
Cdd:cd14004    75 DFFEDDEFYYLVMEKHGSGmDLFDFIeRKPNMDEkeakyifRQVADavkhlhdqgiVHRDIKDEnvildgngtiklidfg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 ------QSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNenplralylIATNGTPELQNPEKL 449
Cdd:cd14004   155 saayikSGPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYN---------IEEILEADLRIPYAV 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1774959464 450 SAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14004   226 SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
276-476 1.23e-16

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: 79.74  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMdvATGQEVAIKQmnLQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14061     2 IGVGGFGKVYRGI--WRGEEVAVKA--ARQDPDEDISVTLENVRQEARlfwmlrHPNIIALRGVCLQPPNLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMDEG-------QIA---------------------------------------------AVCREITpeQ 377
Cdd:cd14061    78 GALNRVLAGRKIPPHvlvdwaiQIArgmnylhneapvpiihrdlkssnilileaienedlenktlkitdfGLAREWH--K 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgTPELQNPEKLSAIFRDFL 457
Cdd:cd14061   156 TTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVN-KLTLPIPSTCPEPFAQLM 234
                         250
                  ....*....|....*....
gi 1774959464 458 NRCLEMDVEKRGSAKELLQ 476
Cdd:cd14061   235 KDCWQPDPHDRPSFADILK 253
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
269-480 1.39e-16

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: 79.49  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLqkLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTD-VVTETCMDEGQIAAVCREI-----------------------------------------TPeQSKRSTMV 384
Cdd:cd14072    81 ASGGEVFDyLVAHGRMKEKEARAKFRQIvsavqychqkrivhrdlkaenllldadmnikiadfgfsnefTP-GNKLDTFC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSAIFRDF 456
Cdd:cd14072   160 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENL 229
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14072   230 LKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
272-477 1.76e-16

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: 78.97  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 272 RFE---KIGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIIN---------EILVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd14073     2 RYElleTLGKGTYGKVKLAIERATGREVAIKSI------KKDKIEDeqdmvrirrEIEIMSSLNHPHIIRIYEVFENKDK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTET---CMDEG-----QIAA----------VCREITPE---------------------QSKR 380
Cdd:cd14073    76 IVIVMEYASGGELYDYISERrrlPEREArrifrQIVSavhychkngvVHRDLKLEnilldqngnakiadfglsnlySKDK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 --STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGtpELQNPEKLSAIFrDFL 457
Cdd:cd14073   156 llQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQI-SSG--DYREPTQPSDAS-GLI 231
                         250       260
                  ....*....|....*....|
gi 1774959464 458 NRCLEMDVEKRGSAKELLQH 477
Cdd:cd14073   232 RWMLTVNPKRRATIEDIANH 251
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
269-480 3.26e-16

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: 78.31  E-value: 3.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEReeSRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTE---TCMDEGQI----AAVC--------REITPEQSKRS-----------------------------T 382
Cdd:cd08218    81 CDGGDLYKRINAqrgVLFPEDQIldwfVQLClalkhvhdRKILHRDIKSQnifltkdgiiklgdfgiarvlnstvelarT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGT-PELqnPEKLSAIFRDFLNRCL 461
Cdd:cd08218   161 CIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGN-MKNLVLKIIRGSyPPV--PSRYSYDLRSLVSQLF 237
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd08218   238 KRNPRDRPSINSILEKPFI 256
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
276-480 3.31e-16

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: 78.50  E-value: 3.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTV--YTAMDVATGQEVAIKQMN------LQQQPKKELIiNEILVMRENKNPNIVNYLDSYLV-GDELWVVMEY 346
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSGVLYAVKEYRrrddesKRKDYVKRLT-SEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTET---------CM-----------------------------DEGQI------AAVCREITPEQSKRST 382
Cdd:cd13994    80 CPGGDLFTLIEKAdslsleekdCFfkqilrgvaylhshgiahrdlkpenilldEDGVLkltdfgTAEVFGMPAEKESPMS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 --MVGTPYWMAPEVVTRKAYGPK-VDIWSLGIMAIEMIEGEPPY---LNENPLRALY---LIATNGTPELQNPEKLSaIF 453
Cdd:cd13994   160 agLCGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPWrsaKKSDSAYKAYeksGDFTNGPYEPIENLLPS-EC 238
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd13994   239 RRLIYRMLHPDPEKRITIDEALNDPWV 265
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
267-481 3.90e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 79.42  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEK-IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-----KELI---------INEILVMRENKNPNIVNYL 331
Cdd:PTZ00024    7 SERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNdvtkdRQLVgmcgihfttLRELKIMNEIKHENIMGLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 332 DSYLVGDELWVVMEYLAgGSLTDVV------TET---CM-----------------------------DEG--QIA---- 367
Cdd:PTZ00024   87 DVYVEGDFINLVMDIMA-SDLKKVVdrkirlTESqvkCIllqilnglnvlhkwyfmhrdlspanifinSKGicKIAdfgl 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 368 ---AVCREITPEQSKRSTM---------VGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYL 434
Cdd:PTZ00024  166 arrYGYPPYSDTLSKDETMqrreemtskVVTLWYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGR 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 435 I-ATNGTPELQN-----------------PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:PTZ00024  246 IfELLGTPNEDNwpqakklplyteftprkPKDLKTIFPnasddaiDLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
270-481 4.19e-16

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: 78.71  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKL--KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMDEGQIAAVC------------------REITPE--------------------------QSKRSTMVG 385
Cdd:cd14085    83 GELFDRIVEKGYYSERDAADAvkqileavaylhengivhRDLKPEnllyatpapdaplkiadfglskivdqQVTMKTVCG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP--EKLSAIFRDFLNRCLEM 463
Cdd:cd14085   163 TPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCDYDFVSPwwDDVSLNAKDLVKKLIVL 242
                         250
                  ....*....|....*...
gi 1774959464 464 DVEKRGSAKELLQHQFLK 481
Cdd:cd14085   243 DPKKRLTTQQALQHPWVT 260
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
274-482 5.11e-16

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: 78.56  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEyLAGGS 351
Cdd:cd06616    12 GEIGRGAFGTVNKMLHKPSGTIMAVKRIrsTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICME-LMDIS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDV------VTETCMDE---GQIAaVC----------------REITP----------------------EQSKRSTM- 383
Cdd:cd06616    91 LDKFykyvyeVLDSVIPEeilGKIA-VAtvkalnylkeelkiihRDVKPsnilldrngniklcdfgisgqlVDSIAKTRd 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGT-PYwMAPEVVT----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPL-RALYLIATNGTPELQNPEKL--SAIFRD 455
Cdd:cd06616   170 AGCrPY-MAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVfDQLTQVVKGDPPILSNSEERefSPSFVN 248
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 456 FLNRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd06616   249 FVNLCLIKDESKRPKYKELLKHPFIKM 275
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
276-480 6.17e-16

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: 77.47  E-value: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASG--TVYTAMDvaTGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd08221     8 LGRGAFGeaVLYRKTE--DNSLVVWKEVNLSRLSEKERrdALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTETC---MDEGQ--------IAAVC---------REI------------------------TPEQSKRSTMVGTP 387
Cdd:cd08221    86 LHDKIAQQKnqlFPEEVvlwylyqiVSAVShihkagilhRDIktlnifltkadlvklgdfgiskvlDSESSMAESIVGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPEKLSAIfRDFLNRCLEMDVEK 467
Cdd:cd08221   166 YYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKI-VQGEYEDIDEQYSEEI-IQLVHDCLHQDPED 243
                         250
                  ....*....|...
gi 1774959464 468 RGSAKELLQHQFL 480
Cdd:cd08221   244 RPTAEELLERPLL 256
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
284-480 7.62e-16

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 77.37  E-value: 7.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 284 VYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD-VVTETCM 361
Cdd:cd14088    17 IFRAKDKTTGKLYTCKKFLKRDGRKvRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDwILDQGYY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 362 DEGQIAAVCREITP-----------------------EQSKRSTMV------------------GTPYWMAPEVVTRKAY 400
Cdd:cd14088    97 SERDTSNVIRQVLEavaylhslkivhrnlklenlvyyNRLKNSKIVisdfhlaklenglikepcGTPEYLAPEVVGRQRY 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 401 GPKVDIWSLGIMAIEMIEGEPPYLN-------ENPLRALYLIATNGTPELQNP--EKLSAIFRDFLNRCLEMDVEKRGSA 471
Cdd:cd14088   177 GRPVDCWAIGVIMYILLSGNPPFYDeaeeddyENHDKNLFRKILAGDYEFDSPywDDISQAAKDLVTRLMEVEQDQRITA 256

                  ....*....
gi 1774959464 472 KELLQHQFL 480
Cdd:cd14088   257 EEAISHEWI 265
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
266-481 7.93e-16

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: 77.97  E-value: 7.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL---QQQP--KKELIINEILVMRENKNPNIVNYLDSYLVGDEL 340
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVakfTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLT-DVVTETcmDEGQI---AAVC--------------------REITPE-------------------- 376
Cdd:cd14094    81 YMVFEFMDGADLCfEIVKRA--DAGFVyseAVAShymrqilealrychdnniihRDVKPHcvllaskensapvklggfgv 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 -------QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENplRALYLIATNGTPELQNPE-- 447
Cdd:cd14094   159 aiqlgesGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKMNPRQws 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1774959464 448 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14094   237 HISESAKDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
273-479 8.23e-16

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: 77.83  E-value: 8.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FEK---IGQGASGTVYTAMDVATGQEVAIKQMN-----LQQQPKKELIINEILVMRENknPNIVNYLDSYLVGDELWVVM 344
Cdd:cd05609     2 FETiklISNGAYGAVYLVRHRETRQRFAMKKINkqnliLRNQIQQVFVERDILTFAEN--PFVVSMYCSFETKRHLCMVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGG------------------------------------------------------SLTD--------VVTETCMD 362
Cdd:cd05609    80 EYVEGGdcatllknigplpvdmarmyfaetvlaleylhsygivhrdlkpdnllitsmghiKLTDfglskiglMSLTTNLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 363 EGQIAAVCREITPEQskrstMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGtpE 442
Cdd:cd05609   160 EGHIEKDTREFLDKQ-----VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFGQVISD--E 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1774959464 443 LQNPEK---LSAIFRDFLNRCLEMDVEKR---GSAKELLQHQF 479
Cdd:cd05609   232 IEWPEGddaLPDDAQDLITRLLQQNPLERlgtGGAEEVKQHPF 274
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
274-480 8.35e-16

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: 77.26  E-value: 8.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTE-----TCMD---------EG-----QIAAVCREITPE-------------------------QSKRSTMVGTPYW 389
Cdd:cd14193    90 DRIIDenynlTELDtilfikqicEGiqymhQMYILHLDLKPEnilcvsreanqvkiidfglarrykpREKLRVNFGTPEF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-YLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd14193   170 LAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLnNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWR 249
                         250
                  ....*....|..
gi 1774959464 469 GSAKELLQHQFL 480
Cdd:cd14193   250 MSASEALKHPWL 261
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
268-480 8.45e-16

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: 77.26  E-value: 8.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVAT-------GQEVAIKQMNLQQQPKKelIINEI-LVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSR--ILNELeCLERLGGSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTEtcMDEGQIAA-----------------VCREITP---------------------EQSKRS 381
Cdd:cd14019    79 VVAVLPYIEHDDFRDFYRK--MSLTDIRIylrnlfkalkhvhsfgiIHRDVKPgnflynretgkgvlvdfglaqREEDRP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMV----GTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGE-PPYLNENPLRALYLIAT-NGTPELQnpeklsaifr 454
Cdd:cd14019   157 EQRapraGTRGFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATiFGSDEAY---------- 226
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14019   227 DLLDKLLELDPSKRITAEEALKHPFF 252
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
276-477 9.05e-16

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 77.15  E-value: 9.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKelIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT-- 353
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRS--FLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEel 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 -----------------------------------DVVTETCM----DEGQIAAV-----CREI------TPEQSKRSTM 383
Cdd:cd14065    79 lksmdeqlpwsqrvslakdiasgmaylhskniihrDLNSKNCLvreaNRGRNAVVadfglAREMpdektkKPDRKKRLTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI---EGEPPYLNEN-----PLRALYLIATNGTPElqnPEKLSAIfrd 455
Cdd:cd14065   159 VGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIgrvPADPDYLPRTmdfglDVRAFRTLYVPDCPP---SFLPLAI--- 232
                         250       260
                  ....*....|....*....|..
gi 1774959464 456 flnRCLEMDVEKRGSAKELLQH 477
Cdd:cd14065   233 ---RCCQLDPEKRPSFVELEHH 251
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
270-479 9.50e-16

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: 77.52  E-value: 9.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDaEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 G------------GSLTDVVTETCMDE-GQIAAVC-------REITPEQ------------------------SKRSTMV 384
Cdd:cd07836    82 KdlkkymdthgvrGALDPNTVKSFTYQlLKGIAFChenrvlhRDLKPQNllinkrgelkladfglarafgipvNTFSNEV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVT-RKAYGPKVDIWSLG-IMAiEMIEGEPPYL---NENPLRALYLIATNGT----------PELQN---- 445
Cdd:cd07836   162 VTLWYRAPDVLLgSRTYSTSIDIWSVGcIMA-EMITGRPLFPgtnNEDQLLKIFRIMGTPTestwpgisqlPEYKPtfpr 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1774959464 446 --PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07836   241 ypPQDLQQLFPhadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
268-480 1.04e-15

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: 76.89  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd14189     1 RSYCKGRLLGKGGFARCYEMTDLATNKTYAVKvipHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDV------------------------------------------VTETC-MDEGQIAAVCREITPEQSKRs 381
Cdd:cd14189    81 ELCSRKSLAHIwkarhtllepevryylkqiisglkylhlkgilhrdlklgnffINENMeLKVGDFGLAARLEPPEQRKK- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDFLNRCL 461
Cdd:cd14189   160 TICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLD-LKETYRCIKQVKYTL--PASLSLPARHLLAGIL 236
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd14189   237 KRNPGDRLTLDQILEHEFF 255
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
387-479 1.15e-15

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: 76.63  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALyliatngtpelQNPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd14012   172 TYWLPPELAQgSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPV-----------LVSLDLSASLQDFLSKCLSLDP 240
                          90
                  ....*....|....
gi 1774959464 466 EKRGSAKELLQHQF 479
Cdd:cd14012   241 KKRPTALELLPHEF 254
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
276-480 1.17e-15

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: 76.97  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILvmrenKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACF-----RHENIAELYGALLWEETVHLFMEAGEGGSVLEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 VtETC--MDEGQIAAVCR-----------------EITPEQ----SKRSTMV-------------------GTPYWMAPE 393
Cdd:cd13995    87 L-ESCgpMREFEIIWVTKhvlkgldflhskniihhDIKPSNivfmSTKAVLVdfglsvqmtedvyvpkdlrGTEIYMSPE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 394 VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA----LYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRG 469
Cdd:cd13995   166 VILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRS 245
                         250
                  ....*....|.
gi 1774959464 470 SAKELLQHQFL 480
Cdd:cd13995   246 SAAELLKHEAL 256
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
270-480 1.28e-15

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 77.33  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETE--DEGVpstaIREISLLKELNHPNIVRLLDVVHSENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGG--SLTDVVTETCMDEGQIA----------AVC-------REITPEQ---SKRSTM-------------------- 383
Cdd:cd07835    79 FLDLDlkKYMDSSPLTGLDPPLIKsylyqllqgiAFChshrvlhRDLKPQNlliDTEGALkladfglarafgvpvrtyth 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 -VGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQN--------------- 445
Cdd:cd07835   159 eVVTLWYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIfRTLGTPDEDVwpgvtslpdykptfp 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 446 ---PEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07835   239 kwaRQDLSKVVpsldedgLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
276-474 1.33e-15

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: 76.92  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 V-------------------------------------TETCM--------------------DEGQIAAVCREITPEQS 378
Cdd:cd14221    81 IksmdshypwsqrvsfakdiasgmaylhsmniihrdlnSHNCLvrenksvvvadfglarlmvdEKTQPEGLRSLKKPDRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI---EGEPPYLnenPLRALYLIATNGTPELQNPEKLSAIFRD 455
Cdd:cd14221   161 KRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIgrvNADPDYL---PRTMDFGLNVRGFLDRYCPPNCPPSFFP 237
                         250
                  ....*....|....*....
gi 1774959464 456 FLNRCLEMDVEKRGSAKEL 474
Cdd:cd14221   238 IAVLCCDLDPEKRPSFSKL 256
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
268-481 1.40e-15

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: 76.88  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNL---------QQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVG 337
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDItgggsfspeEVQELREATLKEIDILRKvSGHPNIIQLKDTYETN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 DELWVVMEYLAGGSLTDVVTE-TCMDEGQ-----------------IAAVCREITPEQ---------------------- 377
Cdd:cd14182    83 TFFFLVFDLMKKGELFDYLTEkVTLSEKEtrkimrallevicalhkLNIVHRDLKPENilldddmnikltdfgfscqldp 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 -SKRSTMVGTPYWMAPEVV------TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPE--K 448
Cdd:cd14182   163 gEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI-MSGNYQFGSPEwdD 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14182   242 RSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
274-480 2.06e-15

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: 76.59  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14178     9 EDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEI--EIL-LRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 D-VVTETCMDEGQIAAVCREIT-----------------------------PEQSK------------RSTMVGTPYW-- 389
Cdd:cd14178    86 DrILRQKCFSEREASAVLCTITktveylhsqgvvhrdlkpsnilymdesgnPESIRicdfgfakqlraENGLLMTPCYta 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 --MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN---ENPLRALYLIATnGTPELQ--NPEKLSAIFRDFLNRCLE 462
Cdd:cd14178   166 nfVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGS-GKYALSggNWDSISDAAKDIVSKMLH 244
                         250
                  ....*....|....*...
gi 1774959464 463 MDVEKRGSAKELLQHQFL 480
Cdd:cd14178   245 VDPHQRLTAPQVLRHPWI 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
273-481 2.72e-15

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: 76.88  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FE---KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIIN-----EILVmrENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd05599     3 FEplkVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHvraerDILA--EADNPWVVKLYYSFQDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLT------DVVTEtcmDEGQ------IAAV---------CREITPE--------QSKRS-------------- 381
Cdd:cd05599    81 EFLPGGDMMtllmkkDTLTE---EETRfyiaetVLAIesihklgyiHRDIKPDnllldargHIKLSdfglctglkkshla 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 -TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAlYLIATNGTPELQNPE--KLSAIFRDFLN 458
Cdd:cd05599   158 ySTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQET-CRKIMNWRETLVFPPevPISPEAKDLIE 236
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 459 RCLeMDVEKR---GSAKELLQHQFLK 481
Cdd:cd05599   237 RLL-CDAEHRlgaNGVEEIKSHPFFK 261
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
251-480 2.83e-15

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: 77.38  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 251 EEILEKLRSIVSVGDpkkkYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELII---------NEILVMRE 321
Cdd:cd05594    12 EVSLTKPKHKVTMND----FEYLKLLGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakdevahtlTENRVLQN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 322 NKNPNIVNYLDSYLVGDELWVVMEYLAGGSL-------------------------------------TDVVTETCM--D 362
Cdd:cd05594    82 SRHPFLTALKYSFQTHDRLCFVMEYANGGELffhlsrervfsedrarfygaeivsaldylhseknvvyRDLKLENLMldK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 363 EGQIA----AVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN 438
Cdd:cd05594   162 DGHIKitdfGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 439 gtpELQNPEKLSAIFRDFLNRCLEMDVEKR---GS--AKELLQHQFL 480
Cdd:cd05594   242 ---EIRFPRTLSPEAKSLLSGLLKKDPKQRlggGPddAKEIMQHKFF 285
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
270-480 3.20e-15

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: 75.83  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK------KELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsREDIEREVSILKEIQHPNVITLHEVYENKTDVILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTET-CMDEGQIAAVCREI-----------------TPEQ---------------------------S 378
Cdd:cd14194    87 LELVAGGELFDFLAEKeSLTEEEATEFLKQIlngvyylhslqiahfdlKPENimlldrnvpkprikiidfglahkidfgN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFL 457
Cdd:cd14194   167 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVsAVNYEFEDEYFSNTSALAKDFI 246
                         250       260
                  ....*....|....*....|...
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14194   247 RRLLVKDPKKRMTIQDSLQHPWI 269
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
270-480 3.21e-15

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: 75.55  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEY 346
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRErkAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTE---TCMDEGQIA-----------------------------------------AVCREITPEQSKRST 382
Cdd:cd08223    82 CEGGDLYTRLKEqkgVLLEERQVVewfvqiamalqymhernilhrdlktqnifltksniikvgdlGIARVLESSSDMATT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRAL-YLIATNGTPELqnPEKLSAIFRDFLNRCL 461
Cdd:cd08223   162 LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAF-NAKDMNSLvYKILEGKLPPM--PKQYSPELGELIKAML 238
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd08223   239 HQDPEKRPSVKRILRQPYI 257
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
274-480 3.28e-15

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: 75.38  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ----QPKKELIINEILvmreNKNP-----NIVNYLDSYLVGDELWVVM 344
Cdd:cd14133     5 EVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKdyldQSLDEIRLLELL----NKKDkadkyHIVRLKDVFYFKNHLCIVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLaGGSLTDVVTETC---MDEGQIAAVCREIT-----------------PE----------QSK-------------RS 381
Cdd:cd14133    81 ELL-SQNLYEFLKQNKfqyLSLPRIRKIAQQILealvflhslglihcdlkPEnillasysrcQIKiidfgsscfltqrLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-YLIATNGTPelqnPEKL-------SAIF 453
Cdd:cd14133   160 SYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLaRIIGTIGIP----PAHMldqgkadDELF 235
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14133   236 VDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
274-417 3.86e-15

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: 75.41  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNL-QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd13996    12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIRLtEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTE----TCMDEG-------QIAA----------VCREITPE----------------------------------- 376
Cdd:cd13996    92 RDWIDRrnssSKNDRKlalelfkQILKgvsyihskgiVHRDLKPSnifldnddlqvkigdfglatsignqkrelnnlnnn 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 377 ----QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 417
Cdd:cd13996   172 nngnTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
270-480 3.93e-15

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: 75.82  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14177     6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEI--EIL-MRYGQHPNIITLKDVYDDGRYVYLVTELMKG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTD-VVTETCMDEGQIAAV------------CREITPEQSKRSTMVG------------------------------- 385
Cdd:cd14177    83 GELLDrILRQKFFSEREASAVlytitktvdylhCQGVVHRDLKPSNILYmddsanadsiricdfgfakqlrgengllltp 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 --TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL---NENPLRALYLIAtNGTPELQ--NPEKLSAIFRDFLN 458
Cdd:cd14177   163 cyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIG-SGKFSLSggNWDTVSDAAKDLLS 241
                         250       260
                  ....*....|....*....|..
gi 1774959464 459 RCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14177   242 HMLHVDPHQRYTAEQVLKHSWI 263
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
268-480 4.54e-15

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 75.28  E-value: 4.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14097     1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKagSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVV--------TET----CMDEGQIA------AVCREITPE------------------------------- 376
Cdd:cd14097    81 LCEDGELKELLlrkgffseNETrhiiQSLASAVAylhkndIVHRDLKLEnilvkssiidnndklnikvtdfglsvqkygl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 -QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIF 453
Cdd:cd14097   161 gEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEI-RKGDLTFTQSvwQSVSDAA 239
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14097   240 KNVLQQLLKVDPAHRMTASELLDNPWI 266
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
273-481 8.25e-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: 75.48  E-value: 8.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FEKI---GQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd06650     7 FEKIselGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDV------VTETCMDEGQIAAV-------------CREITPEQ----------------------SKRSTMVGTP 387
Cdd:cd06650    87 GGSLDQVlkkagrIPEQILGKVSIAVIkgltylrekhkimHRDVKPSNilvnsrgeiklcdfgvsgqlidSMANSFVGTR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEM----------------------IEGEP---PYLNENPLRALYLIATNGTPE 442
Cdd:cd06650   167 SYMSPERLQGTHYSVQSDIWSMGLSLVEMavgrypipppdakelelmfgcqVEGDAaetPPRPRTPGRPLSSYGMDSRPP 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774959464 443 L-----------QNPEKL-----SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd06650   247 MaifelldyivnEPPPKLpsgvfSLEFQDFVNKCLIKNPAERADLKQLMVHAFIK 301
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
272-480 9.30e-15

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 74.89  E-value: 9.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 272 RFE---KIGQGASGTVYTAMDVATGQEVAIK----QMNLQQQPKKELiinEIL-VMRENK---NPNIVNYLDSYLVGDEL 340
Cdd:cd14210    14 RYEvlsVLGKGSFGQVVKCLDHKTGQLVAIKiirnKKRFHQQALVEV---KILkHLNDNDpddKHNIVRYKDSFIFRGHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEyLAGGSLTDVVTET---CMDEGQIAAVCREI-----------------TPE-----QSKRST----------MVG 385
Cdd:cd14210    91 CIVFE-LLSINLYELLKSNnfqGLSLSLIRKFAKQIlqalqflhklniihcdlKPEnillkQPSKSSikvidfgsscFEG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TP--------YWMAPEVVTRKAYGPKVDIWSLGIMAIEM-------------------IE--GEPP-YLNENPLRALYLI 435
Cdd:cd14210   170 EKvytyiqsrFYRAPEVILGLPYDTAIDMWSLGCILAELytgyplfpgeneeeqlaciMEvlGVPPkSLIDKASRRKKFF 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 436 ATNGTPELQNPEK----------LSAI-------FRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14210   250 DSNGKPRPTTNSKgkkrrpgsksLAQVlkcddpsFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
276-480 1.14e-14

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: 75.12  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakdevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSL------------------------------------TDVVTETCM--DEGQIA----AVCREITPEQSKRSTMV 384
Cdd:cd05593    97 VNGGELffhlsrervfsedrtrfygaeivsaldylhsgkivyRDLKLENLMldKDGHIKitdfGLCKEGITDAATMKTFC 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd05593   177 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSADAKSLLSGLLIKD 253
                         250       260
                  ....*....|....*....|.
gi 1774959464 465 VEKR-----GSAKELLQHQFL 480
Cdd:cd05593   254 PNKRlgggpDDAKEIMRHSFF 274
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
276-481 1.19e-14

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: 75.04  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFfeeERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVT--ETCMDEG-----------------QIAAVCREITPE----------------------QSK--RSTM-VGTPY 388
Cdd:cd05601    89 LSLLSryDDIFEESmarfylaelvlaihslhSMGYVHRDIKPEnilidrtghikladfgsaaklsSDKtvTSKMpVGTPD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVT------RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNPE--KLSAIFRDFLNRC 460
Cdd:cd05601   169 YIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDT-VIKTYSNIMNFKKFLKFPEdpKVSESAVDLIKGL 247
                         250       260
                  ....*....|....*....|.
gi 1774959464 461 LEmDVEKRGSAKELLQHQFLK 481
Cdd:cd05601   248 LT-DAKERLGYEGLCCHPFFS 267
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
274-480 1.36e-14

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: 73.92  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQ--QPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRrgQDCRNEILHEIAVLELCKdCPRVVNLHEVYETRSELILILELAAGG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDV-VTETCMDEGQIAAVCREI---------------------------TP----------------EQSKRSTMVGT 386
Cdd:cd14106    94 ELQTLlDEEECLTEADVRRLMRQIlegvqylhernivhldlkpqnilltseFPlgdiklcdfgisrvigEGEEIREILGT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGtpELQNPEKL------SAIfrDFLNRC 460
Cdd:cd14106   174 PDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDK-QETFLNISQC--NLDFPEELfkdvspLAI--DFIKRL 248
                         250       260
                  ....*....|....*....|
gi 1774959464 461 LEMDVEKRGSAKELLQHQFL 480
Cdd:cd14106   249 LVKDPEKRLTAKECLEHPWL 268
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
276-424 1.59e-14

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: 73.70  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 V-------------------------------------TETC------------------MDEGQIAAVC--------RE 372
Cdd:cd14154    81 LkdmarplpwaqrvrfakdiasgmaylhsmniihrdlnSHNClvredktvvvadfglarlIVEERLPSGNmspsetlrHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1774959464 373 ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI---EGEPPYL 424
Cdd:cd14154   161 KSPDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIgrvEADPDYL 215
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
75-110 2.21e-14

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 66.85  E-value: 2.21e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1774959464   75 ISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTS 110
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFTGLPTEWKSLLKTS 36
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
276-480 2.58e-14

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: 72.97  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIV---NYLDS----YLV--------- 336
Cdd:cd14186     9 LGKGSFACVYRARSLHTGLEVAIKMIDkkaMQKAGMVQRVRNEVEIHCQLKHPSILelyNYFEDsnyvYLVlemchngem 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 337 ------------GDELWVVMEYLAGG--------------SLTDVVTETCMDEgQIA--AVCREITPEQSKRSTMVGTPY 388
Cdd:cd14186    89 srylknrkkpftEDEARHFMHQIVTGmlylhshgilhrdlTLSNLLLTRNMNI-KIAdfGLATQLKMPHEKHFTMCGTPN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd14186   168 YISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLA---DYEMPAFLSREAQDLIHQLLRKNPADR 244
                         250
                  ....*....|..
gi 1774959464 469 GSAKELLQHQFL 480
Cdd:cd14186   245 LSLSSVLDHPFM 256
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
276-428 2.73e-14

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: 73.25  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDsylVGDELWVV--------- 343
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSdknRERWCLEVQIMKKLNHPNVVSARD---VPPELEKLspndlplla 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVT--ETC--MDEGQIAAVCREIT-----------------PE-------------------------- 376
Cdd:cd13989    78 MEYCSGGDLRKVLNqpENCcgLKESEVRTLLSDISsaisylhenriihrdlkPEnivlqqgggrviyklidlgyakeldq 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 377 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL-NENP 428
Cdd:cd13989   158 GSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLpNWQP 210
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
270-480 3.29e-14

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: 72.73  E-value: 3.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14191     4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMD--EGQIAAVCREIT-----------------PEQ------------------SKR-------STMVG 385
Cdd:cd14191    84 GELFERIIDEDFEltERECIKYMRQISegveyihkqgivhldlkPENimcvnktgtkiklidfglARRlenagslKVLFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIFRDFLNRCLEM 463
Cdd:cd14191   164 TPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNLLKK 242
                         250
                  ....*....|....*..
gi 1774959464 464 DVEKRGSAKELLQHQFL 480
Cdd:cd14191   243 DMKARLTCTQCLQHPWL 259
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
276-481 3.54e-14

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: 73.59  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQqqpKKELIIN----------EILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05584     4 LGKGGYGKVFQVRKTTGSDKGKIFAMKVL---KKASIVRnqkdtahtkaERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSL------------------------------------TDVVTETCM--DEGQIA----AVCREITPEQSKRSTM 383
Cdd:cd05584    81 YLSGGELfmhleregifmedtacfylaeitlalghlhslgiiyRDLKPENILldAQGHVKltdfGLCKESIHDGTVTHTF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd05584   161 CGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKG---KLNLPPYLTNEARDLLKKLLKR 237
                         250       260
                  ....*....|....*....|...
gi 1774959464 464 DVEKR-----GSAKELLQHQFLK 481
Cdd:cd05584   238 NVSSRlgsgpGDAEEIKAHPFFR 260
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
275-478 3.68e-14

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 72.27  E-value: 3.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQ------PKKELIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14005     7 LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVtewamiNGPVPVPLEIALLLkasKPGVPGVIRLLDWYERPDGFLLIME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGG-SLTDVVTET-CMDEGQ--------IAAV--C-------REITPE-----------------------QSKRSTM 383
Cdd:cd14005    87 RPEPCqDLFDFITERgALSENLariifrqvVEAVrhChqrgvlhRDIKDEnllinlrtgevklidfgcgallkDSVYTDF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPK-VDIWSLGIMAIEMIEGEPPYLNEnplraLYLIatngTPELQNPEKLSAIFRDFLNRCLE 462
Cdd:cd14005   167 DGTRVYSPPEWIRHGRYHGRpATVWSLGILLYDMLCGDIPFEND-----EQIL----RGNVLFRPRLSKECCDLISRCLQ 237
                         250
                  ....*....|....*.
gi 1774959464 463 MDVEKRGSAKELLQHQ 478
Cdd:cd14005   238 FDPSKRPSLEQILSHP 253
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
276-477 4.17e-14

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 71.92  E-value: 4.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD- 354
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMK-KKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDy 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 -VVTETCMDEG------------QIAAVCR----EITPEQSKRST--------------------------MVGTPYWMA 391
Cdd:cd14115    80 lMNHDELMEEKvafyirdimealQYLHNCRvahlDIKPENLLIDLripvprvklidledavqisghrhvhhLLGNPEFAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 392 PEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRCLEMDVEK 467
Cdd:cd14115   160 PEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDFSFPDEyfgdVSQAARDFINVILQEDPRR 236
                         250
                  ....*....|
gi 1774959464 468 RGSAKELLQH 477
Cdd:cd14115   237 RPTAATCLQH 246
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
276-483 4.64e-14

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: 71.76  E-value: 4.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYtaMDVATGQEVAIKQMNLQQQpkkeliiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd14059     1 LGSGAQGAVF--LGKFRGEEVAVKKVRDEKE-------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 ------VTETCMDE--GQIA----------------------------------AVCREITpEQSKRSTMVGTPYWMAPE 393
Cdd:cd14059    72 lragreITPSLLVDwsKQIAsgmnylhlhkiihrdlkspnvlvtyndvlkisdfGTSKELS-EKSTKMSFAGTVAWMAPE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 394 VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKE 473
Cdd:cd14059   151 VIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSL-QLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQ 229
                         250
                  ....*....|
gi 1774959464 474 LLQHqfLKIA 483
Cdd:cd14059   230 ILMH--LDIA 237
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
270-479 4.70e-14

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: 72.60  E-value: 4.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQqpKKE----LIINEILVMRENKNPNIVNYLD------SYLVGDE 339
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEgfpiTAIREIKLLQKLDHPNVVRLKEivtskgSAKYKGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEY----LAGgsLTDVvTETCMDEGQIAAV-----------------------------------------CREIT 374
Cdd:cd07840    79 IYMVFEYmdhdLTG--LLDN-PEVKFTESQIKCYmkqlleglqylhsngilhrdikgsnilinndgvlkladfglARPYT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 PEQSKRST-MVGTPYWMAPEVV---TRkaYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA-TNGTPELQN-P-- 446
Cdd:cd07840   156 KENNADYTnRVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFeLCGSPTEENwPgv 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 447 ------------------------EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07840   234 sdlpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
277-475 5.40e-14

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: 71.53  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 277 GQGASGTVYTAMDVATGQEVAIKQMNlqqQPKKELIINEILVMRenknpNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV 356
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLL---KIEKEAEILSVLSHR-----NIIQFYGAILEAPNYGIVTEYASYGSLFDYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 357 T-----ETCMD------------------EGQIAAVCREITPE----------------------QSKRSTMVGTPYWMA 391
Cdd:cd14060    74 NsneseEMDMDqimtwatdiakgmhylhmEAPVKVIHRDLKSRnvviaadgvlkicdfgasrfhsHTTHMSLVGTFPWMA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 392 PEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpELQNPEKLSAIFRDFLNRCLEMDVEKRGSA 471
Cdd:cd14060   154 PEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNE-RPTIPSSCPRSFAELMRRCWEADVKERPSF 232

                  ....
gi 1774959464 472 KELL 475
Cdd:cd14060   233 KQII 236
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
276-476 9.42e-14

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 70.93  E-value: 9.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAmdVATGQEVAIKQMNLQQQpkKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd14058     1 VGRGSFGVVCKA--RWRNQIVAVKIIESESE--KKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 --------------VTETCMDEGQIAA----------VCREITPE----------------------QSKRSTMVGTPYW 389
Cdd:cd14058    77 lhgkepkpiytaahAMSWALQCAKGVAylhsmkpkalIHRDLKPPnllltnggtvlkicdfgtacdiSTHMTNNKGSAAW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGT--PELQN-PEKLsaifRDFLNRCLEMDV 465
Cdd:cd14058   157 MAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHiGGPAFRIMWAVHNGErpPLIKNcPKPI----ESLMTRCWSKDP 232
                         250
                  ....*....|.
gi 1774959464 466 EKRGSAKELLQ 476
Cdd:cd14058   233 EKRPSMKEIVK 243
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
276-479 1.15e-13

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: 72.00  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKIL------KKEVIIakdevahtlTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSL------------------------------------TDVVTETCM--DEGQIA----AVCREITPEQSKRSTMV 384
Cdd:cd05571    77 VNGGELffhlsrervfsedrtrfygaeivlalgylhsqgivyRDLKLENLLldKDGHIKitdfGLCKEEISYGATTKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd05571   157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILME---EVRFPSTLSPEAKSLLAGLLKKD 233
                         250       260
                  ....*....|....*....|
gi 1774959464 465 VEKR--GS---AKELLQHQF 479
Cdd:cd05571   234 PKKRlgGGprdAKEIMEHPF 253
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
268-481 1.42e-13

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: 71.94  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlqqQPKKELI-----INEILVMRENKNPNIVNYLDSYLVGDEL-- 340
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLS---RPFQSAIhakrtYRELRLLKHMKHENVIGLLDVFTPASSLed 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 ----WVVMEyLAGGSLTDVVTETCMDEGQI----------------AAVC-REITPE---------------------QS 378
Cdd:cd07851    92 fqdvYLVTH-LMGADLNNIVKCQKLSDDHIqflvyqilrglkyihsAGIIhRDLKPSnlavnedcelkildfglarhtDD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 KRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSA---- 451
Cdd:cd07851   171 EMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGcIMA-ELLTGKTLFPGSDHIDQLKRImNLVGTPDEELLKKISSesar 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 452 ----------------IFR-------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07851   250 nyiqslpqmpkkdfkeVFSganplaiDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
274-475 1.43e-13

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: 70.88  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAmdVATGQEVAIKQMNLQQQPKKEL--IINEILVMREnKNPNIVNYL---DSYLVGDELWVVMEYLA 348
Cdd:cd13979     9 EPLGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRqsFWAELNAARL-RHENIVRVLaaeTGTDFASLGLIIMEYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTETC--------------------------------------MDEGQIAAVC--------REITPEQSKRST 382
Cdd:cd13979    86 NGTLQQLIYEGSeplplahrilisldiaralrfchshgivhldvkpanilISEQGVCKLCdfgcsvklGEGNEVGTPRSH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEK--LSAIFRDFLNRC 460
Cdd:cd13979   166 IGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDseFGQRLRSLISRC 245
                         250
                  ....*....|....*
gi 1774959464 461 LEMDVEKRGSAKELL 475
Cdd:cd13979   246 WSAQPAERPNADESL 260
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
273-483 1.78e-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: 71.31  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FEKI---GQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd06615     3 FEKLgelGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAiRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTETC-MDE---GQIA-AVCREITPEQSKRSTM------------------------------------VGTP 387
Cdd:cd06615    83 GGSLDQVLKKAGrIPEnilGKISiAVLRGLTYLREKHKIMhrdvkpsnilvnsrgeiklcdfgvsgqlidsmansfVGTR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEG-------------------EPPYLNENPLRALYLIATNGTP-----EL 443
Cdd:cd06615   163 SYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrypipppdakeleamfgrpVSEGEAKESHRPVSGHPPDSPRpmaifEL 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1774959464 444 ------QNPEKL-----SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIA 483
Cdd:cd06615   243 ldyivnEPPPKLpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRA 293
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
274-477 1.80e-13

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: 70.52  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG-- 349
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQesQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGdm 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 ---------GSLTDVVTETCMDEGQIA---------AVC-------------------------REITPEQSKRSTMVGT 386
Cdd:cd14082    89 lemilssekGRLPERITKFLVTQILVAlrylhskniVHCdlkpenvllasaepfpqvklcdfgfARIIGEKSFRRSVVGT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY-----LNENPLRALYLIATNGTPELQnpekLSAIfrDFLNRCL 461
Cdd:cd14082   169 PAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnededINDQIQNAAFMYPPNPWKEIS----PDAI--DLINNLL 242
                         250
                  ....*....|....*.
gi 1774959464 462 EMDVEKRGSAKELLQH 477
Cdd:cd14082   243 QVKMRKRYSVDKSLSH 258
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
268-480 2.57e-13

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: 70.04  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd14188     1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKiipHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVV-TETCMDEGQIAAVCREIT-----------------------------------------PEQSKRST 382
Cdd:cd14188    81 EYCSRRSMAHILkARKVLTEPEVRYYLRQIVsglkylheqeilhrdlklgnffinenmelkvgdfglaarlePLEHRRRT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLE 462
Cdd:cd14188   161 ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTN-LKETYRCIREARYSL--PSSLLAPAKHLIASMLS 237
                         250
                  ....*....|....*...
gi 1774959464 463 MDVEKRGSAKELLQHQFL 480
Cdd:cd14188   238 KNPEDRPSLDEIIRHDFF 255
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
270-479 2.66e-13

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: 70.23  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 ------------AGGSLTDVVTETCMDEGQIAAVC-------REITPEQ----------------------SKRSTM--V 384
Cdd:cd07860    82 hqdlkkfmdasaLTGIPLPLIKSYLFQLLQGLAFChshrvlhRDLKPQNllintegaikladfglarafgvPVRTYTheV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTP---------ELQN-------- 445
Cdd:cd07860   162 VTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIfRTLGTPdevvwpgvtSMPDykpsfpkw 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 446 -PEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07860   242 aRQDFSKVVppldedgRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
276-479 2.73e-13

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: 70.81  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK---ELIINEILVMREN-KNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRnevKHIMAERNVLLKNvKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 L------------------------------------TDVVTETCM--DEGQIA----AVCREITPEQSKRSTMVGTPYW 389
Cdd:cd05575    83 LffhlqrerhfpeprarfyaaeiasalgylhslniiyRDLKPENILldSQGHVVltdfGLCKEGIEPSDTTSTFCGTPEY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENplralyliatngTPE---------LQNPEKLSAIFRDFLNRC 460
Cdd:cd05575   163 LAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRD------------TAEmydnilhkpLRLRTNVSPSARDLLEGL 230
                         250       260
                  ....*....|....*....|...
gi 1774959464 461 LEMDVEKR-GSA---KELLQHQF 479
Cdd:cd05575   231 LQKDRTKRlGSGndfLEIKNHSF 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
275-480 3.24e-13

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: 69.85  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNlQQQPKKELIINEIL-----VMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14070     9 KLGEGSFAKVREGLHAVTGEKVAIKVID-KKKAKKDSYVTKNLrregrIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETC-MDEGQ--------IAAV-----------------------------------CREITPEQSKRSTMVG 385
Cdd:cd14070    88 GNLMHRIYDKKrLEEREarryirqlVSAVehlhragvvhrdlkienllldendniklidfglsnCAGILGYSDPFSTQCG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN-PLRALYLIATNGtpELQN-PEKLSAIFRDFLNRCLEM 463
Cdd:cd14070   168 SPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQKMVDK--EMNPlPTDLSPGAISFLRSLLEP 245
                         250
                  ....*....|....*..
gi 1774959464 464 DVEKRGSAKELLQHQFL 480
Cdd:cd14070   246 DPLKRPNIKQALANRWL 262
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
276-425 4.24e-13

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: 69.95  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD-----SYLVGDELWVVMEYLAG 349
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKnKDRWCHEIQIMKKLNHPNVVKACDvpeemNFLVNDVPLLAMEYCSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVT--ETC--MDEGQIAA-----------------VCREITPEQ--------------------------SKRST 382
Cdd:cd14039    81 GDLRKLLNkpENCcgLKESQVLSllsdigsgiqylhenkiIHRDLKPENivlqeingkivhkiidlgyakdldqgSLCTS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN 425
Cdd:cd14039   161 FVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLH 203
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
375-480 4.25e-13

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: 70.29  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFR 454
Cdd:cd05610   209 AARVEGERILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVNAQ 288
                          90       100
                  ....*....|....*....|....*.
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd05610   289 NAIEILLTMDPTKRAGLKELKQHPLF 314
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
270-479 5.52e-13

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: 69.56  E-value: 5.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQmnLQQQPKKELI----INEILVMRENKNPNIVNyLDSYLVG---DELWV 342
Cdd:cd07843     7 YEKLNRIEEGTYGVVYRARDKKTGEIVALKK--LKMEKEKEGFpitsLREINILLKLQHPNIVT-VKEVVVGsnlDKIYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEYLAGG--SLTDVVTET-------CM-----------------------------DEGQIAaVC-----REITPEQSK 379
Cdd:cd07843    84 VMEYVEHDlkSLMETMKQPflqsevkCLmlqllsgvahlhdnwilhrdlktsnlllnNRGILK-ICdfglaREYGSPLKP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 RSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI--------------------AT 437
Cdd:cd07843   163 YTQLVVTLWYRAPELLLgAKEYSTAIDMWSVGcIFA-ELLTKKPLFPGKSEIDQLNKIfkllgtptekiwpgfselpgAK 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1774959464 438 NGTPELQNPEKLSAIFR---------DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07843   242 KKTFTKYPYNQLRKKFPalslsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
276-481 6.29e-13

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: 69.09  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 --------TDVVTETCMD--EGQIAA----------VCREITPE-----------------------QSKRSTMVGTPYW 389
Cdd:cd05577    81 kyhiynvgTRGFSEARAIfyAAEIICglehlhnrfiVYRDLKPEnillddhghvrisdlglavefkgGKKIKGRVGTHGY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRK-AYGPKVDIWSLGIMAIEMIEGEPPY------LNENPLRALYLiatngTPELQNPEKLSAIFRDFLNRCLE 462
Cdd:cd05577   161 MAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrqrkekVDKEELKRRTL-----EMAVEYPDSFSPEARSLCEGLLQ 235
                         250       260
                  ....*....|....*....|....
gi 1774959464 463 MDVEKR-----GSAKELLQHQFLK 481
Cdd:cd05577   236 KDPERRlgcrgGSADEVKEHPFFR 259
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
270-477 8.02e-13

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: 68.67  E-value: 8.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVA---IKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRgvsREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTE--------------------TCMDEGQIA--------------------------AVCREITPEQ 377
Cdd:cd14105    87 LELVAGGELFDFLAEkeslseeeateflkqildgvNYLHTKNIAhfdlkpenimlldknvpipriklidfGLAHKIEDGN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNP--EKLSAIFRD 455
Cdd:cd14105   167 EFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI-TAVNYDFDDEyfSNTSELAKD 244
                         250       260
                  ....*....|....*....|..
gi 1774959464 456 FLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14105   245 FIRQLLVKDPRKRMTIQESLRH 266
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
274-480 9.52e-13

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: 68.21  E-value: 9.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIK---QMNLQQQPKKELIiNEILVMRENKNPNIVNYldsYLVGD---ELWVVMEYL 347
Cdd:cd14074     9 ETLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDDVSKAHLF-QEVRCMKLVQHPNVVRL---YEVIDtqtKLYLILELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVT--ETCMDEG-----------------QIAAVCREITPEQ------------------------SKRSTMV 384
Cdd:cd14074    85 DGGDMYDYIMkhENGLNEDlarkyfrqivsaisychKLHVVHRDLKPENvvffekqglvkltdfgfsnkfqpgEKLETSC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELqnPEKLSAIFRDFLNRCLEM 463
Cdd:cd14074   165 GSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMI-MDCKYTV--PAHVSPECKDLIRRMLIR 241
                         250
                  ....*....|....*..
gi 1774959464 464 DVEKRGSAKELLQHQFL 480
Cdd:cd14074   242 DPKKRASLEEIENHPWL 258
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
270-482 1.16e-12

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: 68.11  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVA---IKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAakfIKKRRLSSSRRgvsREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTET-CMDEGQIAAVCREI-----------------TPEQ---------------------------S 378
Cdd:cd14195    87 LELVSGGELFDFLAEKeSLTEEEATQFLKQIldgvhylhskriahfdlKPENimlldknvpnpriklidfgiahkieagN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFL 457
Cdd:cd14195   167 EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNIsAVNYDFDEEYFSNTSELAKDFI 246
                         250       260
                  ....*....|....*....|....*
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd14195   247 RRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
269-477 1.36e-12

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: 67.87  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIE-RGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTET---CMDEGQ------IAAV--------C-REITPE-------------------------QSKRSTMVG 385
Cdd:cd14662    80 GGELFERICNAgrfSEDEARyffqqlISGVsychsmqiChRDLKLEntlldgspaprlkicdfgyskssvlHSQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGTPELQNPE--KLSAIFRDFLNRCL 461
Cdd:cd14662   160 TPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEDpDDPKNFRKTIQRIMSVQYKIPDyvRVSQDCRHLLSRIF 239
                         250
                  ....*....|....*.
gi 1774959464 462 EMDVEKRGSAKELLQH 477
Cdd:cd14662   240 VANPAKRITIPEIKNH 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
276-480 1.52e-12

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: 67.67  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd14116    13 LGKGKFGNVYLAREKQSKFILALKvlfKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTE-TCMDEGQIA-----------------AVCREITPEQ----------------------SKRSTMVGTPYWMAP 392
Cdd:cd14116    93 YRELQKlSKFDEQRTAtyitelanalsychskrVIHRDIKPENlllgsagelkiadfgwsvhapsSRRTTLCGTLDYLPP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 393 EVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY---LNENPLRALYLIatngtpELQNPEKLSAIFRDFLNRCLEMDVEKRG 469
Cdd:cd14116   173 EMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFeanTYQETYKRISRV------EFTFPDFVTEGARDLISRLLKHNPSQRP 246
                         250
                  ....*....|.
gi 1774959464 470 SAKELLQHQFL 480
Cdd:cd14116   247 MLREVLEHPWI 257
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
276-477 1.64e-12

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: 67.28  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK----KELIINEILVMRENKNPNIVNYLDsYLVGDE---LWVVMEYLA 348
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRipngEANVKREIQILRRLNHRNVIKLVD-VLYNEEkqkLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GG--SLTDVVTETCMDEGQ-----------------IAAVCREITP-------------------EQSKR-------STM 383
Cdd:cd14119    80 GGlqEMLDSAPDKRLPIWQahgyfvqlidgleylhsQGIIHKDIKPgnlllttdgtlkisdfgvaEALDLfaeddtcTTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAY--GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCL 461
Cdd:cd14119   160 QGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKG---EYTIPDDVDPDLQDLLRGML 236
                         250
                  ....*....|....*.
gi 1774959464 462 EMDVEKRGSAKELLQH 477
Cdd:cd14119   237 EKDPEKRFTIEQIRQH 252
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
269-485 2.32e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 69.77  E-value: 2.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  269 KYTRFEKIGQGASGTVYTAMDVATgQEV----AIKQMNLQQQPKKELIInEILVMRENKNPNIVNYLDSYL--VGDELWV 342
Cdd:PTZ00266    14 EYEVIKKIGNGRFGEVFLVKHKRT-QEFfcwkAISYRGLKEREKSQLVI-EVNVMRELKHKNIVRYIDRFLnkANQKLYI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  343 VMEYLAGGSLTDVVTETCMDEGQIA---------------AVC--------------REITPE----------------- 376
Cdd:PTZ00266    92 LMEFCDAGDLSRNIQKCYKMFGKIEehaivditrqllhalAYChnlkdgpngervlhRDLKPQniflstgirhigkitaq 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464  377 -----------------------QSKRSTMVGTPYWMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA 431
Cdd:PTZ00266   172 annlngrpiakigdfglsknigiESMAHSCVGTPYYWSPELLLHetKSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQ 251
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464  432 LYLIATNGtPELQ---NPEKLSAIFRDFLNrcleMDVEKRGSAKELLQHQFLKIAKP 485
Cdd:PTZ00266   252 LISELKRG-PDLPikgKSKELNILIKNLLN----LSAKERPSALQCLGYQIIKNVGP 303
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
269-482 2.48e-12

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 67.82  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLD------SYLVGDEL 340
Cdd:cd07850     1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpFQNVTHAKRAYRELVLMKLVNHKNIIGLLNvftpqkSLEEFQDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVME--------------------YL-------------AGGSLTD------VVTETC----MDEG--QIAAVCREITP 375
Cdd:cd07850    81 YLVMElmdanlcqviqmdldhermsYLlyqmlcgikhlhsAGIIHRDlkpsniVVKSDCtlkiLDFGlaRTAGTSFMMTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 376 EqskrstmVGTPYWMAPEVVTRKAYGPKVDIWSLG-IMAiEMIE---------------------GEPP----------- 422
Cdd:cd07850   161 Y-------VVTRYYRAPEVILGMGYKENVDIWSVGcIMG-EMIRgtvlfpgtdhidqwnkiieqlGTPSdefmsrlqptv 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774959464 423 --YLNENPLRALYLIA-----TNGTPELQNPEKLSA-IFRDFLNRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd07850   233 rnYVENRPKYAGYSFEelfpdVLFPPDSEEHNKLKAsQARDLLSKMLVIDPEKRISVDDALQHPYINV 300
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
274-480 3.07e-12

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: 66.70  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMN--------LQQQPKKELIIN-EILVMREN------KNPNIVNYLDSYLVGD 338
Cdd:cd14077     7 KTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglkKEREKRLEKEISrDIRTIREAalssllNHPHICRLRDFLRTPN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYLAGGSLTD-VVTETCMDEG-------QIAA----------VCREITPE-----------------------Q 377
Cdd:cd14077    87 HYYMLFEYVDGGQLLDyIISHGKLKEKqarkfarQIASaldylhrnsiVHRDLKIEnilisksgnikiidfglsnlydpR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELqnPEKLSAIFRDF 456
Cdd:cd14077   167 RLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDEN-MPALHAKIKKGKVEY--PSYLSSECKSL 243
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14077   244 ISRMLVVDPKKRATLEQVLNHPWM 267
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
269-479 3.14e-12

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: 66.55  E-value: 3.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIE-RGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTET---CMDEGQI--------------AAVC-REITPEQ------------------SKRSTM-------VG 385
Cdd:cd14665    80 GGELFERICNAgrfSEDEARFffqqlisgvsychsMQIChRDLKLENtlldgspaprlkicdfgySKSSVLhsqpkstVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNGTPELQNPE--KLSAIFRDFLNRCL 461
Cdd:cd14665   160 TPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDpEEPRNFRKTIQRILSVQYSIPDyvHISPECRHLISRIF 239
                         250
                  ....*....|....*...
gi 1774959464 462 EMDVEKRGSAKELLQHQF 479
Cdd:cd14665   240 VADPATRITIPEIRNHEW 257
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
276-477 3.34e-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: 66.60  E-value: 3.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAmdVATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14146     2 IGVGGFGKVYRA--TWKGQEVAVKAA--RQDPDEDIKATAESVRQEAKlfsmlrHPNIIKLEGVCLEEPNLCLVMEFARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMDEG-----------------QIAA---------------------------------VCRE------- 372
Cdd:cd14146    78 GTLNRALAAANAAPGprrarripphilvnwavQIARgmlylheeavvpilhrdlkssnilllekiehddICNKtlkitdf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 -ITPEQSKRSTM--VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpELQNPEKL 449
Cdd:cd14146   158 gLAREWHRTTKMsaAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKL-TLPIPSTC 236
                         250       260
                  ....*....|....*....|....*...
gi 1774959464 450 SAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14146   237 PEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
275-480 3.72e-12

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: 66.50  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQ--QPKKELIINEILVMR-ENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd14197    16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRkgQDCRMEIIHEIAVLElAQANPWVINLHEVYETASEMILVLEYAAGGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVT---ETCMDEGQIAAVCREI-----------------TPE---------------------------QSKRSTMv 384
Cdd:cd14197    96 IFNQCVadrEEAFKEKDVKRLMKQIlegvsflhnnnvvhldlKPQnilltsesplgdikivdfglsrilknsEELREIM- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAT-NGTPELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd14197   175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQmNVSYSEEEFEHLSESAIDFIKTLLIK 254
                         250
                  ....*....|....*..
gi 1774959464 464 DVEKRGSAKELLQHQFL 480
Cdd:cd14197   255 KPENRATAEDCLKHPWL 271
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
274-480 4.64e-12

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: 66.52  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK------KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd14196    11 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVTET-CMDEGQIAAVCREI-----------------TPEQ---------------------------SKRST 382
Cdd:cd14196    91 SGGELFDFLAQKeSLSEEEATSFIKQIldgvnylhtkkiahfdlKPENimlldknipiphiklidfglaheiedgVEFKN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAIFRDFLNRCL 461
Cdd:cd14196   171 IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItAVSYDFDEEFFSHTSELAKDFIRKLL 250
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd14196   251 VKETRKRLTIQEALRHPWI 269
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
274-480 5.52e-12

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 66.10  E-value: 5.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVA---IKQMNLQQQPKKElIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAakfLKKRRRGQDCRAE-ILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMD---EGQIAAVCREI-----------------TPEQ-------------------SKR-------STM 383
Cdd:cd14198    93 GEIFNLCVPDLAEmvsENDIIRLIRQIlegvyylhqnnivhldlKPQNillssiyplgdikivdfgmSRKighacelREI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE-NPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLE 462
Cdd:cd14198   173 MGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEdNQETFLNISQVNVDYSEETFSSVSQLATDFIQKLLV 252
                         250
                  ....*....|....*...
gi 1774959464 463 MDVEKRGSAKELLQHQFL 480
Cdd:cd14198   253 KNPEKRPTAEICLSHSWL 270
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
270-480 5.97e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 66.97  E-value: 5.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14176    21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTD-VVTETCMDEGQIAAVCREIT-----------------------------PEQSK------------RSTMVGTP 387
Cdd:cd14176    98 GELLDkILRQKFFSEREASAVLFTITktveylhaqgvvhrdlkpsnilyvdesgnPESIRicdfgfakqlraENGLLMTP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YW----MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN---ENPLRALYLIATnGTPELQNP--EKLSAIFRDFLN 458
Cdd:cd14176   178 CYtanfVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGS-GKFSLSGGywNSVSDTAKDLVS 256
                         250       260
                  ....*....|....*....|..
gi 1774959464 459 RCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14176   257 KMLHVDPHQRLTAALVLRHPWI 278
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
267-423 7.72e-12

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: 65.36  E-value: 7.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDvATGQEVAIKQMNLQQ-QPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd14161     2 KHRYEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRiKDEQDLlhIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTETC-MDEGQIAAVCREITP----------------------------------------EQSKRST 382
Cdd:cd14161    81 MEYASRGDLYDYISERQrLSELEARHFFRQIVSavhychangivhrdlklenilldangnikiadfglsnlynQDKFLQT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 383 MVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd14161   161 YCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPF 202
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
274-476 9.44e-12

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: 65.16  E-value: 9.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIK--QMNLQQQPKKELiINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKtcRETLPPDLKRKF-LQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVV--TETCMDEGQIAAVCRE-------------ITPEQSKRSTMVG-----------------------------TP 387
Cdd:cd05041    80 LLTFLrkKGARLTVKQLLQMCLDaaagmeyleskncIHRDLAARNCLVGennvlkisdfgmsreeedgeytvsdglkqIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 Y-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd05041   160 IkWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQIESGY--RMPAPELCPEAVYRLMLQCWAYDP 237
                         250
                  ....*....|.
gi 1774959464 466 EKRGSAKELLQ 476
Cdd:cd05041   238 ENRPSFSEIYN 248
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
274-477 9.77e-12

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: 65.39  E-value: 9.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQmnLQQQPKKEliiNEI-LVMRENKNPNIVNYLDSY--LVGDE--LWVVMEYLA 348
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKV--LRDNPKAR---REVeLHWRASGCPHIVRIIDVYenTYQGRkcLLVVMECME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTETC---MDEGQIAAVCREIT-----------------PE------------------------QSKRS--T 382
Cdd:cd14089    82 GGELFSRIQERAdsaFTEREAAEIMRQIGsavahlhsmniahrdlkPEnllysskgpnailkltdfgfaketTTKKSlqT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLG-IMAIeMIEGEPPYLNENPLRalylIA-------TNGTPELQNPE--KLSAI 452
Cdd:cd14089   162 PCYTPYYVAPEVLGPEKYDKSCDMWSLGvIMYI-LLCGYPPFYSNHGLA----ISpgmkkriRNGQYEFPNPEwsNVSEE 236
                         250       260
                  ....*....|....*....|....*
gi 1774959464 453 FRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14089   237 AKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
276-481 1.20e-11

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: 65.78  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELII--NEI----------LVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKAL------KKGDIIarDEVeslmcekrifETVNSARHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSL-----TDVVTET-------C------------------------MD-EG--QIA--AVCREITPEQSKRST 382
Cdd:cd05589    81 MEYAAGGDLmmhihEDVFSEPravfyaaCvvlglqflhehkivyrdlkldnllLDtEGyvKIAdfGLCKEGMGFGDRTST 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLS----AIFRDFLN 458
Cdd:cd05589   161 FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSteaiSIMRRLLR 237
                         250       260
                  ....*....|....*....|....*...
gi 1774959464 459 RClemdVEKR-GS----AKELLQHQFLK 481
Cdd:cd05589   238 KN----PERRlGAserdAEDVKKQPFFR 261
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
270-480 1.49e-11

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: 64.51  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTA--MDVATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLekfLPRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVV-TETCMDEGQ--------IAAV--------------C-------------------REITPEQSKR-- 380
Cdd:cd14080    82 EYAEHGDLLEYIqKRGALSESQariwfrqlALAVqylhsldiahrdlkCenilldsnnnvklsdfgfaRLCPDDDGDVls 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMIEGEPPYlNENPLRALYLIATN---GTPElqNPEKLSAIFRDF 456
Cdd:cd14080   162 KTFCGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPF-DDSNIKKMLKDQQNrkvRFPS--SVKKLSPECKDL 238
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14080   239 IDQLLEPDPTKRATIEEILNHPWL 262
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
270-481 2.19e-11

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: 65.08  E-value: 2.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQM----NLQQQPKKELiiNEILVMRENKNPNIVNYLD------SYLVGDE 339
Cdd:cd07855     7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafDVVTTAKRTL--RELKILRHFKHDNIIAIRDilrpkvPYADFKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYL---------AGGSLTD--------------------------------VVTETCM----DEGQIAAVCREIT 374
Cdd:cd07855    85 VYVVLDLMesdlhhiihSDQPLTLehiryflyqllrglkyihsanvihrdlkpsnlLVNENCElkigDFGMARGLCTSPE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 PEQSKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN-GTPE---------- 442
Cdd:cd07855   165 EHKYFMTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVlGTPSqavinaigad 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774959464 443 -----LQN-----PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07855   245 rvrryIQNlpnkqPVPWETLYPkadqqalDLLSQMLRFDPSERITVAEALQHPFLA 300
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
276-480 2.22e-11

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: 65.04  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVLQkkaiLKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 L-TDVVTETCMDE-------GQIAA----------VCREITPEQ------------------------SKRSTMVGTPYW 389
Cdd:cd05602    95 LfYHLQRERCFLEprarfyaAEIASalgylhslniVYRDLKPENilldsqghivltdfglckeniepnGTTSTFCGTPEY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKRG 469
Cdd:cd05602   175 LAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNK---PLQLKPNITNSARHLLEGLLQKDRTKRL 251
                         250
                  ....*....|....*
gi 1774959464 470 SAK----ELLQHQFL 480
Cdd:cd05602   252 GAKddftEIKNHIFF 266
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
270-481 2.61e-11

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: 65.03  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlqqqpKKELIINE----------ILVmrENKNPNIVNYLDSYLVGDE 339
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLR-----KKDVLKRNqvahvkaerdILA--EADNEWVVKLYYSFQDKEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTETCMDEGQIAA------VC------------REITPEQ------------------------ 377
Cdd:cd05598    76 LYFVMDYIPGGDLMSLLIKKGIFEEDLARfyiaelVCaiesvhkmgfihRDIKPDNilidrdghikltdfglctgfrwth 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 -SKR---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTNGTPELQNPE--KLSA 451
Cdd:cd05598   156 dSKYylaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKV-INWRTTLKIPHeaNLSP 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1774959464 452 IFRDFLNRcLEMDVEKR---GSAKELLQHQFLK 481
Cdd:cd05598   235 EAKDLILR-LCCDAEDRlgrNGADEIKAHPFFA 266
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
276-480 2.76e-11

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: 64.61  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQkktiLKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 L-TDVVTETCMDE-------GQIAA----------VCREITPE------------------------QSKRSTMVGTPYW 389
Cdd:cd05603    83 LfFHLQRERCFLEprarfyaAEVASaigylhslniIYRDLKPEnilldcqghvvltdfglckegmepEETTSTFCGTPEY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNPEKLSAIfrDFLNRCLEMDVEKRG 469
Cdd:cd05603   163 LAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRD-VSQMYDNILHKPLHLPGGKTVAAC--DLLQGLLHKDQRRRL 239
                         250
                  ....*....|....*
gi 1774959464 470 SAK----ELLQHQFL 480
Cdd:cd05603   240 GAKadflEIKNHVFF 254
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
274-480 2.79e-11

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: 64.40  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQmnLQQQPKKELIINeiLVMRENKNPNIVNYLDSY-----LVGDE-----LWVV 343
Cdd:cd14171    12 QKLGTGISGPVRVCVKKSTGERFALKI--LLDRPKARTEVR--LHMMCSGHPNIVQIYDVYansvqFPGESsprarLLIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVT--------ETCMDEGQIA-AVC---------REITPE------------------------QSKRS 381
Cdd:cd14171    88 MELMEGGELFDRISqhrhftekQAAQYTKQIAlAVQhchslniahRDLKPEnlllkdnsedapiklcdfgfakvdQGDLM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVV-----------------TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-------YLIAT 437
Cdd:cd14171   168 TPQFTPYYVAPQVLeaqrrhrkersgiptspTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTItkdmkrkIMTGS 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1774959464 438 NGTPElQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14171   248 YEFPE-EEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
283-484 3.00e-11

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


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 64.51  E-value: 3.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 283 TVYTAMDVATGQEVAIKQMNLQQQPKKELII--NEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS----LTDVV 356
Cdd:cd08226    15 SVYLARHTPTGTLVTVKITNLDNCSEEHLKAlqNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSarglLKTYF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 357 TETcMDEGQIAAVC-----------------REITP-----------------------EQSKRSTMV--------GTPY 388
Cdd:cd08226    95 PEG-MNEALIGNILygaikalnylhqngcihRSVKAshilisgdglvslsglshlysmvTNGQRSKVVydfpqfstSVLP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYG--PKVDIWSLGIMAIEMIEGEPPYLN-----------ENPLRALYLIA------------------- 436
Cdd:cd08226   174 WLSPELLRQDLHGynVKSDIYSVGITACELARGQVPFQDmrrtqmllqklKGPPYSPLDIFpfpelesrmknsqsgmdsg 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 437 ------------TNGTPELQNP--EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAK 484
Cdd:cd08226   254 igesvatssmtrTMTSERLQTPssKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVK 315
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
274-477 3.02e-11

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: 64.36  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEI-LVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd14090     8 ELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVeTLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGGPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTE-TCMDEGQIAAVCREI-------------------------------------------------------TPE 376
Cdd:cd14090    88 LSHIEKrVHFTEQEASLVVRDIasaldflhdkgiahrdlkpenilcesmdkvspvkicdfdlgsgiklsstsmtpvtTPE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 QskrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMIEGEPPYLNE----------NPLRAL--YLIATNG 439
Cdd:cd14090   168 L---LTPVGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrgEACQDCqeLLFHSIQ 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 440 TPELQNPEK----LSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14090   245 EGEYEFPEKewshISAEAKDLISHLLVRDASQRYTAEQVLQH 286
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
276-480 3.14e-11

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: 64.04  E-value: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVAT-----GQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd14076     9 LGEGEFGKVKLGWPLPKanhrsGVQVAIKLIrrdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVV--------TETCMDEGQIAA----------VCREITPEQ----SKR---------------------STMV 384
Cdd:cd14076    89 SGGELFDYIlarrrlkdSVACRLFAQLISgvaylhkkgvVHRDLKLENllldKNRnlvitdfgfantfdhfngdlmSTSC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPE-VVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLN--ENP----LRALYLIATNgTPeLQNPEKLSAIFRDF 456
Cdd:cd14076   169 GSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFDDdpHNPngdnVPRLYRYICN-TP-LIFPEYVTPKARDL 246
                         250       260
                  ....*....|....*....|....
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14076   247 LRRILVPNPRKRIRLSAIMRHAWL 270
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
272-477 3.57e-11

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: 63.56  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 272 RFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQ-------QQPKKELIINEILvmreNKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd13997     4 ELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPfrgpkerARALREVEAHAAL----GQHPNIVRYYSSWEEGGHLYIQM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVTE----TCMDEGQI----AAVCREITPEQSKR--------------------------------STMV 384
Cdd:cd13997    80 ELCENGSLQDALEElspiSKLSEAEVwdllLQVALGLAFIHSKGivhldikpdnifisnkgtckigdfglatrletSGDV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 --GTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPpyLNEN-----PLRALYLiatngtPELQNPeKLSAIFRDF 456
Cdd:cd13997   160 eeGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEP--LPRNgqqwqQLRQGKL------PLPPGL-VLSQELTRL 230
                         250       260
                  ....*....|....*....|.
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQH 477
Cdd:cd13997   231 LKVMLDPDPTRRPTADQLLAH 251
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
271-486 4.23e-11

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: 63.93  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 271 TRFEK---IGQGASGTVYTAMDVATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLDsYLVGDEL--- 340
Cdd:cd07845     7 TEFEKlnrIGEGTYGIVYRARDTTSGEIVALKKVRMDNE--RDGIpissLREITLLLNLRHPNIVELKE-VVVGKHLdsi 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEY----LAggSLTDVVTeTCMDEGQIAAVCREI------------------------------------------T 374
Cdd:cd07845    84 FLVMEYceqdLA--SLLDNMP-TPFSESQVKCLMLQLlrglqylhenfiihrdlkvsnllltdkgclkiadfglartygL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 PEQSKRSTMVgTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN-GTP---------EL 443
Cdd:cd07845   161 PAKPMTPKVV-TLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLlGTPnesiwpgfsDL 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 444 QNPEK-----------------LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKiAKPL 486
Cdd:cd07845   240 PLVGKftlpkqpynnlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK-EKPL 298
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
276-424 4.45e-11

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: 63.26  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKqMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT-- 353
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALK-MN-TLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEql 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 ----------------------------------DVVTETCM---DEGQIAAVC-----REITPEQSKRS---TMVGTPY 388
Cdd:cd14155    79 ldsneplswtvrvklaldiarglsylhskgifhrDLTSKNCLikrDENGYTAVVgdfglAEKIPDYSDGKeklAVVGSPY 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMI---EGEPPYL 424
Cdd:cd14155   159 WMAPEVLRGEPYNEKADVFSYGIILCEIIariQADPDYL 197
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
268-480 5.06e-11

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 64.15  E-value: 5.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLD---SYLVGDEL-- 340
Cdd:cd07879    15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpFQSEIFAKRAYRELTLLKHMQHENVIGLLDvftSAVSGDEFqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 -WVVMEYL-------AGGSLTD-----VVTETCMDEGQIAA---VCREITP------------------EQSKRSTMVG- 385
Cdd:cd07879    95 fYLVMPYMqtdlqkiMGHPLSEdkvqyLVYQMLCGLKYIHSagiIHRDLKPgnlavnedcelkildfglARHADAEMTGy 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 --TPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKL------------ 449
Cdd:cd07879   175 vvTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQIlKVTGVPGPEFVQKLedkaaksyiksl 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464 450 ---------------SAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07879   255 pkyprkdfstlfpkaSPQAVDLLEKMLELDVDKRLTATEALEHPYF 300
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
382-480 5.41e-11

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: 64.26  E-value: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA-LYLIATNGTPELQNPEKLSAIFRDFLNR- 459
Cdd:cd05626   207 SLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETqLKVINWENTLHIPPQVKLSPEAVDLITKl 286
                          90       100
                  ....*....|....*....|..
gi 1774959464 460 -CLEMDVEKRGSAKELLQHQFL 480
Cdd:cd05626   287 cCSAEERLGRNGADDIKAHPFF 308
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
276-481 6.12e-11

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: 63.42  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEILV---MRENK-------NPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKAL------KKDVVLIDDDVectMVEKRvlalaweNPFLTHLYCTFQTKEHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLT------------------------------------DVVTETCM--DEGQIA----AVCREITPEQSKRSTM 383
Cdd:cd05620    77 FLNGGDLMfhiqdkgrfdlyratfyaaeivcglqflhskgiiyrDLKLDNVMldRDGHIKiadfGMCKENVFGDNRASTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgTPELqnPEKLSAIFRDFLNRCLEM 463
Cdd:cd05620   157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVD-TPHY--PRWITKESKDILEKLFER 233
                         250
                  ....*....|....*....
gi 1774959464 464 DVEKR-GSAKELLQHQFLK 481
Cdd:cd05620   234 DPTRRlGVVGNIRGHPFFK 252
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
276-486 6.43e-11

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: 62.92  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIY--KNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 -------------------------------------------------VTETCMDEGQIAAVCREITPEQSKRS-TMVG 385
Cdd:cd14156    79 lareelplswrekvelacdisrgmvylhskniyhrdlnsknclirvtprGREAVVTDFGLAREVGEMPANDPERKlSLVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---IEGEPPYLNENPLRALYLIA----TNGTPELqnpeklsaiFRDFLN 458
Cdd:cd14156   159 SAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIlarIPADPEVLPRTGDFGLDVQAfkemVPGCPEP---------FLDLAA 229
                         250       260
                  ....*....|....*....|....*...
gi 1774959464 459 RCLEMDVEKRGSAKELLQhQFLKIAKPL 486
Cdd:cd14156   230 SCCRMDAFKRPSFAELLD-ELEDIAETL 256
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
274-480 6.75e-11

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: 62.53  E-value: 6.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqPKKELIINEILVMRENKNPNIVNYLDSYLV-GDELWVVMEYLAGGSL 352
Cdd:cd14109    10 EDEKRAAQGAPFHVTERSTGRNFLAQLR-----YGDPFLMREVDIHNSLDHPNIVQMHDAYDDeKLAVTVIDNLASTIEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 --------TDVVTETC--------------MDEGQIAAVcrEITPE---------------QSKR-------STMVGTPY 388
Cdd:cd14109    85 vrdnllpgKDYYTERQvavfvrqlllalkhMHDLGIAHL--DLRPEdillqddklkladfgQSRRllrgkltTLIYGSPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP-EKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd14109   163 FVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPlGNISDDARDFIKKLLVYIPES 242
                         250
                  ....*....|...
gi 1774959464 468 RGSAKELLQHQFL 480
Cdd:cd14109   243 RLTVDEALNHPWF 255
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
241-481 6.81e-11

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: 63.90  E-value: 6.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 241 KQKKKPKMSDEEILEKlrsivsvgdpkkkytrfekIGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEIL 317
Cdd:cd05600     3 KRRTRLKLSDFQILTQ-------------------VGQGGYGSVFLARKKDTGEICALKIMKkkvLFKLNEVNHVLTERD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 318 VMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS----LTDV-----------VTE--TCMDE-GQIAAVCREITPE--- 376
Cdd:cd05600    64 ILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGDfrtlLNNSgilseeharfyIAEmfAAISSlHQLGYIHRDLKPEnfl 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 ----------------------------------------------------------QSKRSTMVGTPYWMAPEVVTRK 398
Cdd:cd05600   144 idssghikltdfglasgtlspkkiesmkirleevkntafleltakerrniyramrkedQNYANSVVGSPDYMAPEVLRGE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 399 AYGPKVDIWSLGIMAIEMIEGEPPY----LNENPLRALYLIATNGTPELQNPEK---LSAIFRDFLNRCLeMDVEKR-GS 470
Cdd:cd05600   224 GYDLTVDYWSLGCILFECLVGFPPFsgstPNETWANLYHWKKTLQRPVYTDPDLefnLSDEAWDLITKLI-TDPQDRlQS 302
                         330
                  ....*....|.
gi 1774959464 471 AKELLQHQFLK 481
Cdd:cd05600   303 PEQIKNHPFFK 313
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
262-480 7.55e-11

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 63.53  E-value: 7.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 262 SVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlqqQPKKELI-----INEILVMRENKNPNIVNYLDSYLV 336
Cdd:cd07878     9 TVWEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLS---RPFQSLIharrtYRELRLLKHMKHENVIGLLDVFTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 337 G------DELWVVMEyLAGGSLTDVVTETCMDEGQI-----------------AAVCREITPEQ---------------- 377
Cdd:cd07878    86 AtsienfNEVYLVTN-LMGADLNNIVKCQKLSDEHVqfliyqllrglkyihsaGIIHRDLKPSNvavnedcelrildfgl 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 -----SKRSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEP-----PYLNEnpLRALYLIATNGTPEL--- 443
Cdd:cd07878   165 arqadDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKAlfpgnDYIDQ--LKRIMEVVGTPSPEVlkk 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464 444 --------------QNPEK-LSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07878   243 isseharkyiqslpHMPQQdLKKIFRganplaiDLLEKMLVLDSDKRISASEALAHPYF 301
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
265-480 7.74e-11

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: 62.64  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPK--KKYTRFEKIGQGASGTVYTAMDVATGQ----EVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGD 338
Cdd:cd14187     2 DPRtrRRYVRGRFLGKGGFAKCYEITDADTKEvfagKIVPKSLLLKPH-QKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYLAGGSLTDV------VTET------------CM--------------------DEGQIA----AVCREITPE 376
Cdd:cd14187    81 FVYVVLELCRRRSLLELhkrrkaLTEPearyylrqiilgCQylhrnrvihrdlklgnlflnDDMEVKigdfGLATKVEYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYL-IATNgtpELQNPEKLSAIFRD 455
Cdd:cd14187   161 GERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPF-ETSCLKETYLrIKKN---EYSIPKHINPVAAS 236
                         250       260
                  ....*....|....*....|....*
gi 1774959464 456 FLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14187   237 LIQKMLQTDPTARPTINELLNDEFF 261
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
370-480 8.22e-11

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: 62.60  E-value: 8.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 370 CREITPEQSKRSTMvGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELQNPE-- 447
Cdd:cd14107   147 AQEITPSEHQFSKY-GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGEND-RATLLNVAEGVVSWDTPEit 224
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1774959464 448 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14107   225 HLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
270-477 8.73e-11

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: 62.70  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGD-----ELWVVM 344
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaggkkEVYLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSLTDVVT-------------------ETC----------------------------------MDEGQIAAVCR 371
Cdd:cd13986    82 PYYKRGSLQDEIErrlvkgtffpedrilhiflGICrglkamhepelvpyahrdikpgnvllseddepilMDLGSMNPARI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 372 EITPEQ---------SKRSTMVgtpyWMAPEVVTRKAYG---PKVDIWSLGIMAIEMIEGEPPY-LNENPLRALYLIATN 438
Cdd:cd13986   162 EIEGRRealalqdwaAEHCTMP----YRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFeRIFQKGDSLALAVLS 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1774959464 439 GTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd13986   238 GNYSFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
275-424 9.48e-11

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: 62.67  E-value: 9.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD-----SYLVGDEL-WVVMEYL 347
Cdd:cd14038     1 RLGTGGFGNVLRWINQETGEQVAIKQCRQELSPKnRERWCLEIQIMKRLNHPNVVAARDvpeglQKLAPNDLpLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVT--ETC--MDEGQIAA-----------------VCREITPEQ------SKR-------------------- 380
Cdd:cd14038    81 QGGDLRKYLNqfENCcgLREGAILTllsdissalrylhenriIHRDLKPENivlqqgEQRlihkiidlgyakeldqgslc 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL 424
Cdd:cd14038   161 TSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
274-468 1.04e-10

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: 62.74  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd08229    30 KKIGRGQFSEVYRATCLLDGVPVALKKVqifDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTDVVTETCMDEGQI---------AAVC-------------REITPEQ--------------------SKRST----MV 384
Cdd:cd08229   110 DLSRMIKHFKKQKRLIpektvwkyfVQLCsalehmhsrrvmhRDIKPANvfitatgvvklgdlglgrffSSKTTaahsLV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE--NPLRALYLIATNGTPELQNpEKLSAIFRDFLNRCLE 462
Cdd:cd08229   190 GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLYSLCKKIEQCDYPPLPS-DHYSEELRQLVNMCIN 268

                  ....*.
gi 1774959464 463 MDVEKR 468
Cdd:cd08229   269 PDPEKR 274
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
269-480 1.07e-10

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: 62.97  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqQQPKKELII-----NEILVMRENKNPNIVNYLDSYLVGDE-LWV 342
Cdd:cd07856    11 RYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKI---MKPFSTPVLakrtyRELKLLKHLRHENIISLSDIFISPLEdIYF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEyLAGGSLTDVVTETCMDEG-------QI----------AAVCREITP---------------------EQSKRSTMV 384
Cdd:cd07856    88 VTE-LLGTDLHRLLTSRPLEKQfiqyflyQIlrglkyvhsaGVIHRDLKPsnilvnencdlkicdfglariQDPQMTGYV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMIEGEPPY---------------LNENPLRALYLIATNGTPEL----- 443
Cdd:cd07856   167 STRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitelLGTPPDDVINTICSENTLRFvqslp 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 444 -QNPEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07856   247 kRERVPFSEKFKnadpdaiDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
276-476 1.11e-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: 61.93  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAmdVATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14148     2 IGVGGFGKVYKG--LWRGEEVAVKAA--RQDPDEDIAVTAENVRQEARlfwmlqHPNIIALRGVCLNPPHLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVT----------------ETCMD----EGQIAAVCREITP----------------------------EQSKRS 381
Cdd:cd14148    78 GALNRALAgkkvpphvlvnwavqiARGMNylhnEAIVPIIHRDLKSsnililepienddlsgktlkitdfglarEWHKTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TM--VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpELQNPEKLSAIFRDFLNR 459
Cdd:cd14148   158 KMsaAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKL-TLPIPSTCPEPFARLLEE 236
                         250
                  ....*....|....*..
gi 1774959464 460 CLEMDVEKRGSAKELLQ 476
Cdd:cd14148   237 CWDPDPHGRPDFGSILK 253
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
276-427 1.15e-10

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: 62.89  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINE-----------ILVMrENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVL------KKDVILQDddvdctmtekrILAL-AAKHPFLTALHSCFQTKDRLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYLAGGSL------------------TDVVTETCM--------------------DEGQIA----AVCREITPEQSKRST 382
Cdd:cd05591    76 EYVNGGDLmfqiqrarkfdeprarfyAAEVTLALMflhrhgviyrdlkldnilldAEGHCKladfGMCKEGILNGKTTTT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 427
Cdd:cd05591   156 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 200
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
276-481 1.23e-10

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: 62.79  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINE-----ILVMRE-----NKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKAL------KKDVVLEDddvecTMIERRvlalaSQHPFLTHLFCTFQTESHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSL-------------------TDVVT------------------ETCMD-EGQIA----AVCREITPEQSKRSTM 383
Cdd:cd05592    77 YLNGGDLmfhiqqsgrfdedrarfygAEIICglqflhsrgiiyrdlkldNVLLDrEGHIKiadfGMCKENIYGENKASTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEM 463
Cdd:cd05592   157 CGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDE-DELFWSICNDTPHY--PRWLTKEAASCLSLLLER 233
                         250       260
                  ....*....|....*....|...
gi 1774959464 464 DVEKR-----GSAKELLQHQFLK 481
Cdd:cd05592   234 NPEKRlgvpeCPAGDIRDHPFFK 256
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
364-480 1.23e-10

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: 62.59  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 364 GQIA----AVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNg 439
Cdd:cd05585   131 GHIAlcdfGLCKLNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQE- 209
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 440 tpELQNPEKLSAIFRDFLNRCLEMDVEKR---GSAKELLQHQFL 480
Cdd:cd05585   210 --PLRFPDGFDRDAKDLLIGLLNRDPTKRlgyNGAQEIKNHPFF 251
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
274-477 1.44e-10

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: 61.97  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAmdVATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd14147     9 EVIGIGGFGKVYRG--SWRGELVAVKAA--RQDPDEDISVTAESVRQEARlfamlaHPNIIALKAVCLEEPNLCLVMEYA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVT------------ETCMDEGQIAAVCREITP------------------------------------EQSK 379
Cdd:cd14147    85 AGGPLSRALAgrrvpphvlvnwAVQIARGMHYLHCEALVPvihrdlksnnilllqpienddmehktlkitdfglarEWHK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 RSTM--VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpELQNPEKLSAIFRDFL 457
Cdd:cd14147   165 TTQMsaAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKL-TLPIPSTCPEPFAQLM 243
                         250       260
                  ....*....|....*....|
gi 1774959464 458 NRCLEMDVEKRGSAKELLQH 477
Cdd:cd14147   244 ADCWAQDPHRRPDFASILQQ 263
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
276-443 1.46e-10

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: 61.70  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERkaLLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DV----------------VTET--------CMDEG-------------------QIA----AVCREITPEQSKRSTM--- 383
Cdd:cd13978    81 SLlereiqdvpwslrfriIHEIalgmnflhNMDPPllhhdlkpenilldnhfhvKISdfglSKLGMKSISANRRRGTenl 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 384 VGTPYWMAPEVVTRKAYGP--KVDIWSLGIMAIEMIEGEPPYLNE-NPLRALYLIATNGTPEL 443
Cdd:cd13978   161 GGTPIYMAPEAFDDFNKKPtsKSDVYSFAIVIWAVLTRKEPFENAiNPLLIMQIVSKGDRPSL 223
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
269-423 1.56e-10

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: 61.53  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQ------QQPKKELIIneilvMRENKNPNIVNYLDSYLVGDELWV 342
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPksssavEDSRKEAVL-----LAKMKHPNIVAFKESFEADGHLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEYLAGGSLTDVV-----------------TETCMDEGQIA---------------------------AVCREITPEQS 378
Cdd:cd08219    76 VMEYCDGGDLMQKIklqrgklfpedtilqwfVQMCLGVQHIHekrvlhrdiksknifltqngkvklgdfGSARLLTSPGA 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 379 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd08219   156 YACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPF 200
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
270-481 1.59e-10

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: 61.40  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQ----PKKELIINEILVMRE----NKNPNIVNYLDSYLVGDE 339
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQIsrNRVQQwsklPGVNPVPNEVALLQSvgggPGHRGVIRLLDWFEIPEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEY-LAGGSLTDVVTET-CMDEGQ--------IAAVC---------REITPEQ----------------------- 377
Cdd:cd14101    82 FLLVLERpQHCQDLFDYITERgALDESLarrffkqvVEAVQhchskgvvhRDIKDENilvdlrtgdiklidfgsgatlkd 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPY-LNENPLRAlyliatngtpELQNPEKLSAIFRD 455
Cdd:cd14101   162 SMYTDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFeRDTDILKA----------KPSFNKRVSNDCRS 231
                         250       260
                  ....*....|....*....|....*.
gi 1774959464 456 FLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14101   232 LIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
269-479 1.74e-10

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 61.77  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQ----PKKELIINEILVMReNKNPNIVNYLDSYLVGDE----L 340
Cdd:cd07837     2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEeegvPSTALREVSLLQML-SQSIYIVRLLDVEHVEENgkplL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAG-----------GSLTDVVTET--------------CMDEG--------------------QIA--AVCREI 373
Cdd:cd07837    81 YLVFEYLDTdlkkfidsygrGPHNPLPAKTiqsfmyqlckgvahCHSHGvmhrdlkpqnllvdkqkgllKIAdlGLGRAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 TPEQSKRSTMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQ------- 444
Cdd:cd07837   161 TIPIKSYTHEIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIfRLLGTPNEEvwpgvsk 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 445 ----------NPEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07837   241 lrdwheypqwKPQDLSRAVPdlepegvDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
269-479 1.86e-10

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: 61.57  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIK--QMNLQ-QQPKKELII----NEILVMRENKNPNIVNYLDSYLVG-DEL 340
Cdd:cd13990     1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKihQLNKDwSEEKKQNYIkhalREYEIHKSLDHPRIVKLYDVFEIDtDSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLtDVVTETC----------------------------------------MDEGQIAAVCReIT------ 374
Cdd:cd13990    81 CTVLEYCDGNDL-DFYLKQHksiperearsiimqvvsalkylneikppiihydlkpgnilLHSGNVSGEIK-ITdfglsk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 ---PEQSKRSTM------VGTPYWMAPEVVTRKAYGP----KVDIWSLGIMAIEMIEGEPPY-LNENPLRalylIATNGT 440
Cdd:cd13990   159 imdDESYNSDGMeltsqgAGTYWYLPPECFVVGKTPPkissKVDVWSVGVIFYQMLYGRKPFgHNQSQEA----ILEENT 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 441 P----ELQNPEK--LSAIFRDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd13990   235 IlkatEVEFPSKpvVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
276-427 2.31e-10

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: 61.94  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDS-YLVGDELWVVMEYLAGGS 351
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKkdvVIQDDDVECTMVEKRVLALSGKPPFLTQLHScFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LT------------------------------------DVVTETCM--DEGQIA----AVCREITPEQSKRSTMVGTPYW 389
Cdd:cd05616    88 LMyhiqqvgrfkephavfyaaeiaiglfflqskgiiyrDLKLDNVMldSEGHIKiadfGMCKENIWDGVTTKTFCGTPDY 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 427
Cdd:cd05616   168 IAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGED 205
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
276-427 2.50e-10

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: 61.90  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQkkviLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 L------------------------------------TDVVTETCM--DEGQIA----AVCREITPEQSKRSTMVGTPYW 389
Cdd:cd05604    84 LffhlqrersfpeprarfyaaeiasalgylhsinivyRDLKPENILldSQGHIVltdfGLCKEGISNSDTTTTFCGTPEY 163
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 427
Cdd:cd05604   164 LAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRD 201
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
274-481 2.62e-10

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: 61.20  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 351
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGSi 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTETCMDEGQIAAVCREI------------------------------------------------------TPEQ 377
Cdd:cd14174    88 LAHIQKRKHFNEREASRVVRDIasaldflhtkgiahrdlkpenilcespdkvspvkicdfdlgsgvklnsactpitTPEL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SkrsTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMIEGEPPYLNE----------NPLRA----LYLIATN 438
Cdd:cd14174   168 T---TPCGSAEYMAPEVVevfTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgEVCRVcqnkLFESIQE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 439 GTPELqnPEK----LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14174   245 GKYEF--PDKdwshISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
276-481 3.12e-10

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: 61.48  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEILV---MRENK-------NPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKAL------KKDVVLMDDDVectMVEKRvlslaweHPFLTHLFCTFQTKENLFFVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVVtETC--------------------------------------MD-EGQIA----AVCREITPEQSKRST 382
Cdd:cd05619    87 YLNGGDLMFHI-QSChkfdlpratfyaaeiicglqflhskgivyrdlkldnilLDkDGHIKiadfGMCKENMLGDAKTST 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpelQNPEKLSAIFRDFLNRCLE 462
Cdd:cd05619   166 FCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNP---FYPRWLEKEAKDILVKLFV 242
                         250       260
                  ....*....|....*....|
gi 1774959464 463 MDVEKR-GSAKELLQHQFLK 481
Cdd:cd05619   243 REPERRlGVRGDIRQHPFFR 262
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
269-481 3.20e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 60.99  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:PLN00009    3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEgvPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LaggsltDVVTETCMDEG---------------QI---AAVC-------REITPEQ----SKRSTM-------------- 383
Cdd:PLN00009   83 L------DLDLKKHMDSSpdfaknprliktylyQIlrgIAYChshrvlhRDLKPQNllidRRTNALkladfglarafgip 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 -------VGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQN--------- 445
Cdd:PLN00009  157 vrtftheVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIfRILGTPNEETwpgvtslpd 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 446 ---------PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:PLN00009  237 yksafpkwpPKDLATVVPtlepagvDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
276-417 3.24e-10

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 60.73  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 355
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 356 VTET------------------------------------CM---DEGQIAA---VCREITPEQ---------------- 377
Cdd:cd14222    81 LRADdpfpwqqkvsfakgiasgmaylhsmsiihrdlnshnCLiklDKTVVVAdfgLSRLIVEEKkkpppdkpttkkrtlr 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 378 ----SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 417
Cdd:cd14222   161 kndrKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
274-475 4.17e-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: 60.44  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAmdVATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd14145    12 EIIGIGGFGKVYRA--IWIGDEVAVKAA--RHDPDEDISQTIENVRQEAKlfamlkHPNIIALRGVCLKEPNLCLVMEFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVT------ETCMDEG-QIAAV-----CREITP--------------------------------------EQ 377
Cdd:cd14145    88 RGGPLNRVLSgkrippDILVNWAvQIARGmnylhCEAIVPvihrdlkssnililekvengdlsnkilkitdfglarewHR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTpELQNPEKLSAIFRDFL 457
Cdd:cd14145   168 TTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKL-SLPIPSTCPEPFARLM 246
                         250
                  ....*....|....*...
gi 1774959464 458 NRCLEMDVEKRGSAKELL 475
Cdd:cd14145   247 EDCWNPDPHSRPPFTNIL 264
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
275-480 4.69e-10

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: 60.04  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd14075     9 ELGSGNFSQVKLGIHQLTKEKVAIKILDKTKldQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 -TDVVTETCMDE-------GQIAA----------VCREITPE-------------------QSKRSTMV----GTPYWMA 391
Cdd:cd14075    89 yTKISTEGKLSEseakplfAQIVSavkhmhenniIHRDLKAEnvfyasnncvkvgdfgfstHAKRGETLntfcGSPPYAA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 392 PEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSAIFRDFLNRCLEM 463
Cdd:cd14075   169 PELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFraetvakLKKCILEGTYTI----------PSYVSEPCQELIRGILQP 238
                         250
                  ....*....|....*..
gi 1774959464 464 DVEKRGSAKELLQHQFL 480
Cdd:cd14075   239 VPSDRYSIDEIKNSEWL 255
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
276-427 5.03e-10

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: 61.17  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDS-YLVGDELWVVMEYLAGGS 351
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKkdvVIQDDDVECTMVEKRVLALQDKPPFLTQLHScFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LT------------------------------------DVVTETCM--DEGQIA----AVCREITPEQSKRSTMVGTPYW 389
Cdd:cd05615    98 LMyhiqqvgkfkepqavfyaaeisvglfflhkkgiiyrDLKLDNVMldSEGHIKiadfGMCKEHMVEGVTTRTFCGTPDY 177
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1774959464 390 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 427
Cdd:cd05615   178 IAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGED 215
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
276-483 5.41e-10

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: 60.22  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDEL-------WVVMEYL 347
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKlSGHPNIVQFCSAASIGKEEsdqgqaeYLLLTEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVT------------------ETCM-------------------------DEGQI------AAVCREITPEQS 378
Cdd:cd14036    88 CKGQLVDFVKkveapgpfspdtvlkifyQTCRavqhmhkqsppiihrdlkienlligNQGQIklcdfgSATTEAHYPDYS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 379 ----KRS------TMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALyliatNGTPELQN 445
Cdd:cd14036   168 wsaqKRSlvedeiTRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRII-----NAKYTIPP 242
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1774959464 446 PEKLSAIFRDFLNRCLEMDVEKRGSAKELLqHQFLKIA 483
Cdd:cd14036   243 NDTQYTVFHDLIRSTLKVNPEERLSITEIV-EQLQELA 279
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
270-477 5.53e-10

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: 60.00  E-value: 5.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELII---NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVV-TETCMDEGQ--------IAAV----------------------------------CREITPEQSKR--- 380
Cdd:cd14162    82 AENGDLLDYIrKNGALPEPQarrwfrqlVAGVeychskgvvhrdlkcenllldknnnlkitdfgfaRGVMKTKDGKPkls 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMIEGEPPYLNENpLRALyLIATNGTPELQNPEKLSAIFRDFLNR 459
Cdd:cd14162   162 ETYCGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPFDDSN-LKVL-LKQVQRRVVFPKNPTVSEECKDLILR 239
                         250
                  ....*....|....*...
gi 1774959464 460 CLeMDVEKRGSAKELLQH 477
Cdd:cd14162   240 ML-SPVKKRITIEEIKRD 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
270-480 5.62e-10

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: 59.99  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14113     9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTD-VVTETCMDEGQIAAVCREI-----------------TPE-----QSKRSTMV---------------------G 385
Cdd:cd14113    88 GRLLDyVVRWGNLTEEKIRFYLREIlealqylhncriahldlKPEnilvdQSLSKPTIkladfgdavqlnttyyihqllG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRCL 461
Cdd:cd14113   168 SPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNIC---RLDFSFPDDyfkgVSQKAKDFVCFLL 244
                         250
                  ....*....|....*....
gi 1774959464 462 EMDVEKRGSAKELLQHQFL 480
Cdd:cd14113   245 QMDPAKRPSAALCLQEQWL 263
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
269-480 5.71e-10

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: 60.02  E-value: 5.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFE-KIGQGASGTVYTAMDVATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSY---LVGDELWV 342
Cdd:cd14033     1 RFLKFNiEIGRGSFKTVYRGLDTETTVEVAWCELQTRKlsKGERQRFSEEVEMLKGLQHPNIVRFYDSWkstVRGHKCII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 -VMEYLAGGSLT--------------------------------------DVVTETCMDEGQIAAV-CREITPEQSKRST 382
Cdd:cd14033    81 lVTELMTSGTLKtylkrfremklkllqrwsrqilkglhflhsrcppilhrDLKCDNIFITGPTGSVkIGDLGLATLKRAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 ----MVGTPYWMAPEVVTRKaYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTP-----ELQNPEklsaiF 453
Cdd:cd14033   161 faksVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKpdsfyKVKVPE-----L 234
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14033   235 KEIIEGCIRTDKDERFTIQDLLEHRFF 261
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
266-480 5.78e-10

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: 60.12  E-value: 5.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFE-KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSY---LVGDE 339
Cdd:cd14031     7 PGGRFLKFDiELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQqrFKEEAEMLKGLQHPNIVRFYDSWesvLKGKK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWV-VMEYLAGGSLTDVVTE-TCMDEGQIAAVCREI----------TP-------------------------------- 375
Cdd:cd14031    87 CIVlVTELMTSGTLKTYLKRfKVMKPKVLRSWCRQIlkglqflhtrTPpiihrdlkcdnifitgptgsvkigdlglatlm 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 376 EQSKRSTMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRD 455
Cdd:cd14031   167 RTSFAKSVIGTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKE 245
                         250       260
                  ....*....|....*....|....*
gi 1774959464 456 FLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14031   246 IIEGCIRQNKSERLSIKDLLNHAFF 270
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
267-481 6.45e-10

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: 60.74  E-value: 6.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDEL---- 340
Cdd:cd07880    14 PDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYrpFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfh 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 --WVVMEYLaGGSLTDVVTETCMDEGQI-----------------AAVCREITP------------------EQSKRSTM 383
Cdd:cd07880    94 dfYLVMPFM-GTDLGKLMKHEKLSEDRIqflvyqmlkglkyihaaGIIHRDLKPgnlavnedcelkildfglARQTDSEM 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VG---TPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALY-LIATNGTP------ELQNPEKLSAI 452
Cdd:cd07880   173 TGyvvTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMeIMKVTGTPskefvqKLQSEDAKNYV 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1774959464 453 F-------RDF--------------LNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07880   253 KklprfrkKDFrsllpnanplavnvLEKMLVLDAESRITAAEALAHPYFE 302
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
276-480 6.49e-10

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: 59.79  E-value: 6.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGS 351
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfveKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVT-ETCMDEG-------QIAA----------VCREITPEQ----------------SKR------------STMVG 385
Cdd:cd14165    89 LLEFIKlRGALPEDvarkmfhQLSSaikycheldiVHRDLKCENllldkdfnikltdfgfSKRclrdengrivlsKTFCG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd14165   169 SAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSN-VKKMLKIQKEHRVRFPRSKNLTSECKDLIYRLLQPD 247
                         250
                  ....*....|....*.
gi 1774959464 465 VEKRGSAKELLQHQFL 480
Cdd:cd14165   248 VSQRLCIDEVLSHPWL 263
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
384-481 6.62e-10

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: 61.02  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELQNPE--KLSAIFRDFLNRCL 461
Cdd:cd05629   209 VGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPFCSENS-HETYRKIINWRETLYFPDdiHLSVEAEDLIRRLI 287
                          90       100
                  ....*....|....*....|..
gi 1774959464 462 EMDVEK--RGSAKELLQHQFLK 481
Cdd:cd05629   288 TNAENRlgRGGAHEIKSHPFFR 309
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
275-479 6.62e-10

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: 59.98  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRE-NKNPNIVNYLDsyLVGDE----LWVVMEyLA 348
Cdd:cd07831     6 KIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNnLREIQALRRlSPHPNILRLIE--VLFDRktgrLALVFE-LM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVT--ETCMDEGQIAAVC-----------------REITPEQ--------------SKRSTMVGTPY------- 388
Cdd:cd07831    83 DMNLYELIKgrKRPLPEKRVKNYMyqllksldhmhrngifhRDIKPENilikddilkladfgSCRGIYSKPPYteyistr 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WM-APE-VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTP--ELQN------------PEK--- 448
Cdd:cd07831   163 WYrAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIhDVLGTPdaEVLKkfrksrhmnynfPSKkgt 242
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1774959464 449 --------LSAIFRDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07831   243 glrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
276-476 7.87e-10

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: 59.59  E-value: 7.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMdVATGQEVAIKQMNLQ--QQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMncAASKKEFL-TELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTET--------------------CMD----EGQIAAVCREITP--------------------------EQSKRSTM 383
Cdd:cd14066    79 DRLHCHkgspplpwpqrlkiakgiarGLEylheECPPPIIHGDIKSsnilldedfepkltdfglarlippseSVSKTSAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLiatNGTPELQnpEKLSAIFRDFLNRCLEM 463
Cdd:cd14066   159 KGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAV-DENRENASRK---DLVEWVE--SKGKEELEDILDKRLVD 232
                         250
                  ....*....|....
gi 1774959464 464 DVEKR-GSAKELLQ 476
Cdd:cd14066   233 DDGVEeEEVEALLR 246
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
266-475 9.53e-10

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: 59.66  E-value: 9.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVY--TAMDVATGQ---EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd05032     4 PREKITLIRELGQGSFGMVYegLAKGVVKGEpetRVAIKTVNENASMRERIeFLNEASVMKEFNCHHVVRLLGVVSTGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTEtCMDEGQIAAVCREITPEQ-------------------------SKRSTMVG--------- 385
Cdd:cd05032    84 TLVVMELMAKGDLKSYLRS-RRPEAENNPGLGPPTLQKfiqmaaeiadgmaylaakkfvhrdlAARNCMVAedltvkigd 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 ---------TPY------------WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYL---NENPLRalYLIATNgt 440
Cdd:cd05032   163 fgmtrdiyeTDYyrkggkgllpvrWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQglsNEEVLK--FVIDGG-- 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1774959464 441 pELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELL 475
Cdd:cd05032   239 -HLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIV 272
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
74-114 9.75e-10

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 53.98  E-value: 9.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1774959464  74 EISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITK 114
Cdd:cd00132     2 EISTPTDFKHISHVGWDGVGFDGANLPPDLQSLFQTAGISA 42
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
276-481 1.06e-09

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: 59.92  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEILV---MRENK-------NPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVL------KKDVILQDDDVectMTEKRilslarnHPFLTQLYCCFQTPDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSL------------------TDVVTETCM---DEGQIA---------------------AVCREITPEQSKRSTM 383
Cdd:cd05590    77 FVNGGDLmfhiqksrrfdeararfyAAEITSALMflhDKGIIYrdlkldnvlldheghckladfGMCKEGIFNGKTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd05590   157 CGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILND---EVVYPTWLSQDAVDILKAFMTK 233
                         250       260
                  ....*....|....*....|....
gi 1774959464 464 DVEKR------GSAKELLQHQFLK 481
Cdd:cd05590   234 NPTMRlgsltlGGEEAILRHPFFK 257
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
266-476 1.09e-09

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: 58.90  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAmdVATGQEVAIKQMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05039     4 NKKDLKLGELIGKGEFGDVMLG--DYRGQKVAVKCLKDDSTAAQAFL-AEASVMTTLRHPNLVQLLGVVLEGNGLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTD--------VVT---------ETC----------------------MDEGQIAAVCREITPEQSKRSTMVGT 386
Cdd:cd05039    81 YMAKGSLVDylrsrgraVITrkdqlgfalDVCegmeyleskkfvhrdlaarnvlVSEDNVAKVSDFGLAKEASSNQDGGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 -PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNEnPLRALYLIATNGTpELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd05039   161 lPIkWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRI-PLKDVVPHVEKGY-RMEAPEGCPPEVYKVMKNCWEL 238
                         250
                  ....*....|...
gi 1774959464 464 DVEKRGSAKELLQ 476
Cdd:cd05039   239 DPAKRPTFKQLRE 251
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
371-481 1.44e-09

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: 58.94  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 371 REITPEQSKRS-TMVGTPYWMAPEVVTRK--AYGPKVDIWSLGIMAIEMIEGEPPYLNENplralyliATNGTPELQN-- 445
Cdd:cd05583   147 KEFLPGENDRAySFCGTIEYMAPEVVRGGsdGHDKAVDWWSLGVLTYELLTGASPFTVDG--------ERNSQSEISKri 218
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1774959464 446 -------PEKLSAIFRDFLNRCLEMDVEKR-----GSAKELLQHQFLK 481
Cdd:cd05583   219 lkshppiPKTFSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFK 266
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
268-480 1.54e-09

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: 59.24  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYLD-----SYLVGDELW 341
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpFEHQTYCLRTLREIKILLRFKHENIIGILDiqrppTFESFKDVY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEY--------LAGGSLTD--------------------------------VVTETC----MDEGqiaaVCREITPEQ 377
Cdd:cd07849    85 IVQELmetdlyklIKTQHLSNdhiqyflyqilrglkyihsanvlhrdlkpsnlLLNTNCdlkiCDFG----LARIADPEH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTM---VGTPYWMAPEV-VTRKAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLI-ATNGTP---ELQN--- 445
Cdd:cd07849   161 DHTGFLteyVATRWYRAPEImLNSKGYTKAIDIWSVGcILA-EMLSNRPLFPGKDYLHQLNLIlGILGTPsqeDLNCiis 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774959464 446 ----------PEK----LSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07849   240 lkarnyikslPFKpkvpWNKLFPnadpkalDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
276-477 1.71e-09

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: 58.53  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTV----------YTAMDVATGQEVaIKQMNLQQQPKK--------------ELIINEILVMRENKNPNIVNY- 330
Cdd:cd14118     2 IGKGSYGIVklayneedntLYAMKILSKKKL-LKQAGFFRRPPPrrkpgalgkpldplDRVYREIAILKKLDHPNVVKLv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 331 --LDSyLVGDELWVVMEYLAGGSLTDVVTETCMDEGQ---------------------------------------IA-- 367
Cdd:cd14118    81 evLDD-PNEDNLYMVFELVDKGAVMEVPTDNPLSEETarsyfrdivlgieylhyqkiihrdikpsnlllgddghvkIAdf 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 368 AVCREITPEQSKRSTMVGTPYWMAPEVVT--RKAYGPK-VDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQ 444
Cdd:cd14118   160 GVSNEFEGDDALLSSTAGTPAFMAPEALSesRKKFSGKaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTD---PVV 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1774959464 445 NPEK--LSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14118   237 FPDDpvVSEQLKDLILRMLDKNPSERITLPEIKEH 271
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
276-480 1.84e-09

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: 58.17  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14071     8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLkkIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 D-VVTETCMDEGQ--------IAAV----CREI-----------------------------TPEQsKRSTMVGTPYWMA 391
Cdd:cd14071    88 DyLAQHGRMSEKEarkkfwqiLSAVeychKRHIvhrdlkaenllldanmnikiadfgfsnffKPGE-LLKTWCGSPPYAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 392 PEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDVEKRGS 470
Cdd:cd14071   167 PEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPF-DGSTLQTLRDRVLSG--RFRIPFFMSTDCEHLIRRMLVLDPSKRLT 243
                         250
                  ....*....|
gi 1774959464 471 AKELLQHQFL 480
Cdd:cd14071   244 IEQIKKHKWM 253
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
276-427 2.07e-09

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: 58.94  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEILV---MRE-------NKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKIL------KKDVIIQDDDVectMVEkrvlalsGKPPFLTQLHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLT------------------------------------DVVTETCM--DEGQIA----AVCRE-ITPEQSKRsT 382
Cdd:cd05587    78 YVNGGDLMyhiqqvgkfkepvavfyaaeiavglfflhskgiiyrDLKLDNVMldAEGHIKiadfGMCKEgIFGGKTTR-T 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 427
Cdd:cd05587   157 FCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGED 201
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
269-480 2.42e-09

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 58.20  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LA-----------GGSLTDVVTETCMDEGQIAAVC---------REITPEQ---SKRSTM-------------------- 383
Cdd:cd07861    81 LSmdlkkyldslpKGKYMDAELVKSYLYQILQGILfchsrrvlhRDLKPQNlliDNKGVIkladfglarafgipvrvyth 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 -VGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTP---------ELQN------ 445
Cdd:cd07861   161 eVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIfRILGTPtediwpgvtSLPDykntfp 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 446 ---PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07861   241 kwkKGSLRTAVKnldedglDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
274-480 3.27e-09

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: 58.11  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 351
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSi 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTETCMDEGQIAAVCREITP----------------------EQSKRSTMV------------------------- 384
Cdd:cd14173    88 LSHIHRRRHFNELEASVVVQDIASaldflhnkgiahrdlkpenilcEHPNQVSPVkicdfdlgsgiklnsdcspistpel 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 ----GTPYWMAPEVVTR-----KAYGPKVDIWSLGIMAIEMIEGEPPYLNE----------NPLRA----LYLIATNGTP 441
Cdd:cd14173   168 ltpcGSAEYMAPEVVEAfneeaSIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgEACPAcqnmLFESIQEGKY 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1774959464 442 ELqnPEK----LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14173   248 EF--PEKdwahISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
264-479 3.34e-09

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: 58.32  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 264 GDPKKkYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqqQP-KKELIINEILVMRE-NKNPNIVNYLDsyLVGDELW 341
Cdd:cd14132    15 GSQDD-YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL----KPvKKKKIKREIKILQNlRGGPNIVKLLD--VVKDPQS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 ----VVMEYLAG-------GSLTDV-----------VTETCMDEGQIAavcREITP-----EQSKR-------------- 380
Cdd:cd14132    88 ktpsLIFEYVNNtdfktlyPTLTDYdiryymyellkALDYCHSKGIMH---RDVKPhnimiDHEKRklrlidwglaefyh 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 -----STMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATN-GTPELQN------- 445
Cdd:cd14132   165 pgqeyNVRVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQLVKIAKVlGTDDLYAyldkygi 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 446 --PEKLSAIFR------------------------DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd14132   245 elPPRLNDILGrhskkpwerfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHPY 304
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
269-479 3.86e-09

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: 57.83  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQ----PKKELiiNEILVMRENKNPNIVNYLDSYLVGDELWVVM 344
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdegvPSSAL--REICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 345 EYL----------AGGSLTDVVTETCMDE-GQIAAVC-------REITPEQ---SKR---------------------ST 382
Cdd:cd07839    79 EYCdqdlkkyfdsCNGDIDPEIVKSFMFQlLKGLAFChshnvlhRDLKPQNlliNKNgelkladfglarafgipvrcySA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLN----ENPLRALYLIAtnGTPELQN-------PE--- 447
Cdd:cd07839   159 EVVTLWYRPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQLKRIFRLL--GTPTEESwpgvsklPDykp 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 448 ---------------KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07839   237 ypmypattslvnvvpKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
276-481 4.13e-09

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: 57.57  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVehqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 ----------TDVVTETCMDEGQIA--------AVCREITPEQS----------------------KRSTMVGTPYWMAP 392
Cdd:cd14117    94 ykelqkhgrfDEQRTATFMEELADAlhychekkVIHRDIKPENLlmgykgelkiadfgwsvhapslRRRTMCGTLDYLPP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 393 EVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAK 472
Cdd:cd14117   174 EMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIV---KVDLKFPPFLSDGSRDLISKLLRYHPSERLPLK 250

                  ....*....
gi 1774959464 473 ELLQHQFLK 481
Cdd:cd14117   251 GVMEHPWVK 259
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
276-484 4.29e-09

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 58.03  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASG--TVYTAMDVATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 351
Cdd:cd08227     6 IGRGFEDlmTVNLARYKPTGEYVTVRRINLEACTNEmvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTETCMD---EGQIAAVCREITP-----------EQSKRSTMV-----GTPY------------------------ 388
Cdd:cd08227    86 AKDLICTHFMDgmsELAIAYILQGVLKaldyihhmgyvHRSVKASHIlisvdGKVYlsglrsnlsminhgqrlrvvhdfp 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 --------WMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGT------------------ 440
Cdd:cd08227   166 kysvkvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtttipaeeltmk 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 441 ------------------PELQNPEK--------LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAK 484
Cdd:cd08227   245 psrsgansglgesttvstPRPSNGESsshpynrtFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIK 314
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
381-481 8.78e-09

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: 56.97  E-value: 8.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNP---EKLSAI 452
Cdd:cd05597   161 SVAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAES-LVETYGKIMNHKEHFSFPddeDDVSEE 239
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1774959464 453 FRDFLNRcLEMDVEKR---GSAKELLQHQFLK 481
Cdd:cd05597   240 AKDLIRR-LICSRERRlgqNGIDDFKKHPFFE 270
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
384-481 1.11e-08

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: 56.48  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEK--LSAIFRDFLNRCL 461
Cdd:cd05574   193 VGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKK---ELTFPESppVSSEAKDLIRKLL 269
                          90       100
                  ....*....|....*....|....
gi 1774959464 462 EMDVEKR-GS---AKELLQHQFLK 481
Cdd:cd05574   270 VKDPSKRlGSkrgASEIKRHPFFR 293
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
270-478 1.16e-08

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: 56.22  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKI---GQGASGTVYTAMDVATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14046     5 LTDFEELqvlGKGAFGQVVKVRNKLDGRYYAIKKIKLRsESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVVTETCMDEG--------QIAA----------VCREITP-------------------------------- 375
Cdd:cd14046    85 YCEKSTLRDLIDSGLFQDTdrlwrlfrQILEglayihsqgiIHRDLKPvnifldsngnvkigdfglatsnklnvelatqd 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 376 ----------EQSKRSTMVGTPYWMAPEVV--TRKAYGPKVDIWSLGIMAIEMIegEPP---YLNENPLRALYLIATNGT 440
Cdd:cd14046   165 inkstsaalgSSGDLTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMC--YPFstgMERVQILTALRSVSIEFP 242
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1774959464 441 PELQNPEKLSAifRDFLNRCLEMDVEKRGSAKELLQHQ 478
Cdd:cd14046   243 PDFDDNKHSKQ--AKLIRWLLNHDPAKRPSAQELLKSE 278
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
266-496 1.19e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 57.35  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEliinEILVMRENKNPNIVnYLDSYLVGDE------ 339
Cdd:PTZ00036   64 PNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNR----ELLIMKNLNHINII-FLKDYYYTECfkknek 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 ---LWVVMEYLA-------------GGSLTDVVT-----ETCMDEGQIAA--VC-REITPEQ----------------SK 379
Cdd:PTZ00036  139 nifLNVVMEFIPqtvhkymkhyarnNHALPLFLVklysyQLCRALAYIHSkfIChRDLKPQNllidpnthtlklcdfgSA 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 380 RSTMVG--------TPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALY-LIATNGTP-----ELQ 444
Cdd:PTZ00036  219 KNLLAGqrsvsyicSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVrIIQVLGTPtedqlKEM 298
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1774959464 445 NPEKLSAIFRDFLNRCLEmDVEKRGSAKELLQ--HQFLKIaKPLSSLTPLIAAA 496
Cdd:PTZ00036  299 NPNYADIKFPDVKPKDLK-KVFPKGTPDDAINfiSQFLKY-EPLKRLNPIEALA 350
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
382-481 1.29e-08

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: 56.98  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA-LYLIATNGTPELQNPEKLSAIFRDF---L 457
Cdd:cd05625   207 SLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLiikL 286
                          90       100
                  ....*....|....*....|....
gi 1774959464 458 NRCLEMDVEKRGsAKELLQHQFLK 481
Cdd:cd05625   287 CRGPEDRLGKNG-ADEIKAHPFFK 309
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
274-428 1.37e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 57.11  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEILVMR---ENKN------PNIVNYLDsylVGDE---LW 341
Cdd:NF033483   13 ERIGRGGMAEVYLAKDTRLDRDVAVKVL------RPDLARDPEFVARfrrEAQSaaslshPNIVSVYD---VGEDggiPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVTE-------TCMD-EGQIAA----------VCREITPE--------------------------- 376
Cdd:NF033483   84 IVMEYVDGRTLKDYIREhgplspeEAVEiMIQILSalehahrngiVHRDIKPQnilitkdgrvkvtdfgiaralssttmt 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 377 QSkrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP 428
Cdd:NF033483  164 QT--NSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSP 213
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
363-459 1.67e-08

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: 56.25  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 363 EGQIA----AVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI--A 436
Cdd:cd05582   133 DGHIKltdfGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIlkA 212
                          90       100
                  ....*....|....*....|....*..
gi 1774959464 437 TNGTPELQNPEK---LSAIF-RDFLNR 459
Cdd:cd05582   213 KLGMPQFLSPEAqslLRALFkRNPANR 239
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
385-480 1.99e-08

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 55.24  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM-------IEGEPPYLNENPLRALYLiatngtpeLQNPEKlsaifRDFL 457
Cdd:cd13984   166 RNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMaaleiqsNGEKVSANEEAIIRAIFS--------LEDPLQ-----KDFI 232
                          90       100
                  ....*....|....*....|...
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd13984   233 RKCLSVAPQDRPSARDLLFHPVL 255
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
247-481 2.31e-08

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: 55.44  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 247 KMSDEeiLEKLRSIVSVGDPKKKYTRFE-KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENK 323
Cdd:cd14030     5 KQQDE--IEELETKAVG*SPDGRFLKFDiEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERqrFKEEAGMLKGLQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 324 NPNIVNYLDSY---LVGDELWV-VMEYLAGGSLTDVVTE-TCMDEGQIAAVCREIT------------------------ 374
Cdd:cd14030    83 HPNIVRFYDSWestVKGKKCIVlVTELMTSGTLKTYLKRfKVMKIKVLRSWCRQILkglqflhtrtppiihrdlkcdnif 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 ---PEQS-----------KRST----MVGTPYWMAPEVVTRKaYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA 436
Cdd:cd14030   163 itgPTGSvkigdlglatlKRASfaksVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRV 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 437 TNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd14030   242 TSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQ 286
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
275-474 2.74e-08

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 54.82  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILvmrenKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 354
Cdd:cd13991    13 RIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGL-----TSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 355 VVTET-CMDE-------------------------------------GQIAAVC-----REITPEQSKRSTMV-----GT 386
Cdd:cd13991    88 LIKEQgCLPEdralhylgqalegleylhsrkilhgdvkadnvllssdGSDAFLCdfghaECLDPDGLGKSLFTgdyipGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVE 466
Cdd:cd13991   168 ETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPLREIPPSCAPLTAQAIQAGLRKEPV 247

                  ....*...
gi 1774959464 467 KRGSAKEL 474
Cdd:cd13991   248 HRASAAEL 255
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
373-481 3.08e-08

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 55.31  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 ITPEQSKRSTMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNE---NPLRALYLIATNGTPELqnPEK 448
Cdd:cd05614   156 LTEEKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEgekNTQSEVSRRILKCDPPF--PSF 233
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKR-GS----AKELLQHQFLK 481
Cdd:cd05614   234 IGPVARDLLQKLLCKDPKKRlGAgpqgAQEIKEHPFFK 271
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
269-477 3.35e-08

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: 54.97  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTV----------YTAMDVATGQEVaIKQMNLQQQPKK-----------------ELIINEILVMRE 321
Cdd:cd14199     3 QYKLKDEIGKGSYGVVklayneddntYYAMKVLSKKKL-MRQAGFPRRPPPrgaraapegctqprgpiERVYQEIAILKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 322 NKNPNIVNYLDSY--LVGDELWVVMEYLAGGSLTDVVTETCMDEGQI-----------------AAVCREITPEQ----- 377
Cdd:cd14199    82 LDHPNVVKLVEVLddPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQArfyfqdlikgieylhyqKIIHRDVKPSNllvge 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 -------------------SKRSTMVGTPYWMAPEVV--TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNEnplRALYLI 435
Cdd:cd14199   162 dghikiadfgvsnefegsdALLTNTVGTPAFMAPETLseTRKIFsGKALDVWAMGVTLYCFVFGQCPFMDE---RILSLH 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 436 ATNGTPELQNPEK--LSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14199   239 SKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVPEIKLH 282
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
276-481 3.48e-08

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: 54.75  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINE----ILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNErimlSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTE-TCMDEGQI---AA--------------VCREITP--------------------EQSKR--STMVGTPY 388
Cdd:cd05606    82 GGDLHYHLSQhGVFSEAEMrfyAAevilglehmhnrfiVYRDLKPanilldehghvrisdlglacDFSKKkpHASVGTHG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd05606   162 YMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSK 241
                         250
                  ....*....|....*....
gi 1774959464 468 R-----GSAKELLQHQFLK 481
Cdd:cd05606   242 RlgclgRGATEVKEHPFFK 260
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
269-480 3.87e-08

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: 55.09  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 343
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKiirnKKRFHHQALVEVKILDALRRKDRDNShNVIHMKEYFYFRNHLCIT 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEyLAGGSLTDVVTETCMDEGQIAAVCR--------------------EITPEQ---SKRS------------------- 381
Cdd:cd14225   124 FE-LLGMNLYELIKKNNFQGFSLSLIRRfaisllqclrllyreriihcDLKPENillRQRGqssikvidfgsscyehqrv 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 -TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA------------------------ 436
Cdd:cd14225   203 yTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMevlglpppelienaqrrrlffdsk 282
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464 437 ------TN--------GTPELQNPEKLS-AIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14225   283 gnprciTNskgkkrrpNSKDLASALKTSdPLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
286-481 4.23e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 55.41  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 286 TAMDVAT-----GQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT------- 353
Cdd:PTZ00267   81 TAAFVATrgsdpKEKVVAKFVMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNkqikqrl 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 ----------------------DVVTETCMDEGQIAAVCREITPEQ---------SKR----------STMVGTPYWMAP 392
Cdd:PTZ00267  161 kehlpfqeyevgllfyqivlalDEVHSRKMMHRDLKSANIFLMPTGiiklgdfgfSKQysdsvsldvaSSFCGTPYYLAP 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 393 EVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-YLIATNGTPelqNPEKLSAIFRDFLNRCLEMDVEKRGSA 471
Cdd:PTZ00267  241 ELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMqQVLYGKYDP---FPCPVSSGMKALLDPLLSKNPALRPTT 317
                         250
                  ....*....|
gi 1774959464 472 KELLQHQFLK 481
Cdd:PTZ00267  318 QQLLHTEFLK 327
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
269-481 5.03e-08

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: 54.48  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGA-DQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVTETC--MDEGQIAAVCRE-----------------ITPE----QSKRSTMVG-------------------- 385
Cdd:cd14104    80 GVDIFERITTARfeLNEREIVSYVRQvcealeflhsknighfdIRPEniiyCTRRGSYIKiiefgqsrqlkpgdkfrlqy 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 -TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAT-NGTPELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd14104   160 tSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNaEYAFDDEAFKNISIEALDFVDRLLVK 239
                         250
                  ....*....|....*...
gi 1774959464 464 DVEKRGSAKELLQHQFLK 481
Cdd:cd14104   240 ERKSRMTAQEALNHPWLK 257
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
276-475 5.20e-08

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 53.96  E-value: 5.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVY--TAMDV---ATG-QEVAIKqmNLQQ----QPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05044     3 LGSGAFGEVFegTAKDIlgdGSGeTKVAVK--TLRKgatdQEKAEFL-KEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGG-------------------SLTDVVtETCMDEGQ--------------IAAV-CREITPEQSKRSTMVG------ 385
Cdd:cd05044    80 LMEGGdllsylraarptaftppllTLKDLL-SICVDVAKgcvyledmhfvhrdLAARnCLVSSKDYRERVVKIGdfglar 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 ----TPY------------WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPYLNENPLRALYLIATNGtpELQNPEK 448
Cdd:cd05044   159 diykNDYyrkegegllpvrWMAPESLVDGVFTTQSDVWAFGVLMWEiLTLGQQPYPARNNLEVLHFVRAGG--RLDQPDN 236
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 449 LSAIFRDFLNRCLEMDVEKRGSAKELL 475
Cdd:cd05044   237 CPDDLYELMLRCWSTDPEERPSFARIL 263
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
372-481 6.52e-08

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 53.90  E-value: 6.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 372 EITPEQSKRSTmVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENPLRALYLIATNGTPELQNpEKL 449
Cdd:cd05605   151 EIPEGETIRGR-VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFraRKEKVKREEVDRRVKEDQEEYS-EKF 228
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1774959464 450 SAIFRDFLNRCLEMDVEKR-----GSAKELLQHQFLK 481
Cdd:cd05605   229 SEEAKSICSQLLQKDPKTRlgcrgEGAEDVKSHPFFK 265
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
293-472 6.90e-08

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: 53.93  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 293 GQEVAIKQMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV--VTETCMDEG-QIAAV 369
Cdd:cd13992    25 GRTVAIKHITFSRTEKRT-ILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVllNREIKMDWMfKSSFI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 370 ----------------------------------------CREITPEQSKRSTMVGTPY----WMAPEVVTRKAYG---- 401
Cdd:cd13992   104 kdivkgmnylhsssigyhgrlkssnclvdsrwvvkltdfgLRNLLEEQTNHQLDEDAQHkkllWTAPELLRGSLLEvrgt 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 402 PKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT----PEL-----QNPEKLSAIFRDflnrCLEMDVEKRGSAK 472
Cdd:cd13992   184 QKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNkpfrPELavlldEFPPRLVLLVKQ----CWAENPEKRPSFK 259
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
269-480 7.57e-08

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: 53.81  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI--INEILVMR---ENKNPNIVNYLD---SYLVGDEL 340
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLstVREVALLKrleAFDHPNIVRLMDvcaTSRTDRET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVM----------EYLAGGSLTDVVTETCMDEGQ--------IAAVC---REITPE----------------------- 376
Cdd:cd07863    81 KVTLvfehvdqdlrTYLDKVPPPGLPAETIKDLMRqflrgldfLHANCivhRDLKPEnilvtsggqvkladfglariysc 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEP--------------------PYLNENPlRALYLIA 436
Cdd:cd07863   161 QMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPlfcgnseadqlgkifdliglPPEDDWP-RDVTLPR 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 437 TNGTPELQNP-----EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07863   240 GAFSPRGPRPvqsvvPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
270-423 7.64e-08

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: 53.87  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVV---TETCMDEGQI----AAVC-------------REITPEQ--------------------SKRSTM--- 383
Cdd:cd05630    82 MNGGDLKFHIyhmGQAGFPEARAvfyaAEICcgledlhrerivyRDLKPENillddhghirisdlglavhvPEGQTIkgr 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd05630   162 VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPF 201
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
269-481 8.75e-08

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: 54.02  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGD-----ELW 341
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdvFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSrrefkDIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYL---------AGGSLT-------------------------------------DVVTETCmDEGqIAAVCREITP 375
Cdd:cd07859    81 VVFELMesdlhqvikANDDLTpehhqfflyqllralkyihtanvfhrdlkpknilanaDCKLKIC-DFG-LARVAFNDTP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 376 EQSKRSTMVGTPYWMAPEVVTR--KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTN--GTP---------- 441
Cdd:cd07859   159 TAIFWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLI-TDllGTPspetisrvrn 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 442 ----------ELQNPEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07859   238 ekarrylssmRKKQPVPFSQKFPnadplalRLLERLLAFDPKDRPTAEEALADPYFK 294
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
276-476 9.41e-08

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: 54.24  E-value: 9.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEliinEILVMRENKNPnIVN----YLDS--YLVGDE--LWVVMEYL 347
Cdd:cd05624    80 IGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRA----ETACFREERNV-LVNgdcqWITTlhYAFQDEnyLYLVMDYY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVT--ETCMDEG-----------------QIAAVCREITPEQ-------------------------SKRSTM 383
Cdd:cd05624   155 VGGDLLTLLSkfEDKLPEDmarfyigemvlaihsihQLHYVHRDIKPDNvlldmnghirladfgsclkmnddgtVQSSVA 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNPEKLSaifrdfln 458
Cdd:cd05624   235 VGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAES-LVETYGKIMNHEERFQFPSHVT-------- 305
                         250
                  ....*....|....*...
gi 1774959464 459 rclemDVEKrgSAKELLQ 476
Cdd:cd05624   306 -----DVSE--EAKDLIQ 316
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
270-484 9.55e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 53.90  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd06649     7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDV------VTETCMDEGQIAAV-------------CREITPEQ----------------------SKRSTMVGTP 387
Cdd:cd06649    87 GGSLDQVlkeakrIPEEILGKVSIAVLrglaylrekhqimHRDVKPSNilvnsrgeiklcdfgvsgqlidSMANSFVGTR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMI--------------------------EGEPPYLNENP------------- 428
Cdd:cd06649   167 SYMSPERLQGTHYSVQSDIWSMGLSLVELAigrypipppdakeleaifgrpvvdgeEGEPHSISPRPrppgrpvsghgmd 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 429 -------LRALYLIATNGTPELQNpEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAK 484
Cdd:cd06649   247 srpamaiFELLDYIVNEPPPKLPN-GVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKRSE 308
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
276-476 1.00e-07

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: 53.17  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATgqeVAIKQMNLQQQPKKELII--NEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSLT 353
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAfkNEVAVLRKTRHVNILLFM-GYMTKPQLAIVTQWCEGSSLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 D--VVTETCMDEGQIAAVCREIT---------------------------------------------PEQSKRSTmvGT 386
Cdd:cd14062    77 KhlHVLETKFEMLQLIDIARQTAqgmdylhakniihrdlksnniflhedltvkigdfglatvktrwsgSQQFEQPT--GS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQN-----PEKLSAIFRDf 456
Cdd:cd14062   155 ILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGylRPDLSKvrsdtPKALRRLMED- 233
                         250       260
                  ....*....|....*....|
gi 1774959464 457 lnrCLEMDVEKRGSAKELLQ 476
Cdd:cd14062   234 ---CIKFQRDERPLFPQILA 250
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
375-480 1.19e-07

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: 53.59  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 375 PEQSKRSTM-VGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIaTN--GTPELQN----- 445
Cdd:cd07853   155 PDESKHMTQeVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLI-TDllGTPSLEAmrsac 233
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1774959464 446 -------------PEKLSAIFR----------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07853   234 egarahilrgphkPPSLPVLYTlssqatheavHLLCRMLVFDPDKRISAADALAHPYL 291
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
268-477 1.33e-07

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: 52.68  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVytAMDVATGQEVAIKqmNLQQQPKKELIINEILVMRENKNPNIVNYLdSYLVGDE--LWVVME 345
Cdd:cd05082     6 KELKLLQTIGKGEFGDV--MLGDYRGNKVAVK--CIKNDATAQAFLAEASVMTQLRHSNLVQLL-GVIVEEKggLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTD--------VVTETCM-------------------------------DEGQIAAVCR-EITPEQSKRSTMVG 385
Cdd:cd05082    81 YMAKGSLVDylrsrgrsVLGGDCLlkfsldvceameylegnnfvhrdlaarnvlvSEDNVAKVSDfGLTKEASSTQDTGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYlNENPLRALYLIATNGTpELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd05082   161 LPVkWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY-PRIPLKDVVPRVEKGY-KMDAPDGCPPAVYDVMKNCWHL 238
                         250
                  ....*....|....*..
gi 1774959464 464 DVEKRGS---AKELLQH 477
Cdd:cd05082   239 DAAMRPSflqLREQLEH 255
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
237-468 1.45e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 53.45  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 237 RNTEKQKKKPKMSDEEILEKlrsivsvgdPKKKYTRFEKI---GQGASGTVYTAM-DVATGQEVAIKQM---NLQQQPKK 309
Cdd:PTZ00426    5 KNLQLHKKKDSDSTKEPKRK---------NKMKYEDFNFIrtlGTGSFGRVILATyKNEDFPPVAIKRFeksKIIKQKQV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 310 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTET--------CMDEGQIA----------AVCR 371
Cdd:PTZ00426   76 DHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNkrfpndvgCFYAAQIVlifeylqslnIVYR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 372 EITPE---------------------QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLr 430
Cdd:PTZ00426  156 DLKPEnllldkdgfikmtdfgfakvvDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPL- 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1774959464 431 ALYLIATNGTpeLQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:PTZ00426  235 LIYQKILEGI--IYFPKFLDNNCKHLMKKLLSHDLTKR 270
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
265-479 1.51e-07

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: 53.14  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 265 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnLQQQPKKELIIN---EILVMRENKNPNIVNYL---------- 331
Cdd:cd07865     9 DEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKV-LMENEKEGFPITalrEIKILQLLKHENVVNLIeicrtkatpy 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 332 -----DSYLVGD--------------------ELWVVMEYLAGG---------------SLTDVVTETCM----DEGQIA 367
Cdd:cd07865    88 nrykgSIYLVFEfcehdlagllsnknvkftlsEIKKVMKMLLNGlyyihrnkilhrdmkAANILITKDGVlklaDFGLAR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 368 AVCREITPEQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLG-IMAiEMIEGEPPYLNENPLRALYLIAT---NGTPE 442
Cdd:cd07865   168 AFSLAKNSQPNRYTNRVVTLWYRPPELLLgERDYGPPIDMWGAGcIMA-EMWTRSPIMQGNTEQHQLTLISQlcgSITPE 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 443 L----------------QN-----PEKLSAIFR-----DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07865   247 VwpgvdklelfkkmelpQGqkrkvKERLKPYVKdpyalDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
269-480 1.55e-07

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: 52.77  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFE-KIGQGASGTVYTAMDVATGQEVAI------KQMNLQQQPKKEliinEILVMRENKNPNIVNYLDSYLVGDE-- 339
Cdd:cd14032     1 RFLKFDiELGRGSFKTVYKGLDTETWVEVAWcelqdrKLTKVERQRFKE----EAEMLKGLQHPNIVRFYDFWESCAKgk 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 --LWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCREI----------TPEQSKR-------------------------- 380
Cdd:cd14032    77 rcIVLVTELMTSGTLKTYLKRfKVMKPKVLRSWCRQIlkgllflhtrTPPIIHRdlkcdnifitgptgsvkigdlglatl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 ------STMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTP-----ELQNPEkl 449
Cdd:cd14032   157 krasfaKSVIGTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKpasfeKVTDPE-- 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1774959464 450 saiFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14032   234 ---IKEIIGECICKNKEERYEIKDLLSHAFF 261
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
267-423 1.76e-07

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: 53.05  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd05632     1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesMALNEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVV-----------------TETCM---DEGQIAAVCREITPE------------------------QSK 379
Cdd:cd05632    81 LTIMNGGDLKFHIynmgnpgfeeeralfyaAEILCgleDLHRENTVYRDLKPEnillddyghirisdlglavkipegESI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 380 RSTmVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd05632   161 RGR-VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPF 203
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
269-484 1.85e-07

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: 52.42  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKI---GQGASGTVYTAMDVATGQ----EVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLvGDEL 340
Cdd:cd05057     5 KETELEKGkvlGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREETGPKaNEEILDEAYVMASVDHPHLVRLLGICL-SSQV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 341 WVVMEYLAGGSLTDVVTE--TCMDEGQIAAVCREITPEQS-------------KRSTMVGTP------------------ 387
Cdd:cd05057    84 QLITQLMPLGCLLDYVRNhrDNIGSQLLLNWCVQIAKGMSyleekrlvhrdlaARNVLVKTPnhvkitdfglaklldvde 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 ------------YWMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPYLNEnPLRALYLIATNGTpELQNPEKLSAIFR 454
Cdd:cd05057   164 keyhaeggkvpiKWMALESIQYRIYTHKSDVWSYGVTVWElMTFGAKPYEGI-PAVEIPDLLEKGE-RLPQPPICTIDVY 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELLQhQFLKIAK 484
Cdd:cd05057   242 MVLVKCWMIDAESRPTFKELAN-EFSKMAR 270
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
276-435 2.16e-07

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: 52.31  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY------- 346
Cdd:cd07848     9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYveknmle 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 ----LAGGSLTDVVTETCMDEGQIAAVC-------REITPEQ-------------------------SKRSTMVGTPYWM 390
Cdd:cd07848    89 lleeMPNGVPPEKVRSYIYQLIKAIHWChkndivhRDIKPENllishndvlklcdfgfarnlsegsnANYTEYVATRWYR 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 391 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI 435
Cdd:cd07848   169 SPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTI 213
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
271-475 3.82e-07

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 51.49  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 271 TRFEKIGQGASGTVYTAMDVATgQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd05112     7 TFVQEIGSGQFGLVHLGYWLNK-DKVAIKTIR-EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTD------------VVTETCMD--------------------------EGQIAAVC-----REITPEQSKRSTMVGTP 387
Cdd:cd05112    85 CLSDylrtqrglfsaeTLLGMCLDvcegmayleeasvihrdlaarnclvgENQVVKVSdfgmtRFVLDDQYTSSTGTKFP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 Y-WMAPEVVTRKAYGPKVDIWSLGIMAIEMI-EGEPPYlnENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDV 465
Cdd:cd05112   165 VkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFsEGKIPY--ENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERP 242
                         250
                  ....*....|
gi 1774959464 466 EKRGSAKELL 475
Cdd:cd05112   243 EDRPSFSLLL 252
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
269-484 4.85e-07

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: 51.56  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKI---GQGASGTVYTAMDVATGQE----VAIKQMNLQQQPK--KElIINEILVMRENKNPNIVNYLDSYLVgDE 339
Cdd:cd05108     5 KETEFKKIkvlGSGAFGTVYKGLWIPEGEKvkipVAIKELREATSPKanKE-ILDEAYVMASVDNPHVCRLLGICLT-ST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTETCMDEG---------QIAAVC------REITPEQSKRSTMVGTPY---------------- 388
Cdd:cd05108    83 VQLITQLMPFGCLLDYVREHKDNIGsqyllnwcvQIAKGMnyledrRLVHRDLAARNVLVKTPQhvkitdfglakllgae 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 --------------WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPYlNENPLRALYLIATNGTpELQNPEKLSAIF 453
Cdd:cd05108   163 ekeyhaeggkvpikWMALESILHRIYTHQSDVWSYGVTVWElMTFGSKPY-DGIPASEISSILEKGE-RLPQPPICTIDV 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1774959464 454 RDFLNRCLEMDVEKRGSAKELLQhQFLKIAK 484
Cdd:cd05108   241 YMIMVKCWMIDADSRPKFRELII-EFSKMAR 270
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
368-428 5.62e-07

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 51.56  E-value: 5.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 368 AVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENP 428
Cdd:cd05617   161 GMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiITDNP 223
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
276-426 6.06e-07

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: 51.61  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd05596    34 IGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSdsaFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDV-----VTET-----CMDE-------GQIAAVCREITPE-------------------------QSKRSTMVGTPYWM 390
Cdd:cd05596   114 VNLmsnydVPEKwarfyTAEVvlaldaiHSMGFVHRDVKPDnmlldasghlkladfgtcmkmdkdgLVRSDTAVGTPDYI 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1774959464 391 APEVVTRKA----YGPKVDIWSLGIMAIEMIEGEPPYLNE 426
Cdd:cd05596   194 SPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYAD 233
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
270-423 6.49e-07

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: 51.15  E-value: 6.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLT--------------------------------------DVVTETCM--DEGQIA----AVCREItPEQSKRST 382
Cdd:cd05631    82 MNGGDLKfhiynmgnpgfdeqraifyaaelccgledlqrerivyrDLKPENILldDRGHIRisdlGLAVQI-PEGETVRG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd05631   161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
276-481 6.69e-07

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: 51.22  E-value: 6.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSL-------------------TDVV------------------TETCMDE---GQIAAVCREITPEQSKRSTMVGTPYW 389
Cdd:cd05633    93 GDLhyhlsqhgvfsekemrfyaTEIIlglehmhnrfvvyrdlkpANILLDEhghVRISDLGLACDFSKKKPHASVGTHGY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd05633   173 MAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVSKR 252
                         250
                  ....*....|....*...
gi 1774959464 469 -----GSAKELLQHQFLK 481
Cdd:cd05633   253 lgchgRGAQEVKEHSFFK 270
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
276-480 6.86e-07

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: 50.76  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQmnLQQQPKKELIINeiLVMRENKNPNIVNYLDSYLVGDE----LWVVMEYLAGGS 351
Cdd:cd14172    12 LGLGVNGKVLECFHRRTGQKCALKL--LYDSPKARREVE--HHWRASGGPHIVHILDVYENMHHgkrcLLIIMECMEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVVTE---TCMDEGQIAAVCREI-----------------TPEQ----SKRSTMV----------------------G 385
Cdd:cd14172    88 LFSRIQErgdQAFTEREASEIMRDIgtaiqylhsmniahrdvKPENllytSKEKDAVlkltdfgfakettvqnalqtpcY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNeNPLRALYLIATN----GTPELQNPE--KLSAIFRDFLNR 459
Cdd:cd14172   168 TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYS-NTGQAISPGMKRrirmGQYGFPNPEwaEVSEEAKQLIRH 246
                         250       260
                  ....*....|....*....|.
gi 1774959464 460 CLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14172   247 LLKTDPTERMTITQFMNHPWI 267
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
268-481 6.91e-07

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: 51.02  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQM--NLQQQPKKELIINEILVMRE-NKNPNIV---------NYLDSYL 335
Cdd:cd07852     7 RRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdAFRNATDAQRTFREIMFLQElNDHPNIIkllnviraeNDKDIYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 336 VGD-------------------------ELWVVMEYLAGGSL-------------TDVVTETCmDEGqiaaVCREITPEQ 377
Cdd:cd07852    87 VFEymetdlhaviraniledihkqyimyQLLKALKYLHSGGVihrdlkpsnillnSDCRVKLA-DFG----LARSLSQLE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 SKRSTMVGTPY----WM-APEV-VTRKAYGPKVDIWSLG-IMAiEMIEGEPPY-----LNE---------NP-------L 429
Cdd:cd07852   162 EDDENPVLTDYvatrWYrAPEIlLGSTRYTKGVDMWSVGcILG-EMLLGKPLFpgtstLNQlekiievigRPsaediesI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464 430 RALY-------LIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07852   241 QSPFaatmlesLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
267-455 7.08e-07

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: 51.55  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKEliinEILVMRENKNPnIVNYlDS-------YLVGDE 339
Cdd:cd05623    71 KEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRA----ETACFREERDV-LVNG-DSqwittlhYAFQDD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 --LWVVMEYLAGGSLTDVVT--ETCMDEG-----------------QIAAVCREITPEQ--------------------- 377
Cdd:cd05623   145 nnLYLVMDYYVGGDLLTLLSkfEDRLPEDmarfylaemvlaidsvhQLHYVHRDIKPDNilmdmnghirladfgsclklm 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 ----SKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIATNGTPELQNPEK 448
Cdd:cd05623   225 edgtVQSSVAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAES-LVETYGKIMNHKERFQFPTQ 303

                  ....*..
gi 1774959464 449 LSAIFRD 455
Cdd:cd05623   304 VTDVSEN 310
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
274-354 8.00e-07

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: 50.74  E-value: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGD-----ELWVVMEYL 347
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRlSGHKNIVGYIDSSANRSgngvyEVLLLMEYC 88

                  ....*..
gi 1774959464 348 AGGSLTD 354
Cdd:cd14037    89 KGGGVID 95
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
382-481 8.17e-07

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: 51.21  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELQNPEK--LSAIFRDFLNR 459
Cdd:cd05627   196 STVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETP-QETYRKVMNWKETLVFPPEvpISEKAKDLILR 274
                          90       100
                  ....*....|....*....|....*.
gi 1774959464 460 -CLemDVEKR---GSAKELLQHQFLK 481
Cdd:cd05627   275 fCT--DAENRigsNGVEEIKSHPFFE 298
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
382-475 8.88e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 51.41  E-value: 8.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCL 461
Cdd:PTZ00283  204 TFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPL--PPSISPEMQEIVTALL 281
                          90
                  ....*....|....
gi 1774959464 462 EMDVEKRGSAKELL 475
Cdd:PTZ00283  282 SSDPKRRPSSSKLL 295
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
268-425 9.43e-07

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: 50.67  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK-----ELIINEILVMRENknPNIVNYLDSYLVGDELWV 342
Cdd:cd05607     2 KYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKsgekmALLEKEILEKVNS--PFIVSLAYAFETKTHLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEYLAGGSL--------------------TDVVTETCMDEGQIAAVCREITPE----------------------QSKR 380
Cdd:cd05607    80 VMSLMNGGDLkyhiynvgergiemervifySAQITCGILHLHSLKIVYRDMKPEnvllddngncrlsdlglavevkEGKP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464 381 STM-VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN 425
Cdd:cd05607   160 ITQrAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
269-425 9.67e-07

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: 50.45  E-value: 9.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEK-IGQGASGTVYTAMDVATGQE---VAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVV 343
Cdd:cd05033     4 SYVTIEKvIGGGEFGEVCSGSLKLPGKKeidVAIKTLKSGYSDKQRLdFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDVVTETcmdEGQ------------IAA--------------------------VC--------REITPEQ 377
Cdd:cd05033    84 TEYMENGSLDKFLREN---DGKftvtqlvgmlrgIASgmkylsemnyvhrdlaarnilvnsdlVCkvsdfglsRRLEDSE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1774959464 378 SKRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPYLN 425
Cdd:cd05033   161 ATYTTKGGkIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPYWD 211
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
270-423 1.02e-06

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: 50.24  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGAsgtvYTAMDVATGQE----VAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSY-LVGDELW 341
Cdd:cd14164     2 YTLGTTIGEGS----FSKVKLATSQKycckVAIKIVDRRRASPdfvQKFLPRELSILRRVNHPNIVQMFECIeVANGRLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDV--VTETCMDEG-----QIAAV---------------CREI--TPEQSK------------------ 379
Cdd:cd14164    78 IVMEAAATDLLQKIqeVHHIPKDLArdmfaQMVGAvnylhdmnivhrdlkCENIllSADDRKikiadfgfarfvedypel 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1774959464 380 RSTMVGTPYWMAPEVVTRKAYGPK-VDIWSLGIMAIEMIEGEPPY 423
Cdd:cd14164   158 STTFCGSRAYTPPEVILGTPYDPKkYDVWSLGVVLYVMVTGTMPF 202
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
266-428 1.20e-06

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: 49.82  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd14111     1 PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAE-EKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGS-LTDVVTETCMDEGQIAAV-------------CR----EITPEQ-------------------------SKRST 382
Cdd:cd14111    80 FCSGKElLHSLIDRFRYSEDDVVGYlvqilqgleylhgRRvlhlDIKPDNimvtnlnaikivdfgsaqsfnplslRQLGR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP 428
Cdd:cd14111   160 RTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDP 205
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
322-475 1.32e-06

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 50.78  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 322 NKNPnIVNYLDsyLVGDELWVV--MEYLAGGSLT--DVVTETCMD-EGQIAAVC-----REITPEQ---SKRSTMVGTPy 388
Cdd:cd05107   231 NESP-ALSYMD--LVGFSYQVAngMEFLASKNCVhrDLAARNVLIcEGKLVKICdfglaRDIMRDSnyiSKGSTFLPLK- 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYlNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEK 467
Cdd:cd05107   307 WMAPESIFNNLYTTLSDVWSFGILLWEIFTlGGTPY-PELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEI 385

                  ....*...
gi 1774959464 468 RGSAKELL 475
Cdd:cd05107   386 RPDFSQLV 393
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
273-481 1.37e-06

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: 49.88  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 273 FEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd05608     6 FRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRkgyEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLT----DVVTET--------CMDEGQIAA----------VCREITPE------------------------QSKRSTM 383
Cdd:cd05608    86 GDLRyhiyNVDEENpgfqepraCFYTAQIISglehlhqrriIYRDLKPEnvlldddgnvrisdlglavelkdgQTKTKGY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL--------NENPLRALYLIATngtpelqNPEKLSAIFRD 455
Cdd:cd05608   166 AGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRargekvenKELKQRILNDSVT-------YSEKFSPASKS 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1774959464 456 FLNRCLEMDVEKR-----GSAKELLQHQFLK 481
Cdd:cd05608   239 ICEALLAKDPEKRlgfrdGNCDGLRTHPFFR 269
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
275-422 1.45e-06

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: 49.81  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAmdVATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 350
Cdd:cd14158    22 KLGEGGFGVVFKG--YINDKNVAVKKLAamvdISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 351 SLTD-----------VVTETC-----------------------------MDEGQIAAVCREITPEQSKRST-------M 383
Cdd:cd14158   100 SLLDrlaclndtpplSWHMRCkiaqgtanginylhennhihrdiksanilLDETFVPKISDFGLARASEKFSqtimterI 179
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1774959464 384 VGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMIEGEPP 422
Cdd:cd14158   180 VGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPP 217
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
261-457 1.56e-06

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: 50.41  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 261 VSVGDPK----KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSY 334
Cdd:cd07876    10 VQVADSTftvlKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSrpFQNQTHAKRAYRELVLLKCVNHKNIISLLNVF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 335 LVG------DELWVVMEyLAGGSLTDVVtETCMDEGQIA-----------------AVCREITPE--------------- 376
Cdd:cd07876    90 TPQksleefQDVYLVME-LMDANLCQVI-HMELDHERMSyllyqmlcgikhlhsagIIHRDLKPSnivvksdctlkildf 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 ---QSKRSTMVGTPY-----WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRAL-YLIATNGTPELQNPE 447
Cdd:cd07876   168 glaRTACTNFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWnKVIEQLGTPSAEFMN 247
                         250
                  ....*....|
gi 1774959464 448 KLSAIFRDFL 457
Cdd:cd07876   248 RLQPTVRNYV 257
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
382-428 1.56e-06

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: 50.42  E-value: 1.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 382 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP 428
Cdd:cd05628   195 STVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETP 241
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
271-417 1.61e-06

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: 49.87  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 271 TRFEKI---GQGASGTVYTAMDVATGQEVAIKQMNLqqqPKKELIINEilVMRENK------NPNIVNYLDSYLVG---- 337
Cdd:cd14048     6 TDFEPIqclGRGGFGVVFEAKNKVDDCNYAVKRIRL---PNNELAREK--VLREVRalakldHPGIVRYFNAWLERppeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 -----DE--LWVVMEYLAGGSLTDVVTETC-------------------------------------------------- 360
Cdd:cd14048    81 wqekmDEvyLYIQMQLCRKENLKDWMNRRCtmesrelfvclnifkqiasaveylhskglihrdlkpsnvffslddvvkvg 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774959464 361 -------MDEGQIAAVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 417
Cdd:cd14048   161 dfglvtaMDQGEPEQTVLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
259-491 1.72e-06

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: 50.04  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 259 SIVSVGDPK----KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLD 332
Cdd:cd07875    11 YSVEIGDSTftvlKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIIGLLN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 333 SYLVG------DELWVVMEyLAGGSLTDVVtETCMDEGQIAAVCRE------------ITPEQSKRSTMV---------- 384
Cdd:cd07875    91 VFTPQksleefQDVYIVME-LMDANLCQVI-QMELDHERMSYLLYQmlcgikhlhsagIIHRDLKPSNIVvksdctlkil 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 --------GTPYWMAPEVVTRKAYGPK----------VDIWSLGIMAIEMIEG--------------------------- 419
Cdd:cd07875   169 dfglartaGTSFMMTPYVVTRYYRAPEvilgmgykenVDIWSVGCIMGEMIKGgvlfpgtdhidqwnkvieqlgtpcpef 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 420 ----EP---PYLNENPLRALY----LIATNGTPELQNPEKLSAI-FRDFLNRCLEMDVEKRGSAKELLQHQFLKI-AKPL 486
Cdd:cd07875   249 mkklQPtvrTYVENRPKYAGYsfekLFPDVLFPADSEHNKLKASqARDLLSKMLVIDASKRISVDEALQHPYINVwYDPS 328

                  ....*
gi 1774959464 487 SSLTP 491
Cdd:cd07875   329 EAEAP 333
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
251-423 2.07e-06

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: 50.00  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 251 EEILEKLRSIVSVGDpkkKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNI 327
Cdd:cd05621    38 EKIVNKIRELQMKAE---DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSdsaFFWEERDIMAFANSPWV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 328 VNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEG-----------------QIAAVCREITPEQS------------ 378
Cdd:cd05621   115 VQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKwakfytaevvlaldaihSMGLIHRDVKPDNMlldkyghlklad 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 379 -------------KRSTMVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd05621   195 fgtcmkmdetgmvHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPF 256
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
386-480 2.34e-06

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: 49.24  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI-EGEPPYLNENPLRALY-LIATNGTPELQNPEKLSAIFRDFLNRCLEM 463
Cdd:cd14011   189 NLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKkNSNQLRQLSLSLLEKVPEELRDHVKTLLNV 268
                          90
                  ....*....|....*..
gi 1774959464 464 DVEKRGSAKELLQHQFL 480
Cdd:cd14011   269 TPEVRPDAEQLSKIPFF 285
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
385-468 2.49e-06

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: 49.19  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSaIFR--DFLNRCLE 462
Cdd:cd14067   179 GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKGIRPVLGQPEEVQ-FFRlqALMMECWD 257

                  ....*.
gi 1774959464 463 MDVEKR 468
Cdd:cd14067   258 TKPEKR 263
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
267-475 2.50e-06

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: 48.98  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 267 KKKYTRFEKIGQGASGTVYTAMdvATGQ-EVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05059     3 PSELTFLKELGSGQFGVVHLGK--WRGKiDVAIKMIK-EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSL------------TDVVTETCMDegqiaaVCREITPEQSK---------RSTMVG------------TPY---- 388
Cdd:cd05059    80 YMANGCLlnylrerrgkfqTEQLLEMCKD------VCEAMEYLESNgfihrdlaaRNCLVGeqnvvkvsdfglARYvldd 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 -------------WMAPEVVTRKAYGPKVDIWSLGIMAIEMI-EGEPPYLNENPLRALYLIATNgtPELQNPEKLSAIFR 454
Cdd:cd05059   154 eytssvgtkfpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFsEGKMPYERFSNSEVVEHISQG--YRLYRPHLAPTEVY 231
                         250       260
                  ....*....|....*....|.
gi 1774959464 455 DFLNRCLEMDVEKRGSAKELL 475
Cdd:cd05059   232 TIMYSCWHEKPEERPTFKILL 252
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
269-415 2.50e-06

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: 48.96  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMD-VATGQEVAIKQM--NLQQQPKKELIINEILVMRENKN---PNIVNYLDSYLVGDELWV 342
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSErVPTGKVYAVKKLkpNYAGAKDRLRRLEEVSILRELTLdghDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 343 VMEYLAGGSLTDVVTE----TCMDEGQIAAVCREIT----------------------------------------PEQS 378
Cdd:cd14052    81 QTELCENGSLDVFLSElgllGRLDEFRVWKILVELSlglrfihdhhfvhldlkpanvlitfegtlkigdfgmatvwPLIR 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1774959464 379 KRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIE 415
Cdd:cd14052   161 GIE-REGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
276-480 2.70e-06

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: 49.26  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQmnLQQQPKKELIINeiLVMRENKNPNIVNYLDSY--LVGDE--LWVVMEYLAGGS 351
Cdd:cd14170    10 LGLGINGKVLQIFNKRTQEKFALKM--LQDCPKARREVE--LHWRASQCPHIVRIVDVYenLYAGRkcLLIVMECLDGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 352 LTDVV-------------TETCMDEGQ-------IAAVCREITPEQ----SKR----------------------STMVG 385
Cdd:cd14170    86 LFSRIqdrgdqaftereaSEIMKSIGEaiqylhsINIAHRDVKPENllytSKRpnailkltdfgfakettshnslTTPCY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLR---ALYLIATNGTPELQNPE--KLSAIFRDFLNRC 460
Cdd:cd14170   166 TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispGMKTRIRMGQYEFPNPEwsEVSEEVKMLIRNL 245
                         250       260
                  ....*....|....*....|
gi 1774959464 461 LEMDVEKRGSAKELLQHQFL 480
Cdd:cd14170   246 LKTEPTQRMTITEFMNHPWI 265
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
363-459 3.11e-06

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 49.26  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 363 EGQIA----AVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY----LNENPLRAL-- 432
Cdd:cd05618   157 EGHIKltdyGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgSSDNPDQNTed 236
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1774959464 433 YLIATNGTPELQNPEKLS----AIFRDFLNR 459
Cdd:cd05618   237 YLFQVILEKQIRIPRSLSvkaaSVLKSFLNK 267
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
268-421 3.90e-06

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: 48.49  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQE-VAIKQMNLQQQPKKELI--INEILVMRE---NKNPNIVNYLDSYLVG---- 337
Cdd:cd07862     1 QQYECVAEIGEGAYGKVFKARDLKNGGRfVALKRVRVQTGEEGMPLstIREVAVLRHletFEHPNVVRLFDVCTVSrtdr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 -DELWVVME--------YLAGGSLTDVVTETCMD------EG-----QIAAVCREITPE--------------------- 376
Cdd:cd07862    81 eTKLTLVFEhvdqdlttYLDKVPEPGVPTETIKDmmfqllRGldflhSHRVVHRDLKPQnilvtssgqikladfglariy 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 377 --QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEP 421
Cdd:cd07862   161 sfQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKP 207
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
315-482 3.94e-06

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 48.31  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 315 EILV---MRenKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRE-----------------I 373
Cdd:PHA03390   58 EPMVhqlMK--DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLkKEGKLSEAEVKKIIRQlvealndlhkhniihndI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 374 TPE-----QSKR----------------STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY-------LN 425
Cdd:PHA03390  136 KLEnvlydRAKDriylcdyglckiigtpSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFkededeeLD 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1774959464 426 ENPLRALYliatngTPELQNPEKLSAIFRDFLNRCLEMDVEKR-GSAKELLQHQFLKI 482
Cdd:PHA03390  216 LESLLKRQ------QKKLPFIKNVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFLKI 267
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
364-420 4.03e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 49.22  E-value: 4.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 364 GQIAAVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGE 420
Cdd:PHA03212  224 GDFGAACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
269-355 4.40e-06

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: 48.22  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIK-QMNLQQQPkkeLIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKiEKKDSKHP---QLEYEAKVYKLlQGGPGIPRLYWFGQEGDYNVMVMDL 77

                  ....*....
gi 1774959464 347 LaGGSLTDV 355
Cdd:cd14016    78 L-GPSLEDL 85
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
276-477 5.07e-06

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: 48.09  E-value: 5.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELiINEILVMRE-NKNPNIVNYLDSYLVGDELWV-VMEYLAGGSLT 353
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDF-LREYNISLElSVHPHIIKTYDVAFETEDYYVfAQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 354 DVVTET----------CMDegQIAA----------VCREITPE----------QSK-----RSTMVGT---------PYw 389
Cdd:cd13987    80 SIIPPQvglpeervkrCAA--QLASaldfmhsknlVHRDIKPEnvllfdkdcrRVKlcdfgLTRRVGStvkrvsgtiPY- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVV-TRKAYG----PKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-------ATNGTPELQNP--EKLSAIFRd 455
Cdd:cd13987   157 TAPEVCeAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEfvrwqkrKNTAVPSQWRRftPKALRMFK- 235
                         250       260
                  ....*....|....*....|..
gi 1774959464 456 flnRCLEMDVEKRGSAKELLQH 477
Cdd:cd13987   236 ---KLLAPEPERRCSIKEVFKY 254
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
371-481 5.17e-06

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: 48.07  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 371 REITPEQSKRS-TMVGTPYWMAPEVVT--RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN-GTPELQNP 446
Cdd:cd05613   153 KEFLLDENERAySFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRiLKSEPPYP 232
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1774959464 447 EKLSAIFRDFLNRCLEMDVEKR-----GSAKELLQHQFLK 481
Cdd:cd05613   233 QEMSALAKDIIQRLLMKDPKKRlgcgpNGADEIKKHPFFQ 272
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
261-480 5.96e-06

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 48.34  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 261 VSVGDP-KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKqmnLQQQPKK--ELIINEILVMRE--NKNP------NIVN 329
Cdd:cd14136     2 VKIGEVyNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALK---VVKSAQHytEAALDEIKLLKCvrEADPkdpgreHVVQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 330 YLDSYLV----GDELWVVMEYLaGGSLTDVVtETCMDEG-------QIAA-----------VCR----EITPE------- 376
Cdd:cd14136    79 LLDDFKHtgpnGTHVCMVFEVL-GPNLLKLI-KRYNYRGiplplvkKIARqvlqgldylhtKCGiihtDIKPEnvllcis 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 377 --QSKRSTMvGTPYWM--------------APEVVTRKAYGPKVDIWSLGIMAIEMIEGEppYL-----------NENPL 429
Cdd:cd14136   157 kiEVKIADL-GNACWTdkhftediqtrqyrSPEVILGAGYGTPADIWSTACMAFELATGD--YLfdphsgedysrDEDHL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 430 rALYL---------IATNG--TPELQN--------------------------PEKLSAIFRDFLNRCLEMDVEKRGSAK 472
Cdd:cd14136   234 -ALIIellgriprsIILSGkySREFFNrkgelrhisklkpwpledvlvekykwSKEEAKEFASFLLPMLEYDPEKRATAA 312

                  ....*...
gi 1774959464 473 ELLQHQFL 480
Cdd:cd14136   313 QCLQHPWL 320
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
274-481 6.39e-06

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: 47.73  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTV---YTAMDVATGQEVAIKQM--NLQQQPKKElIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLA 348
Cdd:cd05060     1 KELGHGNFGSVrkgVYLMKSGKEVEVAVKTLkqEHEKAGKKE-FLREASVMAQLDHPCIVR-LIGVCKGEPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVVtetcMDEGQIAAV---------------------------CREI---TPEQSK-------RSTMVGTPY--- 388
Cdd:cd05060    79 LGPLLKYL----KKRREIPVSdlkelahqvamgmayleskhfvhrdlaARNVllvNRHQAKisdfgmsRALGAGSDYyra 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 ---------WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGtpELQNPEKLSAIFRDFLN 458
Cdd:cd05060   155 ttagrwplkWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGE--RLPRPEECPQEIYSIML 232
                         250       260
                  ....*....|....*....|...
gi 1774959464 459 RCLEMDVEKRGSAKELlqHQFLK 481
Cdd:cd05060   233 SCWKYRPEDRPTFSEL--ESTFR 253
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
266-475 6.45e-06

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 47.75  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAmdvATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVV 343
Cdd:cd14151     6 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLTDV--VTETCMDEGQIAAVCRE-------------------------------------ITPEQSKRS--- 381
Cdd:cd14151    82 TQWCEGSSLYHHlhIIETKFEMIKLIDIARQtaqgmdylhaksiihrdlksnniflhedltvkigdfgLATVKSRWSgsh 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 ---TMVGTPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQN-----PEK 448
Cdd:cd14151   162 qfeQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKvrsncPKA 241
                         250       260
                  ....*....|....*....|....*..
gi 1774959464 449 LSAIFRDflnrCLEMDVEKRGSAKELL 475
Cdd:cd14151   242 MKRLMAE----CLKKKRDERPLFPQIL 264
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
275-484 7.51e-06

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 47.72  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 275 KIGQGASGTVYTAmdvATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSL 352
Cdd:cd14149    19 RIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQFqaFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 ----------------TDVVTETCM-------------------------------DEGQIAAVCREITPEQSKRSTmvG 385
Cdd:cd14149    95 ykhlhvqetkfqmfqlIDIARQTAQgmdylhakniihrdmksnniflhegltvkigDFGLATVKSRWSGSQQVEQPT--G 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 386 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMIEGEPPYLN-ENPLRALYLIATNG-TPELQN-----PEKLSAIFRD 455
Cdd:cd14149   173 SILWMAPEVIRMQDNNPfsfQSDVYSYGIVLYELMTGELPYSHiNNRDQIIFMVGRGYaSPDLSKlykncPKAMKRLVAD 252
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1774959464 456 flnrCLEMDVEKRG------SAKELLQHQFLKIAK 484
Cdd:cd14149   253 ----CIKKVKEERPlfpqilSSIELLQHSLPKINR 283
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
233-481 8.03e-06

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: 48.08  E-value: 8.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 233 DALTRNTEKQKKKPKMSDEEILEKLRSIVS-VGDPKKKYTRFEK---IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPK 308
Cdd:cd05622    34 DALVYDLDFPALRKNKNIDNFLSRYKDTINkIRDLRMKAEDYEVvkvIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 309 KE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEG-----------------QIAA 368
Cdd:cd05622   114 RSdsaFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKwarfytaevvlaldaihSMGF 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 369 VCREITPEQS-------------------------KRSTMVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMIEG 419
Cdd:cd05622   194 IHRDVKPDNMlldksghlkladfgtcmkmnkegmvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVG 273
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 420 EPPYLNENpLRALYLIATNGTPELQNPEKlSAIFRDFLNRCLEMDVEK-----RGSAKELLQHQFLK 481
Cdd:cd05622   274 DTPFYADS-LVGTYSKIMNHKNSLTFPDD-NDISKEAKNLICAFLTDRevrlgRNGVEEIKRHLFFK 338
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
266-438 9.22e-06

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: 47.04  E-value: 9.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMdVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 345
Cdd:cd05148     4 PREEFTLERKLGSGYFGEVWEGL-WKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 346 YLAGGSLTDVV---------TETCMDEG-QIA-AVC-----REITPEQSKRSTMVG------------------------ 385
Cdd:cd05148    83 LMEKGSLLAFLrspegqvlpVASLIDMAcQVAeGMAyleeqNSIHRDLAARNILVGedlvckvadfglarlikedvylss 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1774959464 386 ---TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATN 438
Cdd:cd05148   163 dkkIPYkWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG 220
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
269-477 1.04e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 47.23  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQmnlQQQPKKELiINEILVMRE-------NKNPNIVNYLDSYLVGDELW 341
Cdd:cd14139     1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKR---SMRPFAGS-SNEQLALHEvyahavlGHHPHVVRYYSAWAEDDHMI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLAGGSLTDVVTETC-----MDEGQIAA----------------------------VCREITPEQSKRSTMVGTPY 388
Cdd:cd14139    77 IQNEYCNGGSLQDAISENTksgnhFEEPELKDillqvsmglkyihnsglvhldikpsnifICHKMQSSSGVGEEVSNEED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRK---------AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYL---IATNGTPELQN----------- 445
Cdd:cd14139   157 EFLSANVVYKigdlghvtsINKPQVEEGDSRFLANEILQEDYRHLPKADIFALGLtvaLAAGAEPLPTNgaawhhirkgn 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1774959464 446 ----PEKLSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14139   237 fpdvPQELPESFSSLLKNMIQPDPEQRPSATALARH 272
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
266-476 1.08e-05

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: 47.27  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVY--TAMDVATGQ---EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd05061     4 SREKITLLRELGQGSFGMVYegNARDIIKGEaetRVAVKTVNESASLRERIeFLNEASVMKGFTCHHVVRLLGVVSKGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVV----TETCMDEGQIAAVCREITP--------------------EQSKRSTMVGTPY------- 388
Cdd:cd05061    84 TLVVMELMAHGDLKSYLrslrPEAENNPGRPPPTLQEMIQmaaeiadgmaylnakkfvhrDLAARNCMVAHDFtvkigdf 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 -----------------------WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGTpeLQ 444
Cdd:cd05061   164 gmtrdiyetdyyrkggkgllpvrWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDGGY--LD 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1774959464 445 NPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQ 476
Cdd:cd05061   242 QPDNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
363-428 1.10e-05

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: 47.42  E-value: 1.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774959464 363 EGQIA----AVCREITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY----LNENP 428
Cdd:cd05588   132 EGHIKltdyGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNP 205
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
270-480 1.31e-05

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: 46.92  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL- 347
Cdd:cd07873     4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLd 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 ---------AGGSLT--------------------------DVVTETCM--DEGQIA----AVCREITPEQSKRSTMVGT 386
Cdd:cd07873    84 kdlkqylddCGNSINmhnvklflfqllrglaychrrkvlhrDLKPQNLLinERGELKladfGLARAKSIPTKTYSNEVVT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 PYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPE-------LQNPE---------- 447
Cdd:cd07873   164 LWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIfRILGTPTeetwpgiLSNEEfksynypkyr 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1774959464 448 ---------KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07873   244 adalhnhapRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYF 285
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
373-480 1.71e-05

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: 46.27  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 373 ITPEQSKRSTMVGTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLrALYLIATNGtpELQNPEKLS 450
Cdd:cd13976   136 LEGEDDSLSDKHGCPAYVSPEILnSGATYsGKAADVWSLGVILYTMLVGRYPFHDSEPA-SLFAKIRRG--QFAIPETLS 212
                          90       100       110
                  ....*....|....*....|....*....|
gi 1774959464 451 AIFRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd13976   213 PRARCLIRSLLRREPSERLTAEDILLHPWL 242
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
266-354 1.75e-05

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: 46.61  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTV----YTAMDVATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD-SYLVGD- 338
Cdd:cd05038     2 EERHLKFIKQLGEGHFGSVelcrYDPLGDNTGEQVAVKSLQPSGEEQhMSDFKREIEILRTLDHEYIVKYKGvCESPGRr 81
                          90
                  ....*....|....*.
gi 1774959464 339 ELWVVMEYLAGGSLTD 354
Cdd:cd05038    82 SLRLIMEYLPSGSLRD 97
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
344-474 1.95e-05

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: 46.49  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLT--DVVTETCM-DEGQIAAVC-----REITPEQS--KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMA 413
Cdd:cd05045   140 MQYLAEMKLVhrDLAARNVLvAEGRKMKISdfglsRDVYEEDSyvKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLL 219
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 414 IEMIE-GEPPYLNENPLRALYLIATNgtPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKEL 474
Cdd:cd05045   220 WEIVTlGGNPYPGIAPERLFNLLKTG--YRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
261-417 2.03e-05

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: 46.62  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 261 VSVGDPK----KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSY 334
Cdd:cd07874     6 VEVGDSTftvlKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIISLLNVF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 335 LVGDEL------WVVMEyLAGGSLTDVVtETCMDEGQIA-----------------AVCREITPE--------------- 376
Cdd:cd07874    86 TPQKSLeefqdvYLVME-LMDANLCQVI-QMELDHERMSyllyqmlcgikhlhsagIIHRDLKPSnivvksdctlkildf 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 377 ---QSKRSTMVGTP-----YWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 417
Cdd:cd07874   164 glaRTAGTSFMMTPyvvtrYYRAPEVILGMGYKENVDIWSVGCIMGEMV 212
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
270-481 2.20e-05

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 46.52  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLa 348
Cdd:cd07872     8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 ggsltDVVTETCMDE-GQIA----------------AVC-------REITPEQ------------------------SKR 380
Cdd:cd07872    87 -----DKDLKQYMDDcGNIMsmhnvkiflyqilrglAYChrrkvlhRDLKPQNllinergelkladfglaraksvptKTY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPELQNPEKLSAI--FRDF 456
Cdd:cd07872   162 SNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIfRLLGTPTEETWPGISSNdeFKNY 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 457 ------------------------LNRCLEMDVEKRGSAKELLQHQFLK 481
Cdd:cd07872   242 nfpkykpqplinhaprldtegielLTKFLQYESKKRISAEEAMKHAYFR 290
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
274-477 2.46e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 45.86  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQEVAIKQmnlQQQPKKELiINEILVMRE-------NKNPNIVNYLDSYLVGDELWVVMEY 346
Cdd:cd14051     6 EKIGSGEFGSVYKCINRLDGCVYAIKK---SKKPVAGS-VDEQNALNEvyahavlGKHPHVVRYYSAWAEDDHMIIQNEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 347 LAGGSLTDVVTETC-----MDEG-------QIAA---------------------VCREITPEQSKRS------------ 381
Cdd:cd14051    82 CNGGSLADAISENEkagerFSEAelkdlllQVAQglkyihsqnlvhmdikpgnifISRTPNPVSSEEEeedfegeednpe 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 --------------TMVGTPY-------WMAPEVVtRKAYG--PKVDIWSLGIMAIEMIEGEPpyLNENPlRALYLIATN 438
Cdd:cd14051   162 snevtykigdlghvTSISNPQveegdcrFLANEIL-QENYShlPKADIFALALTVYEAAGGGP--LPKNG-DEWHEIRQG 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1774959464 439 GTPELQNpekLSAIFRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14051   238 NLPPLPQ---CSPEFNELLRSMIHPDPEKRPSAAALLQH 273
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
271-492 3.25e-05

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: 45.75  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 271 TRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELiinEILVMRENkNPNIVNYLDSYlvGDEL--WVVMEYLA 348
Cdd:cd14092     9 LREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREV---QLLRLCQG-HPNIVKLHEVF--QDELhtYLVMELLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTDVV--------TETCMDEGQIAA----------VCREITPE--------------------------QSKRSTMV 384
Cdd:cd14092    83 GGELLERIrkkkrfteSEASRIMRQLVSavsfmhskgvVHRDLKPEnllftdedddaeikivdfgfarlkpeNQPLKTPC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVV----TRKAYGPKVDIWSLGIMAIEMIEGEPPY---LNENPLRALYLIATNGTPELQNPE--KLSAIFRD 455
Cdd:cd14092   163 FTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqspSRNESAAEIMKRIKSGDFSFDGEEwkNVSSEAKS 242
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1774959464 456 FLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSlTPL 492
Cdd:cd14092   243 LIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSS-TPL 278
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
268-484 3.31e-05

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: 46.16  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIK----QMNLQQQPKKELIINEILVMR--ENKNpNIVNYLDSYLVGDELW 341
Cdd:cd14226    13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKiiknKKAFLNQAQIEVRLLELMNKHdtENKY-YIVRLKRHFMFRNHLC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 342 VVMEYLA-------------GGSLT-------DVVTETC-MDEGQIAAVCREITPEQ-----SKRSTM------------ 383
Cdd:cd14226    92 LVFELLSynlydllrntnfrGVSLNltrkfaqQLCTALLfLSTPELSIIHCDLKPENillcnPKRSAIkiidfgsscqlg 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 384 ------VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEP---------------------P------------YL 424
Cdd:cd14226   172 qriyqyIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPlfsganevdqmnkivevlgmpPvhmldqapkarkFF 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 425 NENPLRALYLIATNGTPELQNP--EKLSAI-------------------------FRDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14226   252 EKLPDGTYYLKKTKDGKKYKPPgsRKLHEIlgvetggpggrragepghtvedylkFKDLILRMLDYDPKTRITPAEALQH 331

                  ....*..
gi 1774959464 478 QFLKIAK 484
Cdd:cd14226   332 SFFKRTA 338
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
276-481 3.89e-05

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: 45.64  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIIN-----EILVMRENKN-PNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHtigerNILVRTALDEsPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLT-DVVTETCMDEGQ----IAA-------------VCREITPEQ----------------SK--------RSTMVGTP 387
Cdd:cd05586    81 GELFwHLQKEGRFSEDRakfyIAElvlalehlhkndiVYRDLKPENilldanghialcdfglSKadltdnktTNTFCGTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVV-TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtpELQNPEK-LSAIFRDF----LNRCL 461
Cdd:cd05586   161 EYLAPEVLlDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFG---KVRFPKDvLSDEGRSFvkglLNRNP 237
                         250       260
                  ....*....|....*....|
gi 1774959464 462 EMDVEKRGSAKELLQHQFLK 481
Cdd:cd05586   238 KHRLGAHDDAVELKEHPFFA 257
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
269-355 4.74e-05

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 44.94  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpkKELIINEILVMRENKN-PNIVNYLDSYLVGDELWVVMEyL 347
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQP--KQVLKMEVAVLKKLQGkPHFCRLIGCGRTERYNYIVMT-L 77

                  ....*...
gi 1774959464 348 AGGSLTDV 355
Cdd:cd14017    78 LGPNLAEL 85
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
276-476 5.53e-05

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: 45.17  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQE-----VAIKQMN-LQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd05055    43 LGAGAFGKVVEATAYGLSKSdavmkVAVKMLKpTAHSSEREALMSELKIMSHlGNHENIVNLLGACTIGGPILVITEYCC 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GGSLTD----------------------------VVTETC-----------MDEGQIAAVC-----REITPEQ---SKRS 381
Cdd:cd05055   123 YGDLLNflrrkresfltledllsfsyqvakgmafLASKNCihrdlaarnvlLTHGKIVKICdfglaRDIMNDSnyvVKGN 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 382 TMVGTPyWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY----LNENplraLYLIATNGTPELQnPEKLSAIFRDF 456
Cdd:cd05055   203 ARLPVK-WMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYpgmpVDSK----FYKLIKEGYRMAQ-PEHAPAEIYDI 276
                         250       260
                  ....*....|....*....|
gi 1774959464 457 LNRCLEMDVEKRGSAKELLQ 476
Cdd:cd05055   277 MKTCWDADPLKRPTFKQIVQ 296
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
270-482 5.58e-05

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: 45.09  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQE--VAIKQM-NLQQqpKKELI---INEILVMRENKN-PNIVNYLDSYLVG----D 338
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEetVAIKKItNVFS--KKILAkraLRELKLLRHFRGhKNITCLYDMDIVFpgnfN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 339 ELWVVMEYL---------AGGSLTD--------------------------------VVTETCmdEGQIA--AVCREITP 375
Cdd:cd07857    80 ELYLYEELMeadlhqiirSGQPLTDahfqsfiyqilcglkyihsanvlhrdlkpgnlLVNADC--ELKICdfGLARGFSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 376 ----EQSKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTPE------- 442
Cdd:cd07857   158 npgeNAGFMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQIlQVLGTPDeetlsri 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 443 -----------LQNPEK--LSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd07857   238 gspkaqnyirsLPNIPKkpFESIFPnanplalDLLEKLLAFDPTKRISVEEALEHPYLAI 297
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
276-423 5.65e-05

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: 45.17  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYL--DSYLVGDELWVVMEYLAGGSL 352
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNnLSFMRPLDVQMREFEVLKKLNHKNIVKLFaiEEELTTRHKVLVMELCPCGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 353 TDVVTETC----MDEGQIAAVCREIT-----------------PEQSKRS---------------------------TMV 384
Cdd:cd13988    81 YTVLEEPSnaygLPESEFLIVLRDVVagmnhlrengivhrdikPGNIMRVigedgqsvykltdfgaareleddeqfvSLY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1774959464 385 GTPYWMAPEVVTR--------KAYGPKVDIWSLGIMAIEMIEGEPPY 423
Cdd:cd13988   161 GTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
268-428 6.21e-05

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: 44.52  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 268 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIKqMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd14110     3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAK-IIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 348 AGGSLTDVVTE-TCMDEGQI--------AAV----CREITPEQSKRSTMVGTPY-------------------------- 388
Cdd:cd14110    82 SGPELLYNLAErNSYSEAEVtdylwqilSAVdylhSRRILHLDLRSENMIITEKnllkivdlgnaqpfnqgkvlmtdkkg 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 389 ----WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENP 428
Cdd:cd14110   162 dyveTMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLN 205
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
389-477 7.62e-05

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 44.97  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY----LNENPLRALYLIATNGTPELQNPEklsaIFRDFLNrCLEM 463
Cdd:cd05103   247 WMAPETIFDRVYTIQSDVWSFGVLLWEIFSlGASPYpgvkIDEEFCRRLKEGTRMRAPDYTTPE----MYQTMLD-CWHG 321
                          90
                  ....*....|....
gi 1774959464 464 DVEKRGSAKELLQH 477
Cdd:cd05103   322 EPSQRPTFSELVEH 335
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
270-477 8.22e-05

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: 44.12  E-value: 8.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTS-ARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLTDVVTETCMDEGQIAAVCREI-----------------TPE------QSKRSTMV-------------------GTP 387
Cdd:cd14108    83 ELLERITKRPTVCESEVRSYMRQLlegieylhqndvlhldlKPEnllmadQKTDQVRIcdfgnaqeltpnepqyckyGTP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 388 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAT-NGTPELQNPEKLSAIFRDFLNRCLEMDvE 466
Cdd:cd14108   163 EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNyNVAFEESMFKDLCREAKGFIIKVLVSD-R 241
                         250
                  ....*....|.
gi 1774959464 467 KRGSAKELLQH 477
Cdd:cd14108   242 LRPDAEETLEH 252
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
266-476 8.62e-05

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 44.33  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTA----MDVATGQE--VAIKqMNLQQQPKKELI--INEILVMRE-NKNPNIVNYLDSYLV 336
Cdd:cd05053    10 PRDRLTLGKPLGEGAFGQVVKAeavgLDNKPNEVvtVAVK-MLKDDATEKDLSdlVSEMEMMKMiGKHKNIINLLGACTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 337 GDELWVVMEYLAGGSLTD-----------------VVTE---TCMDEGQIA-AVCREITPEQSK---------RSTMVGT 386
Cdd:cd05053    89 DGPLYVVVEYASKGNLREflrarrppgeeaspddpRVPEeqlTQKDLVSFAyQVARGMEYLASKkcihrdlaaRNVLVTE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 387 -----------------------------PY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPYLNEnPLRALYLI 435
Cdd:cd05053   169 dnvmkiadfglardihhidyyrkttngrlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGI-PVEELFKL 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1774959464 436 ATNG---TPELQNPEKLSAIFRDflnrCLEMDVEKRGSAKELLQ 476
Cdd:cd05053   248 LKEGhrmEKPQNCTQELYMLMRD----CWHEVPSQRPTFKQLVE 287
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
385-477 1.02e-04

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: 43.87  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGtpELQNPEKLSAIFRDFLNRCLE 462
Cdd:cd14022   148 GCPAYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEP-SSLFSKIRRG--QFNIPETLSPKAKCLIRSILR 224
                          90
                  ....*....|....*
gi 1774959464 463 MDVEKRGSAKELLQH 477
Cdd:cd14022   225 REPSERLTSQEILDH 239
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
269-482 1.12e-04

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: 44.38  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV---------NYLDSYLVG-- 337
Cdd:cd07854     6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVkvyevlgpsGSDLTEDVGsl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 338 ---DELWVVMEYLAggslTDVvtETCMDEGQIAA---------------------------------------------- 368
Cdd:cd07854    86 telNSVYIVQEYME----TDL--ANVLEQGPLSEeharlfmyqllrglkyihsanvlhrdlkpanvfintedlvlkigdf 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 369 -VCREITPEQSKR---STMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMIEGEP------------------PYLN 425
Cdd:cd07854   160 gLARIVDPHYSHKgylSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPlfagaheleqmqlilesvPVVR 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774959464 426 ENPLRAL-----YLIATNGT----------PELqNPEKLsaifrDFLNRCLEMDVEKRGSAKELLQHQFLKI 482
Cdd:cd07854   240 EEDRNELlnvipSFVRNDGGeprrplrdllPGV-NPEAL-----DFLEQILTFNPMDRLTAEEALMHPYMSC 305
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
274-354 1.23e-04

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 43.86  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMdvATGQEVAIKQMNLQQ----QPKKELIINEILvmrenKNPNIVNYLDSYLVG----DELWVVME 345
Cdd:cd14053     1 EIKARGRFGAVWKAQ--YLNRLVAVKIFPLQEkqswLTEREIYSLPGM-----KHENILQFIGAEKHGesleAEYWLITE 73

                  ....*....
gi 1774959464 346 YLAGGSLTD 354
Cdd:cd14053    74 FHERGSLCD 82
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
270-479 1.24e-04

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: 44.23  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVN---------------- 329
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNE--KDGFpitaLREIKILKKLKHPNVVPlidmaverpdkskrkr 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 330 --------YLDSYLVG------------------DELWVVMEYL-----------AGGSLTDvvtetcmDEG--QIA--A 368
Cdd:cd07866    88 gsvymvtpYMDHDLSGllenpsvkltesqikcymLQLLEGINYLhenhilhrdikAANILID-------NQGilKIAdfG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 369 VCREIT--PEQSKR---------STMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI- 435
Cdd:cd07866   161 LARPYDgpPPNPKGgggggtrkyTNLVVTRWYRPPELLLgERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIf 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 436 ATNGTPELQN-------------------PEKLSAIFR-------DFLNRCLEMDVEKRGSAKELLQHQF 479
Cdd:cd07866   241 KLCGTPTEETwpgwrslpgcegvhsftnyPRTLEERFGklgpeglDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
276-468 1.28e-04

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: 44.27  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 276 IGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKE---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAG 349
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSlvsTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 350 GSLT------DVVTETCMD--EGQIA----------AVCREITP----------------------EQSKRSTMVGTPYW 389
Cdd:cd14223    88 GDLHyhlsqhGVFSEAEMRfyAAEIIlglehmhsrfVVYRDLKPanilldefghvrisdlglacdfSKKKPHASVGTHGY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 390 MAPEVVTRK-AYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKR 468
Cdd:cd14223   168 MAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRR 247
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
385-477 1.29e-04

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: 43.50  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGtpELQNPEKLSAIFRDFLNRCLE 462
Cdd:cd14023   148 GCPAYVSPEILnTTGTYsGKSADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRG--QFCIPDHVSPKARCLIRSLLR 224
                          90
                  ....*....|....*
gi 1774959464 463 MDVEKRGSAKELLQH 477
Cdd:cd14023   225 REPSERLTAPEILLH 239
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
269-358 1.42e-04

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 43.86  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKqmnlqqQPKKELI--INEILVMRE-------NKNPNIVNYLDSYLVGDE 339
Cdd:cd14138     6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIK------RSKKPLAgsVDEQNALREvyahavlGQHSHVVRYYSAWAEDDH 79
                          90
                  ....*....|....*....
gi 1774959464 340 LWVVMEYLAGGSLTDVVTE 358
Cdd:cd14138    80 MLIQNEYCNGGSLADAISE 98
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
270-480 1.43e-04

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: 43.91  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTaIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 ggslTDVVT--ETC-----MDEGQI--------AAVC-------REITPEQ---SKR---------------------ST 382
Cdd:cd07844    82 ----TDLKQymDDCggglsMHNVRLflfqllrgLAYChqrrvlhRDLKPQNlliSERgelkladfglaraksvpsktySN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 383 MVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYL-NENPLRALYLI-ATNGTPELQ-------NPEKLSAI 452
Cdd:cd07844   158 EVVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFPgSTDVEDQLHKIfRVLGTPTEEtwpgvssNPEFKPYS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 453 FR---------------------DFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd07844   238 FPfypprplinhaprldriphgeELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
381-480 1.96e-04

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: 43.40  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 381 STMVGTPYWMAPEVV--TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLrALYLIATNGTPELQNPEKLSAIFRDFL 457
Cdd:cd14200   182 SSTAGTPAFMAPETLsdSGQSFsGKALDVWAMGVTLYCFVYGKCPFIDEFIL-ALHNKIKNKPVEFPEEPEISEELKDLI 260
                          90       100
                  ....*....|....*....|...
gi 1774959464 458 NRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14200   261 LKMLDKNPETRITVPEIKVHPWV 283
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
270-441 2.09e-04

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: 43.07  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 348
Cdd:cd07871     7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 349 GG---SLTDVVTETCMDEGQI--------AAVC-------REITPEQ------------------------SKRSTMVGT 386
Cdd:cd07871    87 SDlkqYLDNCGNLMSMHNVKIfmfqllrgLSYChkrkilhRDLKPQNllinekgelkladfglaraksvptKTYSNEVVT 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1774959464 387 PYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-ATNGTP 441
Cdd:cd07871   167 LWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIfRLLGTP 223
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
389-477 2.14e-04

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 43.25  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY----LNENPLRALYLIATNGTPELQNPEklsaIFRDFLNrCLEM 463
Cdd:cd05054   206 WMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYpgvqMDEEFCRRLKEGTRMRAPEYTTPE----IYQIMLD-CWHG 280
                          90
                  ....*....|....
gi 1774959464 464 DVEKRGSAKELLQH 477
Cdd:cd05054   281 EPKERPTFSELVEK 294
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
269-418 2.15e-04

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 43.31  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMR--ENKNPNIVNY---------------- 330
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSsiQRQHPNVIQLeecvlqrdglaqrmsh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 331 ----LDSYLVGDE----------------LWVVMEYLAGGSLTDVV--------TETC-----------MDEGQI----- 366
Cdd:cd13977    81 gsskSDLYLLLVEtslkgercfdprsacyLWFVMEFCDGGDMNEYLlsrrpdrqTNTSfmlqlssalafLHRNQIvhrdl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 367 -----------------------AAVCREITPE--------QSKRSTMVGTPYWMAPEvVTRKAYGPKVDIWSLGIMAIE 415
Cdd:cd13977   161 kpdnilishkrgepilkvadfglSKVCSGSGLNpeepanvnKHFLSSACGSDFYMAPE-VWEGHYTAKADIFALGIIIWA 239

                  ...
gi 1774959464 416 MIE 418
Cdd:cd13977   240 MVE 242
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
389-476 2.91e-04

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 43.04  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY----LNENPLRALyliaTNGT----PELQNPEklsaIFRDFLNr 459
Cdd:cd05102   240 WMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYpgvqINEEFCQRL----KDGTrmraPEYATPE----IYRIMLS- 310
                          90
                  ....*....|....*..
gi 1774959464 460 CLEMDVEKRGSAKELLQ 476
Cdd:cd05102   311 CWHGDPKERPTFSDLVE 327
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
274-428 3.40e-04

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: 42.46  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVY--TAMDVAtGQEV--AIKQMN-LQQQPKKELIINEILVMRENKNPNIV-------------------- 328
Cdd:cd05058     1 EVIGKGHFGCVYhgTLIDSD-GQKIhcAVKSLNrITDIEEVEQFLKEGIIMKDFSHPNVLsllgiclpsegsplvvlpym 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 329 ------NYLDSY--------LVGDELWVV--MEYLAGGSLT--DVVTETCM-DEGQIAAVC-----REITPEQ---SKRS 381
Cdd:cd05058    80 khgdlrNFIRSEthnptvkdLIGFGLQVAkgMEYLASKKFVhrDLAARNCMlDESFTVKVAdfglaRDIYDKEyysVHNH 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1774959464 382 TMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPYLNENP 428
Cdd:cd05058   160 TGAKLPVkWMALESLQTQKFTTKSDVWSFGVLLWElMTRGAPPYPDVDS 208
pknD PRK13184
serine/threonine-protein kinase PknD;
269-426 3.57e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 43.22  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 269 KYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMnlqqqpKKELIINEIL---VMRENK------NPNIVNYLDSYLVGDE 339
Cdd:PRK13184    3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKI------REDLSENPLLkkrFLREAKiaadliHPGIVPVYSICSDGDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLT---------DVVTETCMDEGQIAA-------VC-------------REITPE-------------- 376
Cdd:PRK13184   77 VYYTMPYIEGYTLKsllksvwqkESLSKELAEKTSVGAflsifhkICatieyvhskgvlhRDLKPDnillglfgevvild 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774959464 377 ----------------------QSKRSTM------VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE 426
Cdd:PRK13184  157 wgaaifkkleeedlldidvderNICYSSMtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRK 234
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
266-352 3.59e-04

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: 42.67  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYT--------------AMDVATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIV 328
Cdd:cd05095     3 PRKLLTFKEKLGEGQFGEVHLceaegmekfmdkdfALEVSENQPVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNII 82
                          90       100
                  ....*....|....*....|....
gi 1774959464 329 NYLDSYLVGDELWVVMEYLAGGSL 352
Cdd:cd05095    83 RLLAVCITDDPLCMITEYMENGDL 106
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
344-491 4.84e-04

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 42.32  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLT--DVVTETCM-DEGQIAAVC-----REITPEQ---SKRSTMVGTPyWMAPEVVTRKAYGPKVDIWSLGIM 412
Cdd:cd05105   250 MEFLASKNCVhrDLAARNVLlAQGKIVKICdfglaRDIMHDSnyvSKGSTFLPVK-WMAPESIFDNLYTTLSDVWSYGIL 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 413 AIEMIE-GEPPYLNENPLRALYLIATNGTpELQNPEKLSAIFRDFLNRCLEMDVEKRGSakellqhqFLKIAKPLSSLTP 491
Cdd:cd05105   329 LWEIFSlGGTPYPGMIVDSTFYNKIKSGY-RMAKPDHATQEVYDIMVKCWNSEPEKRPS--------FLHLSDIVESLLP 399
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
385-480 5.25e-04

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: 41.79  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLrALYLIATNGTPELqnPEKLSAIFRDFLNRCLE 462
Cdd:cd14024   148 GCPAYVGPEILsSRRSYsGKAADVWSLGVCLYTMLLGRYPFQDTEPA-ALFAKIRRGAFSL--PAWLSPGARCLVSCMLR 224
                          90
                  ....*....|....*...
gi 1774959464 463 MDVEKRGSAKELLQHQFL 480
Cdd:cd14024   225 RSPAERLKASEILLHPWL 242
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
270-477 5.79e-04

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: 41.71  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQqpkkELIINEILVMRENKNPNIVNYLDSYLVGDE---------- 339
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNN----EKAEREVKALAKLDHPNIVRYNGCWDGFDYdpetsssnss 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 ------LWVVMEYLAGGSLTDVVTEtcMDEGQIAAVC----------------------REITPEQ-------------- 377
Cdd:cd14047    84 rsktkcLFIQMEFCEKGTLESWIEK--RNGEKLDKVLaleifeqitkgveyihskklihRDLKPSNiflvdtgkvkigdf 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 378 ---------SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMiegeppylnenplraLYLIAT-NGTPE----L 443
Cdd:cd14047   162 glvtslkndGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL---------------LHVCDSaFEKSKfwtdL 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1774959464 444 QNpEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQH 477
Cdd:cd14047   227 RN-GILPDIFdkrykieKTIIKKMLSKKPEDRPNASEILRT 266
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
385-471 6.77e-04

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: 41.45  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 385 GTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEklSAIFR---DFLNRC 460
Cdd:cd14000   177 GTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRPPLKQYE--CAPWPeveVLMKKC 254
                          90
                  ....*....|.
gi 1774959464 461 LEMDVEKRGSA 471
Cdd:cd14000   255 WKENPQQRPTA 265
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
389-476 8.40e-04

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 41.53  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY----LNENPLRALYLIATNGTPELQNPEklsaIFRDFLNrCLEM 463
Cdd:cd14207   248 WMAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASPYpgvqIDEDFCSKLKEGIRMRAPEFATSE----IYQIMLD-CWQG 322
                          90
                  ....*....|...
gi 1774959464 464 DVEKRGSAKELLQ 476
Cdd:cd14207   323 DPNERPRFSELVE 335
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
266-423 9.98e-04

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: 41.22  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 266 PKKKYTRFEKIGQGASGTVYTAMDVA-TGQ----EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDE 339
Cdd:cd05036     4 PRKNLTLIRALGQGAFGEVYEGTVSGmPGDpsplQVAVKTLPELCSEQDEMdFLMEALIMSKFNHPNIVRCIGVCFQRLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 340 LWVVMEYLAGGSLTDVVTETCMDEGQ---------------IAAVC----------REI-------TPEQSKRSTMVG-- 385
Cdd:cd05036    84 RFILLELMAGGDLKSFLRENRPRPEQpssltmldllqlaqdVAKGCryleenhfihRDIaarncllTCKGPGRVAKIGdf 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464 386 --------TPY------------WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY 423
Cdd:cd05036   164 gmardiyrADYyrkggkamlpvkWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPY 222
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
389-476 1.38e-03

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: 40.53  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMI-EGEPPY---LNENPLRALyliaTNGTPELQNPEKLSAIFRDFLNRCLEMD 464
Cdd:cd05046   184 WLAPEAVQEDDFSTKSDVWSFGVLMWEVFtQGELPFyglSDEEVLNRL----QAGKLELPVPEGCPSRLYKLMTRCWAVN 259
                          90
                  ....*....|..
gi 1774959464 465 VEKRGSAKELLQ 476
Cdd:cd05046   260 PKDRPSFSELVS 271
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
344-474 1.46e-03

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: 40.60  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 344 MEYLAGGSLT--DVVTETCM-DEGQIAAVC-----REITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMA 413
Cdd:cd05035   126 MEYLSNRNFIhrDLAARNCMlDENMTVCVAdfglsRKIYSGDYYRQGRISKmPVkWIALESLADNVYTSKSDVWSFGVTM 205
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774959464 414 IE-MIEGEPPYLN-ENPLRALYLIatNGTPELQNPEKLSAIFrDFLNRCLEMDVEKRGSAKEL 474
Cdd:cd05035   206 WEiATRGQTPYPGvENHEIYDYLR--NGNRLKQPEDCLDEVY-FLMYFCWTVDPKDRPTFTKL 265
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
383-428 1.53e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 40.63  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1774959464 383 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIeGEPPYLNENP 428
Cdd:PHA03209  216 LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML-AYPSTIFEDP 260
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
389-476 2.66e-03

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: 39.74  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 389 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENP------LRALYLIATngtpELQNPEKLSAIfrdfLNRCL 461
Cdd:cd05043   184 WMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDPfemaayLKDGYRLAQ----PINCPDELFAV----MACCW 255
                          90
                  ....*....|....*
gi 1774959464 462 EMDVEKRGSAKELLQ 476
Cdd:cd05043   256 ALDPEERPSFQQLVQ 270
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
270-347 2.82e-03

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: 39.68  E-value: 2.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774959464 270 YTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 347
Cdd:cd07869     7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTaIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYV 85
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
453-480 2.91e-03

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: 39.90  E-value: 2.91e-03
                          10        20
                  ....*....|....*....|....*...
gi 1774959464 453 FRDFLNRCLEMDVEKRGSAKELLQHQFL 480
Cdd:cd14135   291 LKDLLDKCLMLDPEKRITPNEALQHPFI 318
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
274-352 4.52e-03

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: 38.94  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMDVATGQE---VAIKQMNLQQQP-KKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAG 349
Cdd:cd05056    12 RCIGEGQFGDVYQGVYMSPENEkiaVAVKTCKNCTSPsVREKFLQEAYIMRQFDHPHIVK-LIGVITENPVWIVMELAPL 90

                  ...
gi 1774959464 350 GSL 352
Cdd:cd05056    91 GEL 93
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
401-480 5.29e-03

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 38.75  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 401 GPKVDIWSLGIMAIEMI------EGEPPYLNENPLRALYliatngtpELQNPEklsaiFRDFLNRCLEMDVEKRGSAKEL 474
Cdd:cd14035   190 GTAVDIFSFGMCALEMAvleiqaNGDTRVSEEAIARARH--------SLEDPN-----MREFILSCLRHNPCKRPTAHDL 256

                  ....*.
gi 1774959464 475 LQHQFL 480
Cdd:cd14035   257 LFHRVL 262
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
274-374 6.26e-03

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 38.50  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 274 EKIGQGASGTVYTAMdvATGQEVAIK--QMNLQQQPKKELIINEILVMRenkNPNIVNYL--DSYLVGDELW---VVMEY 346
Cdd:cd14054     1 QLIGQGRYGTVWKGS--LDERPVAVKvfPARHRQNFQNEKDIYELPLME---HSNILRFIgaDERPTADGRMeylLVLEY 75
                          90       100
                  ....*....|....*....|....*...
gi 1774959464 347 LAGGSLTDVVTETCMDEGQIAAVCREIT 374
Cdd:cd14054    76 APKGSLCSYLRENTLDWMSSCRMALSLT 103
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
287-373 7.79e-03

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 38.08  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959464 287 AMDVATGQEVAIKQMNLQQQPKKELIINEIL----VMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMD 362
Cdd:cd13973    19 ARDTVLGRDVALTFVDPGGAAAAARRAAEVLraarRLARLNDPGLARVLDAVAYRGGVYVVAEWVPGSSLADVAESGPLD 98
                          90
                  ....*....|.
gi 1774959464 363 EGQIAAVCREI 373
Cdd:cd13973    99 PEAAARAVAEL 109
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH