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Conserved domains on  [gi|75906578|ref|YP_320874|]
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serine/threonine kinase protein [Anabaena variabilis ATCC 29413]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
177-418 3.04e-39

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 141.22  E-value: 3.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKaqELFEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAMELV 256
Cdd:cd00180   1 LGEGGFGTVYLARD-----KKTGKKVAIKIIKKEDSSSLL--EELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 257 HGQDLEKRIYATGPVIP-SQAIAWMIQTCDILDYLHSqeQPLIHRDIKPANLMVKTANNQIAVLDFGAVKEIGT---TPG 332
Cdd:cd00180  74 EGGSLKDLLKENEGKLSeDEILRILLQILEGLEYLHS--NGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSdksLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 333 TRIGAEGYCAPEQERGQPL--TQSDLYAIGpTIIFLLtgenpfkfyrqkgrgfrfdvskiptvtPKLRDVIERTTEPLPR 410
Cdd:cd00180 152 TIVGTPAYMAPEVLLGKGYysEKSDIWSLG-VILYEL---------------------------PELKDLIRKMLQKDPE 203

                ....*...
gi 75906578 411 DRFqSAKE 418
Cdd:cd00180 204 KRP-SAKE 210
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
4-103 1.14e-13

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


:

Pssm-ID: 238017  Cd Length: 102  Bit Score: 66.64  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   4 LTLLEPQQKTPLKQWCFENSSVIRIGRAADNH-VILSDNLVSRHHLEIRQVSSGGGgsWQVLSKGTNGTFLNGVLVIQDA 82
Cdd:cd00060   2 PRLVVLSGDASGRRYYLDPGGTYTIGRDSDNCdIVLDDPSVSRRHAVIRYDGDGGV--VLIDLGSTNGTFVNGQRVSPGE 79
                        90       100
                ....*....|....*....|....
gi 75906578  83 ---LPNNALLQLaqGGPILQFQVQ 103
Cdd:cd00060  80 pvrLRDGDVIRL--GNTSISFRFE 101
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
171-418 1.16e-47

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 165.40  E-value: 1.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    171 YQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNadMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKKY 250
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-----KKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    251 LAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEIGTT 330
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILL-DEDGHVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    331 P--GTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPF-------KFYRQKGRGFRFDVSKIPTVTPKLRDV 400
Cdd:smart00220 151 EklTTFVGTPEYMAPEVLLGKGYGkAVDIWSLGVILYELLTGKPPFpgddqllELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....*...
gi 75906578    401 IERTTEPLPRDRFqSAKE 418
Cdd:smart00220 231 IRKLLVKDPEKRL-TAEE 247
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
1-92 3.34e-12

FOG: FHA domain [Signal transduction mechanisms]


:

Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 64.21  E-value: 3.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   1 MVTLTLLEPQQKTPLKQWCFENSS------VIRIGRAADNHVILSDNLVSRHHLEIRQVSSGGggsWQVLSKGTNGTFLN 74
Cdd:COG1716  60 LEPGVLTALDGPLAVTIGLDEGSVivlgepVTTIGRDPDNDIVLDDDVVSRRHAELRREGNEV---FLEDLGSTNGTYVN 136
                        90
                ....*....|....*....
gi 75906578  75 GVLVIQD-ALPNNALLQLA 92
Cdd:COG1716 137 GEKVRQRvLLQDGDVIRLG 155
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
177-418 3.04e-39

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 141.22  E-value: 3.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKaqELFEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAMELV 256
Cdd:cd00180   1 LGEGGFGTVYLARD-----KKTGKKVAIKIIKKEDSSSLL--EELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 257 HGQDLEKRIYATGPVIP-SQAIAWMIQTCDILDYLHSqeQPLIHRDIKPANLMVKTANNQIAVLDFGAVKEIGT---TPG 332
Cdd:cd00180  74 EGGSLKDLLKENEGKLSeDEILRILLQILEGLEYLHS--NGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSdksLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 333 TRIGAEGYCAPEQERGQPL--TQSDLYAIGpTIIFLLtgenpfkfyrqkgrgfrfdvskiptvtPKLRDVIERTTEPLPR 410
Cdd:cd00180 152 TIVGTPAYMAPEVLLGKGYysEKSDIWSLG-VILYEL---------------------------PELKDLIRKMLQKDPE 203

                ....*...
gi 75906578 411 DRFqSAKE 418
Cdd:cd00180 204 KRP-SAKE 210
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
4-103 1.14e-13

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 66.64  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   4 LTLLEPQQKTPLKQWCFENSSVIRIGRAADNH-VILSDNLVSRHHLEIRQVSSGGGgsWQVLSKGTNGTFLNGVLVIQDA 82
Cdd:cd00060   2 PRLVVLSGDASGRRYYLDPGGTYTIGRDSDNCdIVLDDPSVSRRHAVIRYDGDGGV--VLIDLGSTNGTFVNGQRVSPGE 79
                        90       100
                ....*....|....*....|....
gi 75906578  83 ---LPNNALLQLaqGGPILQFQVQ 103
Cdd:cd00060  80 pvrLRDGDVIRL--GNTSISFRFE 101
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
26-91 1.80e-11

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 249907  Cd Length: 67  Bit Score: 59.53  E-value: 1.80e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75906578    26 IRIGRAADNHVILSDNLVSRHHLEIRQvssGGGGSWQVLSKG-TNGTFLNGVLVIQDA--LPNNALLQL 91
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIRY---DGGGRFYLEDLGsTNGTFVNGQRLGPGPvrLRDGDVIRL 66
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
26-78 6.47e-09

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578  Cd Length: 52  Bit Score: 52.18  E-value: 6.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 75906578     26 IRIGRA-ADNHVILSDNLVSRHHLEIRqvsSGGGGSWQVLSKG-TNGTFLNGVLV 78
Cdd:smart00240   1 VTIGRSsEDCDIQLDGPSISRRHAVIV---YDGGGRFYLIDLGsTNGTFVNGKRI 52
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
159-324 3.06e-04

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 41.09  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  159 GQPLSVIqTIRHYQVLRTLGQGGMGTTYLAWDAAGVIVGHPKLLVLKQMNAD--MARIAKAQELFEREAYTL----KSLN 232
Cdd:PHA02882   3 GIPLIDI-TGKEWKIDKLIGCGGFGCVYETQCASDHCINNQAVAKIENLENEtiVMETLVYNNIYDIDKIALwkniHNID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  233 HSGIPKYY-----------------DFFVEGGKKYLAMELVHGQDLEKRIyatgpvipsqaiawMIQTCDILDYLHsqEQ 295
Cdd:PHA02882  82 HLGIPKYYgcgsfkrcrmyyrfillEKLVENTKEIFKRIKCKNKKLIKNI--------------MKDMLTTLEYIH--EH 145
                        170       180
                 ....*....|....*....|....*....
gi 75906578  296 PLIHRDIKPANLMVKTaNNQIAVLDFGAV 324
Cdd:PHA02882 146 GISHGDIKPENIMVDG-NNRGYIIDYGIA 173
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
171-418 1.16e-47

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 165.40  E-value: 1.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    171 YQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNadMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKKY 250
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-----KKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    251 LAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEIGTT 330
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILL-DEDGHVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    331 P--GTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPF-------KFYRQKGRGFRFDVSKIPTVTPKLRDV 400
Cdd:smart00220 151 EklTTFVGTPEYMAPEVLLGKGYGkAVDIWSLGVILYELLTGKPPFpgddqllELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....*...
gi 75906578    401 IERTTEPLPRDRFqSAKE 418
Cdd:smart00220 231 IRKLLVKDPEKRL-TAEE 247
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
170-418 2.46e-47

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 168.00  E-value: 2.46e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDaagvivghPKLLVLKQMNADMARIAKAQELFEREAYTLKSLNHSG-IPKYYDFFVEGGK 248
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARD--------RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQDEGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 249 KYLAMELVHGQDLEKRI---YATGPVIPSQAIAWMIQTCDILDYLHsqEQPLIHRDIKPANLMVKTANNQIAVLDFGAVK 325
Cdd:COG0515  73 LYLVMEYVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLH--SKGIIHRDIKPENILLDRDGRVVKLIDFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 326 EIG---------TTPGTRIGAEGYCAPEQERGQPL----TQSDLYAIGPTIIFLLTGENPF--------------KFYRQ 378
Cdd:COG0515 151 LLPdpgstssipALPSTSVGTPGYMAPEVLLGLSLayasSSSDIWSLGITLYELLTGLPPFegeknssatsqtlkIILEL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75906578 379 KGRGFRFDVSKI--PTVTPKLRDVIERTTEPLPRDRFQSAKE 418
Cdd:COG0515 231 PTPSLASPLSPSnpELISKAASDLLKKLLAKDPKNRLSSSSD 272
Pkinase pfam00069
Protein kinase domain;
171-418 4.15e-43

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 153.17  E-value: 4.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   171 YQVLRTLGQGGMGTTYLA-WDAAGVIVghpkllVLKQMNADMARIAKAQELFeREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAkHKGTGKIV------AVKILKKRSEKSKKDQTAR-REIRILRRLSHPNIVRLIDAFEDKDHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   250 YLAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSqeQPLIHRDIKPANLMVKTaNNQIAVLDFGAVKEI-- 327
Cdd:pfam00069  74 YLVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHS--NGIIHRDLKPENILLDE-NGVVKIADFGLAKKLtk 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   328 -GTTPGTRIGAEGYCAPEQERGQP--LTQSDLYAIGPTIIFLLTGENPF----------KFYRQKGRGFRFDVSKIPTVT 394
Cdd:pfam00069 151 sSSSLTTFVGTPEYMAPEVLLGGNgyGPKVDVWSLGVILYELLTGKPPFsgesildqlqLIRRILGPPLEFDEPKSDSGS 230
                         250       260
                  ....*....|....*....|....
gi 75906578   395 PKLRDVIERTTEPLPRDRFqSAKE 418
Cdd:pfam00069 231 EEAKDLIKKCLNKDPSKRP-TAEE 253
pknD PRK13184
serine/threonine-protein kinase; Reviewed
168-418 1.05e-24

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 105.62  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  168 IRHYQVLRTLGQGGMGTTYLAWDAAGvivghPKLLVLKQMNADMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGG 247
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVC-----SRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  248 KKYLAMELVHG------------QDLEKRIYATGPVIPSqAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVKTAnNQ 315
Cdd:PRK13184  76 PVYYTMPYIEGytlksllksvwqKESLSKELAEKTSVGA-FLSIFHKICATIEYVHSKG--VLHRDLKPDNILLGLF-GE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  316 IAVLDFGAVKEIG---------------------TTPGTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPF 373
Cdd:PRK13184 152 VVILDWGAAIFKKleeedlldidvdernicyssmTIPGKIVGTPDYMAPERLLGVPASeSTDIYALGVILYQMLTLSFPY 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 75906578  374 KfyRQKGRGFRFD--------VSKIPTVTPKLRDVIERTTEPLPRDRFQSAKE 418
Cdd:PRK13184 232 R--RKKGRKISYRdvilspieVAPYREIPPFLSQIAMKALAVDPAERYSSVQE 282
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
202-417 4.80e-21

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 94.91  E-value: 4.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    202 LVLKQMNADMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEG-GKKYLAMELVHGQDLEKRIYATGPVIPSQAIAWM 280
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    281 IQTCDILDYLHSQEqpLIHRDIKPANLMVKTANNQ--IAVLDFGavkeIGTT-PGTR-------------IGAEGYCAPE 344
Cdd:TIGR03903   86 LQVLDALACAHNQG--IVHRDLKPQNIMVSQTGVRphAKVLDFG----IGTLlPGVRdadvatltrttevLGTPTYCAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578    345 QERGQPLT-QSDLYAIGPTIIFLLTGENPFK-------FYRQKGrgfRFDVSkIPTVTPKLR--DVIERTTEPLPRDRFQ 414
Cdd:TIGR03903  160 QLRGEPVTpNSDLYAWGLIFLECLTGQRVVQgasvaeiLYQQLS---PVDVS-LPPWIAGHPlgQVLRKALNKDPRQRAA 235

                   ...
gi 75906578    415 SAK 417
Cdd:TIGR03903  236 SAP 238
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
280-407 3.95e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 67.96  E-value: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  280 MIQTCDILDYLHSQEqpLIHRDIKPANLMVKTANNQIAVLDFGAVKEIGtTPGTRIGAEGYCAPEQERGQPLTQS-DLYA 358
Cdd:PHA03390 115 IRQLVEALNDLHKHN--IIHNDIKLENVLYDRAKDRIYLCDYGLCKIIG-TPSCYDGTLDYFSPEKIKGHNYDVSfDWWA 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75906578  359 IGPTIIFLLTGENPFK------------FYRQkgrgfRFDVSKIPTVTPKLRDVIERTTEP 407
Cdd:PHA03390 192 VGVLTYELLTGKHPFKededeeldleslLKRQ-----QKKLPFIKNVSKNANDFVQSMLKY 247
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
1-92 3.34e-12

FOG: FHA domain [Signal transduction mechanisms]


Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 64.21  E-value: 3.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   1 MVTLTLLEPQQKTPLKQWCFENSS------VIRIGRAADNHVILSDNLVSRHHLEIRQVSSGGggsWQVLSKGTNGTFLN 74
Cdd:COG1716  60 LEPGVLTALDGPLAVTIGLDEGSVivlgepVTTIGRDPDNDIVLDDDVVSRRHAELRREGNEV---FLEDLGSTNGTYVN 136
                        90
                ....*....|....*....
gi 75906578  75 GVLVIQD-ALPNNALLQLA 92
Cdd:COG1716 137 GEKVRQRvLLQDGDVIRLG 155
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
218-379 2.55e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 60.80  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  218 QELFER-EAYTLKSLNHSGIPKYYDFFVEGGKKYLAMELVHGQDLEK----RIYATGPVIPSQAIAWMIQTCDILDYLHS 292
Cdd:PTZ00267 108 QAAYARsELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKqikqRLKEHLPFQEYEVGLLFYQIVLALDEVHS 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  293 QEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEIGTTPGTRI-----GAEGYCAPE-QERGQPLTQSDLYAIGPTIIFL 366
Cdd:PTZ00267 188 RK--MMHRDLKSANIFL-MPTGIIKLGDFGFSKQYSDSVSLDVassfcGTPYYLAPElWERKRYSKKADMWSLGVILYEL 264
                        170
                 ....*....|...
gi 75906578  367 LTGENPFKFYRQK 379
Cdd:PTZ00267 265 LTLHRPFKGPSQR 277
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
138-378 1.48e-09

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 57.91  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  138 PGSLTCTHEGNSPQNLFCIHCGQPLSVIQTIRHyqvlrtLGQGGMGTTYLawdaagvIVGHP--KLLVLKQMNADMARIA 215
Cdd:PLN00034  49 PPSSSSSSSSSSSASGSAPSAAKSLSELERVNR------IGSGAGGTVYK-------VIHRPtgRLYALKVIYGNHEDTV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  216 KAQelFEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAMELVHGQDLEKRIYATGPVIPSQAIawmiQTCDILDYLHSQEq 295
Cdd:PLN00034 116 RRQ--ICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVAR----QILSGIAYLHRRH- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578  296 pLIHRDIKPANLMVKTANNqIAVLDFGAVKEIGTT--P-GTRIGAEGYCAPEQERGQpLTQ-------SDLYAIGPTIIF 365
Cdd:PLN00034 189 -IVHRDIKPSNLLINSAKN-VKIADFGVSRILAQTmdPcNSSVGTIAYMSPERINTD-LNHgaydgyaGDIWSLGVSILE 265
                        250
                 ....*....|...
gi 75906578  366 LLTGENPFKFYRQ 378
Cdd:PLN00034 266 FYLGRFPFGVGRQ 278
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
3-132 1.98e-05

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis].


Pssm-ID: 234178 [Multi-domain]  Cd Length: 396  Bit Score: 45.05  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578     3 TLTLLEPQQKTP--LKQWCFENSSViRIGRAADNHVILSD--NLVSRHHLEIRqvssGGGGSWQVLSKGTNGTFLNGVLV 78
Cdd:TIGR03354   2 VLTVLNAHQLTPgiAAQKTFGTNGG-TIGRSEDCDWVLPDpeRHVSGRHARIR----YRDGAYLLTDLSTNGVFLNGSGS 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 75906578    79 iqdALPNNALLQLAQGGPIL--QFQVQGIIPPEWQSISGSDSPLS-GVGSSAEKISP 132
Cdd:TIGR03354  77 ---PLGRGNPVRLEQGDRLRlgDYEIRVSLGDPLVSRQASESRADtSLPTAGGPPTP 130
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
177-418 3.04e-39

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 141.22  E-value: 3.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKaqELFEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAMELV 256
Cdd:cd00180   1 LGEGGFGTVYLARD-----KKTGKKVAIKIIKKEDSSSLL--EELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 257 HGQDLEKRIYATGPVIP-SQAIAWMIQTCDILDYLHSqeQPLIHRDIKPANLMVKTANNQIAVLDFGAVKEIGT---TPG 332
Cdd:cd00180  74 EGGSLKDLLKENEGKLSeDEILRILLQILEGLEYLHS--NGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSdksLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 333 TRIGAEGYCAPEQERGQPL--TQSDLYAIGpTIIFLLtgenpfkfyrqkgrgfrfdvskiptvtPKLRDVIERTTEPLPR 410
Cdd:cd00180 152 TIVGTPAYMAPEVLLGKGYysEKSDIWSLG-VILYEL---------------------------PELKDLIRKMLQKDPE 203

                ....*...
gi 75906578 411 DRFqSAKE 418
Cdd:cd00180 204 KRP-SAKE 210
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
4-103 1.14e-13

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 66.64  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578   4 LTLLEPQQKTPLKQWCFENSSVIRIGRAADNH-VILSDNLVSRHHLEIRQVSSGGGgsWQVLSKGTNGTFLNGVLVIQDA 82
Cdd:cd00060   2 PRLVVLSGDASGRRYYLDPGGTYTIGRDSDNCdIVLDDPSVSRRHAVIRYDGDGGV--VLIDLGSTNGTFVNGQRVSPGE 79
                        90       100
                ....*....|....*....|....
gi 75906578  83 ---LPNNALLQLaqGGPILQFQVQ 103
Cdd:cd00060  80 pvrLRDGDVIRL--GNTSISFRFE 101
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
170-412 3.93e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 133.78  E-value: 3.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMN-ADMARIAKAQELfeREAYTLKSLNHSGIPKYYDFFVEGGK 248
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRR-----KSDGKLYVLKEIDlSNMSEKEREDAL--NEVKILKKLNHPNIIKYYESFEEKGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 249 KYLAMELVHGQDLEKRI---YATGPVIP-SQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAV 324
Cdd:cd08215  74 LCIVMEYADGGDLSQKIkkqKKEGKPFPeEQILDWFVQLCLALKYLHSRK--ILHRDIKPQNIFL-TSNGLVKLGDFGIS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 325 KEIGTTPG---TRIGAEGYCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPFKFYRQKG------RGfrfDVSKIPT-V 393
Cdd:cd08215 151 KVLSSTVDlakTVVGTPYYLSPELCQNKPYNYkSDIWSLGCVLYELCTLKHPFEGENLLElalkilKG---QYPPIPSqY 227
                       250
                ....*....|....*....
gi 75906578 394 TPKLRDVIERTTEPLPRDR 412
Cdd:cd08215 228 SSELRNLVSSLLQKDPEER 246
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
170-412 5.91e-31

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 119.23  E-value: 5.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDAA-GVIVGhpkllvLKQMNAdmaRIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGK 248
Cdd:cd05122   1 LFEILEKIGKGGFGEVYKARHKRtGKEVA------IKVIKL---ESKEKKEKIINEIQILKKCKHPNIVKYYGSYLKKDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 249 KYLAMELVHGQDLEKRIYATGPVIPSQAIAW-MIQTCDILDYLHSQEqpLIHRDIKPANLMVKTaNNQIAVLDFGAVKEI 327
Cdd:cd05122  72 LWIVMEFCSGGSLKDLLKSTNQTLTESQIAYvCKELLKGLEYLHSNG--IIHRDIKAANILLTS-DGEVKLIDFGLSAQL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 328 GTTPG--TRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPF-KFYRQKGrgfRFDVSKIP--------TVTP 395
Cdd:cd05122 149 SDTKArnTMVGTPYWMAPEVINGKPYDyKADIWSLGITAIELAEGKPPYsELPPMKA---LFKIATNGppglrnpeKWSD 225
                       250
                ....*....|....*..
gi 75906578 396 KLRDVIERTTEPLPRDR 412
Cdd:cd05122 226 EFKDFLKKCLQKNPEKR 242
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
171-412 1.17e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 109.57  E-value: 1.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKAQELfEREAYTLKSLNHSGIPKYYDFFVEGGKK- 249
Cdd:cd06606   2 WTRGELLGRGSFGSVYLALD-----KDTGELMAVKSVELSGDSEEELEAL-EREIRILSSLQHPNIVRYYGSERDEEKNt 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 -YLAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEIG 328
Cdd:cd06606  76 lNIFLEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNG--IVHRDIKGANILV-DSDGVVKLADFGCAKRLG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 329 TTP-----GTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPfkFYRQKGR-------GFRFDVSKIPT-VT 394
Cdd:cd06606 153 DIEtgegtGSVRGTPYWMAPEVIRGEEYGrAADIWSLGCTVIEMATGKPP--WSELGNPmaalykiGSSGEPPEIPEhLS 230
                       250
                ....*....|....*...
gi 75906578 395 PKLRDVIERTTEPLPRDR 412
Cdd:cd06606 231 EEAKDFLRKCLRRDPKKR 248
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
170-373 4.12e-25

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. 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. 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.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 102.33  E-value: 4.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDA-AGVIVGHPKLLVLKQMNADMARIakaqelfEREAYTLKSLNHSGIPKYYDFFVEGGK 248
Cdd:cd06627   1 NYQLGDLIGRGAFGVVYKGLNLeTGDFVAIKQISLEKIKEEALKSI-------MQEIDLLKNLKHPNIVKYIGSIETSDS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 249 KYLAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHsqEQPLIHRDIKPANLMVkTANNQIAVLDFGAVKEIG 328
Cdd:cd06627  74 LYIILEYAENGSLRQIIKKFGPFPESLVAVYVYQVLQGLAYLH--EQGVIHRDIKAANILT-TKDGVVKLADFGVATKLN 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75906578 329 TTPGTRIGAEG---YCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPF 373
Cdd:cd06627 151 DVSKDDASVVGtpyWMAPEVIEMSGASTaSDIWSLGCTVIELLTGNPPY 199
STKc_FA2-like cd08529
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii FA2 and ...
171-412 1.11e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii FA2 and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii FA2-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes FA2 and CNK4. The Nek 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. 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.


Pssm-ID: 173771 [Multi-domain]  Cd Length: 256  Bit Score: 98.35  E-value: 1.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAwdaagVIVGHPKLLVLKQMN-ADMARIAKAQELfeREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd08529   2 FEILNKIGKGSFGVVFKV-----VRKADKRVYAMKQIDlSKMNRREREEAI--DEARVLAKLDSSYIIRYYESFLDKGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLAMELVHGQDLEKRIYA-TGPVIPSQAIaW--MIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKE 326
Cdd:cd08529  75 NIVMEYAENGDLHKLLKMqRGRPLPEDQV-WrfFIQILLGLAHLHSKK--ILHRDIKSLNLFL-DAYDNVKIGDLGVAKL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 327 IGTT---PGTRIGAEGYCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPFKFYRQKGRGFRFDVSKIPTV----TPKLR 398
Cdd:cd08529 151 LSDNtnfANTIVGTPYYLSPELCEDKPYNEkSDVWALGVVLYECCTGKHPFDANNQGALILKIIRGVFPPVsqmySQQLA 230
                       250
                ....*....|....
gi 75906578 399 DVIERTTEPLPRDR 412
Cdd:cd08529 231 QLIDQCLTKDYRQR 244
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
171-412 3.24e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 5; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 5 (Nek5) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek5 subfamily is one of a family of 11 different Neks (Nek1-11). The Nek 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. 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.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 94.25  E-value: 3.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDAAgvivgHPKLLVLKQMNADMARIaKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKKY 250
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKS-----DSEHCVIKEIDLTKMPV-KEKEASKKEVILLAKMKHPNIVTFFASFQENGRLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 251 LAMELVHGQDLEKRIYATGPVIPS--QAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVL-DFGAVKEI 327
Cdd:cd08225  76 IVMEYCDGGDLMKRINRQRGVLFSedQILSWFVQISLGLKHIHDRK--ILHRDIKSQNIFL-SKNGMVAKLgDFGIARQL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 328 GTT---PGTRIGAEGYCAPEQERGQPL-TQSDLYAIGPTIIFLLTGENPFkfyrqKGRGFRFDVSKI---------PTVT 394
Cdd:cd08225 153 NDSmelAYTCVGTPYYLSPEICQNRPYnNKTDIWSLGCVLYELCTLKHPF-----EGNNLHQLVLKIcqgyfapisPNFS 227
                       250
                ....*....|....*...
gi 75906578 395 PKLRDVIERTTEPLPRDR 412
Cdd:cd08225 228 RDLRSLISQLFKVSPRDR 245
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
177-418 4.00e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK that 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. 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.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 94.03  E-value: 4.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLAWDAagvivGHPKLLVLKQMNADMARiAKAQEL---FEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAM 253
Cdd:cd06632   8 LGSGSFGSVYEGLNL-----DDGDFFAVKEVSLADDG-QTGQEAvkqLEQEIALLSKLQHPNIVQYLGTEREEDNLYIFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 254 ELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVKTaNNQIAVLDFGAVKEIGTTPGT 333
Cdd:cd06632  82 ELVPGGSLAKLLKKYGSFPEPVIRLYTRQILLGLEYLHDRN--TVHRDIKGANILVDT-NGVVKLADFGMAKQVVEFSFA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 334 R--IGAEGYCAPE--QERGQPLTQSDLYAIGPTIIFLLTGENPFKFYRQKGRGFRFDVSK----IP-TVTPKLRDVIERT 404
Cdd:cd06632 159 KsfKGSPYWMAPEviAQQGGYGLAADIWSLGCTVLEMATGKPPWSQLEGVAAVFKIGRSKelppIPdHLSDEAKDFILKC 238
                       250
                ....*....|....
gi 75906578 405 TEPLPRDRfQSAKE 418
Cdd:cd06632 239 LQRDPSLR-PTAAE 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
170-418 5.30e-22

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 93.81  E-value: 5.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLA---WDAagvivghpKLLVLKQMNADMaRIAKAQELfEREAYTLKSLNHSGIPKYYDFFVEG 246
Cdd:cd06623   2 DLERVKVLGQGSSGVVYKVrhkPTG--------KIYALKKIHVDG-DEEFRKQL-LRELKTLRSCESPYVVKCYGAFYKE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 247 GKKYLAMELVHGQDLEKRIYATGPvIPSQAIAWM-IQTCDILDYLHSQEQpLIHRDIKPANLMVkTANNQIAVLDFGAVK 325
Cdd:cd06623  72 GEISIVLEYMDGGSLADLLKKVGK-IPEPVLAYIaRQILKGLDYLHTKRH-IIHRDIKPSNLLI-NSKGEVKIADFGISK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 326 EIGTTPG---TRIGAEGYCAPEQERGQPL-TQSDLYAIGPTIIFLLTGENPFKFYRQKgrGF--------RFDVSKIP-- 391
Cdd:cd06623 149 VLENTLDqcnTFVGTVTYMSPERIQGESYsYAADIWSLGLTLLECALGKFPFLPPGQP--SFfelmqaicDGPPPSLPae 226
                       250       260
                ....*....|....*....|....*..
gi 75906578 392 TVTPKLRDVIERTTEPLPRDRfQSAKE 418
Cdd:cd06623 227 EFSPEFRDFISACLQKDPKKR-PSAAE 252
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
171-373 3.91e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii Never In Mitosis gene A (NIMA)-related kinase 1 (CNK2)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii CNK2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173772 [Multi-domain]  Cd Length: 256  Bit Score: 90.97  E-value: 3.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDAAgvivgHPKLLVLKQMN-ADMARIAKAQELfeREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLS-----DNQFYALKEVDlGSMSQKEREDAV--NEIRILASVNHPNIISYKEAFLDGNKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLAMELVHGQDLEKRI---YATGPVIPSQAIaW--MIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAV 324
Cdd:cd08530  75 CIVMEYAPFGDLSKAIskrKKKRKLIPEQEI-WriFIQLLRGLQALHEQK--ILHRDLKSANILL-VANDLVKIGDLGIS 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75906578 325 KEI-GTTPGTRIGAEGYCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPF 373
Cdd:cd08530 151 KVLkKNMAKTQIGTPHYMAPEVWKGRPYSYkSDIWSLGCLLYEMATFAPPF 201
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
170-379 1.99e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 2; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 2 (Nek2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173757 [Multi-domain]  Cd Length: 265  Bit Score: 89.23  E-value: 1.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKAQELFErEAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRR-----KSDGKILVWKEIDYGNMTEKEKQQLVS-EVNILRELKHPNIVRYYDRIIDRSNQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 --YLAMELVHGQDLE---KRIYATGPVIPSQAIaW--MIQTCDILDYLHSQEQP---LIHRDIKPANLMVKTANNqIAVL 319
Cdd:cd08217  75 tlYIVMEYCEGGDLAqliQKCKKERKYIEEEFI-WriLTQLLLALYECHNRSDPgntVLHRDLKPANIFLDANNN-VKLG 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75906578 320 DFGAVKEIGTT---PGTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPFKFYRQK 379
Cdd:cd08217 153 DFGLAKILGHDssfAKTYVGTPYYMSPEQLNHMSYDeKSDIWSLGCLIYELCALSPPFTARNQL 216
STKc_MEKK3_like cd06625
Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine ...
177-418 2.20e-19

Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3-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. This subfamily is composed of MEKK3, MEKK2, and related proteins, all containing an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks), proteins that 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. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132956 [Multi-domain]  Cd Length: 263  Bit Score: 86.40  E-value: 2.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKAQEL--FEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAME 254
Cdd:cd06625  10 LGQGAFGRVYLCYD-----VDTGRELAVKQVPFDPDSPETKKEVnaLECEIQLLKNLQHERIVQYYGCLRDDETLSIFME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 255 LVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVKTANNqIAVLDFGAVKEI------G 328
Cdd:cd06625  85 YMPGGSVKDQLKAYGALTETVTRKYTRQILEGVEYLHSNM--IVHRDIKGANILRDSAGN-VKLGDFGASKRLqticssG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 329 TTPGTRIGAEGYCAPEQERGQPL-TQSDLYAIGPTIIFLLTGENPFKFYrqKGRGFRFDVSKIPT-------VTPKLRDV 400
Cdd:cd06625 162 TGMKSVTGTPYWMSPEVISGEGYgRKADVWSVGCTVVEMLTEKPPWAEF--EAMAAIFKIATQPTnpqlpshVSPDARNF 239
                       250
                ....*....|....*...
gi 75906578 401 IERTTEPLPRDRfQSAKE 418
Cdd:cd06625 240 LRRTFVENAKKR-PSAEE 256
STKc_Nek6_Nek7 cd08224
Catalytic domain of the Protein Serine/Threonine Kinases, Never In Mitosis gene A-related ...
168-412 2.30e-19

Catalytic domain of the Protein Serine/Threonine Kinases, Never In Mitosis gene A-related kinase 6 and 7; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 6 (Nek6) and Nek7 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek6/7 subfamily 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173764 [Multi-domain]  Cd Length: 267  Bit Score: 86.33  E-value: 2.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 168 IRHYQVLRTLGQGGMGTTYLA---WDaaGVIVGHPKLLVLKQMNAdmariaKAQELFEREAYTLKSLNHSGIPKYYDFFV 244
Cdd:cd08224   1 LGNFKIEKKIGKGQFSVVYKAiclLD--GRVVALKKVQIFEMMDA------KARQDCLKEIDLLKQLDHPNVIKYLASFI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 245 EGGKKYLAMELVHGQDLEKRIYAT---GPVIPSQAI-AWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLD 320
Cdd:cd08224  73 ENNELNIVLELADAGDLSRMIKHFkkqKRLIPERTIwKYFVQLCSALEHMHSKR--IMHRDIKPANVFI-TATGVVKLGD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 321 FGA---VKEIGTTPGTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPfkFYRQKGRGFRF-------DVSK 389
Cdd:cd08224 150 LGLgrfFSSKTTAAHSLVGTPYYMSPERIHENGYNfKSDIWSLGCLLYEMAALQSP--FYGDKMNLYSLckkiekcDYPP 227
                       250       260
                ....*....|....*....|....*
gi 75906578 390 IPT--VTPKLRDVIERTTEPLPRDR 412
Cdd:cd08224 228 LPAdhYSEELRDLVSRCINPDPEKR 252
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
171-412 7.39e-19

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 84.70  E-value: 7.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKAQELfEREAYTLKSLNHSGIPKYYDFFVEGGKKY 250
Cdd:cd06626   2 WQRGNKIGGGTFGKVYTAVN-----LDTGELMAVKEIRIQDNDPKTIKEI-ADEMKVLELLKHPNLVKYYGVEVHREKVY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 251 LAMELVHGQDLEkRIYATGPVIPSQAI-AWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEI-- 327
Cdd:cd06626  76 IFMEYCSGGTLE-ELLEHGRILDEHVIrVYTLQLLEGLAYLHSHG--IVHRDIKPANIFL-DHNGVIKLGDFGCAVKLkn 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 328 -GTTPGTRI----GAEGYCAPEQERGQPLT----QSDLYAIGPTIIFLLTGENPFKFYRQK-------GRGFRFDVSKIP 391
Cdd:cd06626 152 nTTTMGEEVqslaGTPAYMAPEVITGGKGKghgrAADIWSLGCVVLEMATGKRPWSELDNEfqimfhvGAGHKPPIPDSL 231
                       250       260
                ....*....|....*....|.
gi 75906578 392 TVTPKLRDVIERTTEPLPRDR 412
Cdd:cd06626 232 QLSPEGKDFLDRCLESDPKKR 252
PKc_MAPKK_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity MAP kinase kinases; Protein kinases (PKs) ...
174-373 8.66e-19

Catalytic domain of fungal Pek1-like dual-specificity MAP kinase kinases; Protein kinases (PKs), MAP kinase kinase(MAPKK) subfamily, fungal Pek1-like proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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 the MAPK Pmk1/Spm1 and is regulated by the MAPKKK Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKKK Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis.


Pssm-ID: 132952 [Multi-domain]  Cd Length: 287  Bit Score: 84.79  E-value: 8.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 174 LRTLGQGGMGTTYLAWDAAGvivghPKLLVLKQMNADMARIAKAQELfeREAYTLKSLNHSGIPKYYDFFVE--GGKKYL 251
Cdd:cd06621   6 LSRLGEGAGGSVTKCRLKNT-----GMIFALKTITTDPNPDLQKQIL--RELEINKSCKSPYIVKYYGAFLDesSSSIGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 252 AMELVHGQDLE---KRIYATGPVIpSQAIAWMIQTCDI--LDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKE 326
Cdd:cd06621  79 AMEYCEGGSLDsiyKKVKKRGGRI-GEKVLGKIAESVLkgLSYLHSRK--IIHRDIKPSNILL-TRKGQVKLCDFGVSGE 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75906578 327 IGTT-PGTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPF 373
Cdd:cd06621 155 LVNSlAGTFTGTSFYMAPERIQGKPYSiTSDVWSLGLTLLEVAQNRFPF 203
STKc_Nek10 cd08528
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
171-373 1.01e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 10; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 10 (Nek10) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek10 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173770 [Multi-domain]  Cd Length: 269  Bit Score: 84.48  E-value: 1.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDAAGvivgHPKLLVLKQMNadMARIAKAQELFEREA----------YTLKSLNHSGIPKYY 240
Cdd:cd08528   2 YAVLEHLGSGAFGCVYKVRKKNN----GQNLLALKEIN--VHNPAFGKDKRERDKsigdivsevtIIKEQLRHPNIVRYY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 241 DFFVEGGKKYLAMELVHGQDL---------------EKRIYATgpvipsqaiawMIQTCDILDYLHsQEQPLIHRDIKPA 305
Cdd:cd08528  76 KTFLENDRLYIVMDLIEGAPLgehfnslkekkqrftEERIWNI-----------FVQMVLALRYLH-KEKRIVHRDLTPN 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75906578 306 NLMVkTANNQIAVLDFGAVKEIGTTP--GTRIGAEGYCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPF 373
Cdd:cd08528 144 NIML-GEDDKVTITDFGLAKQKQPESklTSVVGTILYSCPEIVKNEPYGEkADVWAFGCILYQMCTLQPPF 213
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
177-417 1.10e-18

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 84.11  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLAwdaagVIVGHPKLLVLKQMNADMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAMELV 256
Cdd:cd05123   1 LGKGSFGKVLLV-----RKKDTGKLYAMKVLKKKKIIKRKEVEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVLEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 257 HGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEI---GTTPGT 333
Cdd:cd05123  76 PGGELFSHLSKEGRFSEERARFYAAEIVLALEYLHSLG--IIYRDLKPENILL-DADGHIKLTDFGLAKELsseGSRTNT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 334 RIGAEGYCAPEQERGQPLTQS-DLYAIGpTIIF-LLTGENPFkFYRQKGRGFRfdvsKI--------PTVTPKLRDVIER 403
Cdd:cd05123 153 FCGTPEYLAPEVLLGKGYGKAvDWWSLG-VLLYeMLTGKPPF-YAEDRKEIYE----KIlkdplrfpEFLSPEARDLISG 226
                       250
                ....*....|....
gi 75906578 404 TTEPLPRDRFQSAK 417
Cdd:cd05123 227 LLQKDPTKRLGSGG 240
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ...
171-344 1.47e-18

Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), CMGC family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC 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. 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 similar proteins. 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.


Pssm-ID: 143333 [Multi-domain]  Cd Length: 283  Bit Score: 83.92  E-value: 1.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDA-AGVIVGHPKLLvLKQMNADMARIAKaqelfeREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd05118   1 YQKLGKIGEGTYGVVYKARDKlTGEIVAIKKIK-LRFESEGIPKTAL------REIKLLKELNHPNIIKLLDVFRHKGDL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLAMELVHgQDLEKRIYATGPVIPSQAI-AWMIQTCDILDYLHSQEqpLIHRDIKPANLMVKTaNNQIAVLDFGAVKEIG 328
Cdd:cd05118  74 YLVFEFMD-TDLYKLIKDRQRGLPESLIkSYLYQLLQGLAFCHSHG--ILHRDLKPENLLINT-EGVLKLADFGLARSFG 149
                       170
                ....*....|....*....
gi 75906578 329 TTPGT---RIGAEGYCAPE 344
Cdd:cd05118 150 SPVRPythYVVTRWYRAPE 168
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine ...
170-412 3.33e-18

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 1 (MEKK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK1 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK1 activates the extracellular signal-regulated kinase 1/2 (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.


Pssm-ID: 132961 [Multi-domain]  Cd Length: 268  Bit Score: 82.99  E-value: 3.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNADMARIAKAQELFE---REAYTLKSLNHSGIPKYYDFFVEG 246
Cdd:cd06630   1 EWLKGQQLGTGAFSSCYQARD-----VKTGTLMAVKQVTYVRNTSSEQEEVVEalrKEIRLMARLNHPHIIRMLGATCED 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 247 GKKYLAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHsqEQPLIHRDIKPANLMVKTANNQIAVLDFGAVKE 326
Cdd:cd06630  76 SHFNLFVEWMAGGSVSHLLSKYGAFKEAVIINYTEQLLRGLSYLH--ENQIIHRDVKGANLLIDSTGQRLRIADFGAAAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 327 IGTT-------PGTRIGAEGYCAPEQERGQPLTQS-DLYAIGPTIIFLLTGENPFKFYRQKGR-GFRFDVS------KIP 391
Cdd:cd06630 154 LAAKgtgagefQGQLLGTIAFMAPEVLRGEQYGRScDVWSVGCVIIEMATAKPPWNAEKHSNHlALIFKIAsattapSIP 233
                       250       260
                ....*....|....*....|..
gi 75906578 392 T-VTPKLRDVIERTTEPLPRDR 412
Cdd:cd06630 234 EhLSPGLRDVTLRCLELQPEDR 255
STKc_Nek4 cd08223
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
171-412 4.78e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 4; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 4 (Nek4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek4 subfamily is one of a family of 11 different Neks (Nek1-11). The Nek 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. 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 highly abundant in the testis. Its specific function is unknown.


Pssm-ID: 173763 [Multi-domain]  Cd Length: 257  Bit Score: 82.33  E-value: 4.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLawdaagviVGH---PKLLVLKQMNADMARiAKAQELFEREAYTLKSLNHSGIPKYYDFFV-EG 246
Cdd:cd08223   2 YCFVRVVGKGSYGEVSL--------VRHrtdGKQYVIKKLNLRNAS-RRERKAAEQEAQLLSQLKHPNIVAYRESWEgED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 247 GKKYLAMELVHGQDLEKRIY-ATGPVIP-SQAIAWMIQTCDILDYLHsqEQPLIHRDIKPANLMVkTANNQIAVLDFGAV 324
Cdd:cd08223  73 GLLYIVMGFCEGGDLYHKLKeQKGKLLPeNQVVEWFVQIAMALQYLH--EKHILHRDLKTQNVFL-TRTNIIKVGDLGIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 325 KEIGT---TPGTRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPFKFYRQKGRGFRFDVSKIPTV----TPK 396
Cdd:cd08223 150 RVLENqcdMASTLIGTPYYMSPELFSNKPYNyKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMpkdySPE 229
                       250
                ....*....|....*.
gi 75906578 397 LRDVIERTTEPLPRDR 412
Cdd:cd08223 230 LGELIATMLSKRPEKR 245
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
177-373 8.73e-18

Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cGMP-dependent protein kinase (cGK or PKG) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 81.51  E-value: 8.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 177 LGQGGMGTTYLawdaagVIV-GHPKLLVLKQMNADMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKKYLAMEL 255
Cdd:cd05572   1 LGVGGFGRVEL------VKVkSKNRTFALKCVKKRHIVETGQQEHIFSEKEILEECNHPFIVKLYRTFKDKKYIYMLMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 256 VHGQDLEKRIYATGPVIPSQA---IAWMIQtcdILDYLHSQEqpLIHRDIKPANLMVKTaNNQIAVLDFGAVKEIGTTPG 332
Cdd:cd05572  75 CLGGELWTILRDRGLFDEYTArfyIACVVL---AFEYLHNRG--IIYRDLKPENLLLDS-NGYVKLVDFGFAKKLKSGQK 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75906578 333 TR--IGAEGYCAPEQERGQPLTQS-DLYAIGPTIIFLLTGENPF 373
Cdd:cd05572 149 TWtfCGTPEYVAPEIILNKGYDFSvDYWSLGILLYELLTGRPPF 192
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
171-374 1.00e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 3; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 3 (Nek3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek3 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 81.17  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDaagviVGHPKLLVLKQMNadMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKKY 250
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQH-----VNSDQKYAMKEIR--LPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 251 LAMELVHGQDLEKRI-YATGPVIPSQAI-AWMIQTCDILDYLHsqEQPLIHRDIKPANLMVkTANNQIAVLDFGAVKeIG 328
Cdd:cd08219  75 IVMEYCDGGDLMQKIkLQRGKLFPEDTIlQWFVQMCLGVQHIH--EKRVLHRDIKSKNIFL-TQNGKVKLGDFGSAR-LL 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75906578 329 TTPG----TRIGAEGYCAPEQERGQPL-TQSDLYAIGPTIIFLLTGENPFK 374
Cdd:cd08219 151 TSPGayacTYVGTPYYVPPEIWENMPYnNKSDIWSLGCILYELCTLKHPFQ 201
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
170-376 1.19e-17

Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; Serine/threonine kinases (STKs), oxidative stress response kinase (OSR1) and Ste20-related proline alanine-rich kinase (SPAK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 81.25  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDAAGVIVGHPKLLVLKQMNADMARIAKaqelferEAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd06610   2 DYELIEVIGVGATAVVYAAICLPNNEKVAIKRIDLEKCQTSVDELRK-------EVQAMSQCNHPNVVKYYTSFVVGDEL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLAMELVHG---QDLEKRIYATGpVIPSQAIAWMI-QTCDILDYLHSQEQplIHRDIKPANLMVkTANNQIAVLDFGAVK 325
Cdd:cd06610  75 WLVMPYLSGgslLDIMKSSYPRG-GLDEAIIATVLkEVLKGLEYLHSNGQ--IHRDIKAGNILL-GEDGSVKIADFGVSA 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75906578 326 EIgTTPGTR--------IGAEGYCAPE---QERGQPLtQSDLYAIGPTIIFLLTGENPFKFY 376
Cdd:cd06610 151 SL-ADGGDRtrkvrktfVGTPCWMAPEvmeQVHGYDF-KADIWSFGITAIELATGAAPYSKY 210
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
173-375 1.62e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. 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.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 80.82  E-value: 1.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 173 VLRTLGQGGMGTTYLAwdaagVIVGHPKLLVLKQMNADMARIAKAQELfeREAYTLKSLNHSGIPKYYDFFVEGGKKYLA 252
Cdd:cd06605   5 YLGELGAGNSGVVSKV-----LHRPTGKIMAVKTIRLEINEAIQKQIL--RELDILHKCNSPYIVGFYGAFYNNGDISIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 253 MELVHGQDLEKRIYATGPVIPSQAIAWM-IQTCDILDYLHSQEQpLIHRDIKPANLMVkTANNQIAVLDFGAVKE-IGTT 330
Cdd:cd06605  78 MEYMDGGSLDKILKEVQGRIPERILGKIaVAVLKGLTYLHEKHK-IIHRDVKPSNILV-NSRGQIKLCDFGVSGQlVNSL 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75906578 331 PGTRIGAEGYCAPeqERGQPLT---QSDLYAIGPTIIFLLTGENPFKF 375
Cdd:cd06605 156 AKTFVGTSSYMAP--ERIQGNDysvKSDIWSLGLSLIELATGRFPYPP 201
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
171-410 1.69e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 81.09  E-value: 1.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWD-------AAGVIvghPKLLVLKQMNADMARIakaqelfEREAytLKSLN-HSGIPKYYDF 242
Cdd:cd05581   3 FKFGKIIGEGSFSTVVLAKEketnkeyAIKIL---DKRQLIKEKKVKYVKI-------EKEV--LTRLNgHPGIIKLYYT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 243 FVEGGKKYLAMELVHGQDLEK--RIYATGPVIPSQAIAwmIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLD 320
Cdd:cd05581  71 FQDEENLYFVLEYAPNGELLQyiRKYGSLDEKCTRFYA--AEILLALEYLHSKG--IIHRDLKPENILL-DKDMHIKITD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 321 FGAVKEIGTTP---------------------------GTrigAEgYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENP 372
Cdd:cd05581 146 FGTAKVLDPNSspesnkgdatnidsqieknrrrfasfvGT---AE-YVSPELLNEKPAGkSSDLWALGCIIYQMLTGKPP 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 75906578 373 FK-------FYRQKGRGFRFDvSKIPtvtPKLRDVIER--TTEPLPR 410
Cdd:cd05581 222 FRgsneyltFQKILKLEYSFP-PNFP---PDAKDLIEKllVLDPQDR 264
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
170-413 1.75e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs), Yank1 or STK32A subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily contains uncharacterized STKs with similarity to the human protein designated Yank1 or STK32A.


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 80.44  E-value: 1.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYlawdaagvIVGH---PKLLVLKQMN-ADMARIAKAQELFeREAYTLKSLNHSGIPKYYDFFVE 245
Cdd:cd05578   1 HFELLRVIGKGAFGKVC--------IVQKrdtKKMFAMKYMNkQKCVEKGSVRNVL-NERRILQELNHPFLVNLWYSFQD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 246 GGKKYLAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLM------VKTANNQIAVl 319
Cdd:cd05578  72 EENMYLVVDLLLGGDLRYHLSQKVKFSEEQVKFWICEIVLALEYLHSKG--IIHRDIKPDNILldeqghVHITDFNIAT- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 320 DFGAVKEIGTTPGTRigaeGYCAPEQERGQPLT-QSDLYAIGPTIIFLLTGENPFKFYRQKGRG--FRFDVSKIPTVTP- 395
Cdd:cd05578 149 KVTPDTLTTSTSGTP----GYMAPEVLCRQGYSvAVDWWSLGVTAYECLRGKRPYRGHSRTIRDqiRAKQETADVLYPAt 224
                       250       260
                ....*....|....*....|.
gi 75906578 396 ---KLRDVIERTTEPLPRDRF 413
Cdd:cd05578 225 wstEAIDAINKLLERDPQKRL 245
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
171-412 2.96e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 1; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 1 (Nek1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek1 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173758 [Multi-domain]  Cd Length: 256  Bit Score: 79.87  E-value: 2.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDAAgvivgHPKLLVLKQMNadMARIA-KAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd08218   2 YVKVKKIGEGSFGKAILVKSKE-----DGKQYVIKEIN--ISKMSpKEREESRKEVAVLSNMKHPNIVQYQESFEENGNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLAMELVHGQDLEKRIYATGPVIPS--QAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGAVKEI 327
Cdd:cd08218  75 YIVMDYCEGGDLYKKINAQRGVLFPedQILDWFVQICLALKHVHDRK--ILHRDIKSQNIFL-TKDGTIKLGDFGIARVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 328 GTT---PGTRIGAEGYCAPEQERGQPL-TQSDLYAIGPTIIFLLTGENPFKFYRQKGRGFRFDVSKIPTVTPK----LRD 399
Cdd:cd08218 152 NSTvelARTCIGTPYYLSPEICENRPYnNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVSSHysydLRN 231
                       250
                ....*....|...
gi 75906578 400 VIERTTEPLPRDR 412
Cdd:cd08218 232 LVSQLFKRNPRDR 244
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
170-368 5.87e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 9; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 9 (Nek9) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek9 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173761 [Multi-domain]  Cd Length: 256  Bit Score: 79.02  E-value: 5.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYL---AWDAAgvivghpkLLVLKQMNadMARIA-KAQELFEREAYTLKSLNHSGIPKYYDFFVE 245
Cdd:cd08221   1 HYIPIRVLGKGAFGEATLyrrTEDDS--------LVVWKEVN--LTRLSeKERRDALNEIVILSLLQHPNIIAYYNHFMD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 246 GGKKYLAMELVHGQDLEKRIYAT-GPVIPSQAIAW-MIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGA 323
Cdd:cd08221  71 DNTLLIEMEYANGGTLYDKIVRQkGQLFEEEMVLWyLFQIVSAVSYIHKAG--ILHRDIKTLNIFL-TKAGLIKLGDFGI 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75906578 324 VKEIGTTPG---TRIGAEGYCAPEQERGQPLT-QSDLYAIGPTIIFLLT 368
Cdd:cd08221 148 SKILGSEYSmaeTVVGTPYYMSPELCQGVKYNfKSDIWALGCVLYELLT 196
STKc_MEKK2 cd06652
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 2; Serine ...
170-403 7.36e-17

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 2; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 2 (MEKK2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK2 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132983 [Multi-domain]  Cd Length: 265  Bit Score: 78.92  E-value: 7.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 170 HYQVLRTLGQGGMGTTYLAWDAAgviVGHPKLLVLKQMNADMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDAD---TGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPMER 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLA--MELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVKTANNqIAVLDFGAVKEI 327
Cdd:cd06652  80 TLSifMEHMPGGSIKDQLKSYGALTENVTRKYTRQILEGVSYLHSNM--IVHRDIKGANILRDSVGN-VKLGDFGASKRL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 328 ------GTTPGTRIGAEGYCAPEQERGQPL-TQSDLYAIGPTIIFLLTGENPFKFYRQKGRGFRFDVSKI-----PTVTP 395
Cdd:cd06652 157 qticlsGTGMKSVTGTPYWMSPEVISGEGYgRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTnpvlpPHVSD 236

                ....*...
gi 75906578 396 KLRDVIER 403
Cdd:cd06652 237 HCRDFLKR 244
STKc_Nek6 cd08228
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
168-412 1.29e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 6; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 6 (Nek6) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek6 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173768 [Multi-domain]  Cd Length: 267  Bit Score: 78.14  E-value: 1.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 168 IRHYQVLRTLGQGGMGTTYLAwdaagVIVGHPKLLVLKQMNADMARIAKAQELFEREAYTLKSLNHSGIPKYYDFFVEGG 247
Cdd:cd08228   1 LANFQIEKKIGRGQFSEVYRA-----TCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 248 KKYLAMELVHGQDLEKRIY---ATGPVIPSQAI-AWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFGA 323
Cdd:cd08228  76 ELNIVLELADAGDLSQMIKyfkKQKRLIPERTVwKYFVQLCSAVEHMHSRR--VMHRDIKPANVFI-TATGVVKLGDLGL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 324 VKEIG---TTPGTRIGAEGYCAPEQ--ERGQPLtQSDLYAIGPTIIFLLTGENPfkFYRQKGRGFRF-------DVSKIP 391
Cdd:cd08228 153 GRFFSsktTAAHSLVGTPYYMSPERihENGYNF-KSDIWSLGCLLYEMAALQSP--FYGDKMNLFSLcqkieqcDYPPLP 229
                       250       260
                ....*....|....*....|...
gi 75906578 392 T--VTPKLRDVIERTTEPLPRDR 412
Cdd:cd08228 230 TehYSEKLRELVSMCIYPDPDQR 252
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
171-373 4.61e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 8; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 8 (Nek8) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek8 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173760 [Multi-domain]  Cd Length: 256  Bit Score: 76.43  E-value: 4.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWDAAGvivghPKLLVLKQMNAD-MARiaKAQELFEREAYTLKSLNHSGIPKYYDFFVEGGKK 249
Cdd:cd08220   2 YEKIRVVGRGAFGIVHLCRRKAD-----QKLVIIKQIPVEqMTK--DERLAAQNECQVLKLLSHPNIIEYYENFLEDKAL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 250 YLAMELVHGQDLEKRIYATG-PVIPSQAIA-WMIQTCDILDYLHSQEqpLIHRDIKPANLMVKTANNQIAVLDFGAVKEI 327
Cdd:cd08220  75 MIVMEYAPGGTLAEYIQKRCnSLLDEDTILhFFVQILLALHHVHTKL--ILHRDLKTQNILLDKHKMVVKIGDFGISKIL 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75906578 328 GTTPG--TRIGAEGYCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPF 373
Cdd:cd08220 153 SSKSKayTVVGTPCYISPELCEGKPYNQkSDIWALGCVLYELASLKRAF 201
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
238-412 5.96e-16

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 75.98  E-value: 5.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 238 KYYDFFVEGGKKYLAMELVHGQDLEKRIYATGPVIPSQAIAWMIQTCDILDYLHsqEQPLIHRDIKPANLMVkTANNQIA 317
Cdd:cd05611  61 KLYYSFQSKDYLYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLH--QRGIIHRDIKPENLLI-DQTGHLK 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 318 VLDFGaVKEIGTTPGTRIGAEGYCAPEQERGQPLTQ-SDLYAIGPTIIFLLTGENPFK-------FYRQKGRGFRFDVSK 389
Cdd:cd05611 138 LTDFG-LSRNGLENKKFVGTPDYLAPETILGVGDDKmSDWWSLGCVIFEFLFGYPPFHaetpdavFDNILSRRINWPEEV 216
                       170       180
                ....*....|....*....|...
gi 75906578 390 IPTVTPKLRDVIERTTEPLPRDR 412
Cdd:cd05611 217 KEFCSPEAVDLINRLLCMDPAKR 239
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine ...
171-322 6.27e-16

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase (CDK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK-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. 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.


Pssm-ID: 173733 [Multi-domain]  Cd Length: 282  Bit Score: 76.37  E-value: 6.27e-16
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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75906578 171 YQVLRTLGQGGMGTTYLAWD-AAGVIVghpkllVLKQMnadmaRIAKAQELFE----REAYTLKSLNHSGIPKYYDFFVE 245
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKARDkKTGEIV------ALKKI-----RLDNEEEGIPstalREISLLKELKHPNIVKLLDVIHT 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75906578 246 GGKKYLAMELVHgQDLEKRIYATGPVI-PSQAIAWMIQTCDILDYLHSQEqpLIHRDIKPANLMVkTANNQIAVLDFG 322