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Conserved domains on  [gi|113476931|ref|YP_722992|]
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serine/threonine protein kinase [Trichodesmium erythraeum IMS101]

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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 ...
20-210 1.55e-47

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: 165.10  E-value: 1.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  20 LGQGGFGTTYRAIYDQLNKIVVLKTLNeslhqHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMVMDYIPG 99
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIK-----KEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 100 QNLADLIQS-GHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFGITCDLTDGIKQTHANLF 178
Cdd:cd00180   76 GSLKDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSDKSLLKTIVG 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 113476931 179 SVGYSPPEQYNPQEKLSPSTDIYALTATLYYL 210
Cdd:cd00180  156 TPAYMAPEVLLGKGYYSEKSDIWSLGVILYEL 187
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-265 1.22e-50

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.03  E-value: 1.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931    14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNeslhqHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMV 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-----KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931    94 MDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTDFGITCDLTDGIKQT 173
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LDEDGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931   174 HanlfSVG---YSPPEQYNpQEKLSPSTDIYALTATLYYLLTGNIPTPAALRLSQTVpQTLKFSEKELKDILPNLSSNIE 250
Cdd:smart00220 155 T----FVGtpeYMAPEVLL-GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELF-KKIGKPKPPFPPPEWDISPEAK 228
                          250
                   ....*....|....*
gi 113476931   251 ETIVRGLAIDPQKRP 265
Cdd:smart00220 229 DLIRKLLVKDPEKRL 243
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
20-210 1.55e-47

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: 165.10  E-value: 1.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  20 LGQGGFGTTYRAIYDQLNKIVVLKTLNeslhqHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMVMDYIPG 99
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIK-----KEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 100 QNLADLIQS-GHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFGITCDLTDGIKQTHANLF 178
Cdd:cd00180   76 GSLKDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSDKSLLKTIVG 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 113476931 179 SVGYSPPEQYNPQEKLSPSTDIYALTATLYYL 210
Cdd:cd00180  156 TPAYMAPEVLLGKGYYSEKSDIWSLGVILYEL 187
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
64-168 1.23e-09

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine [Unknown function, General].


Pssm-ID: 234331  Cd Length: 199  Bit Score: 56.84  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931   64 AEAHLLANLRHpNIVN---VRDFFEEEQLffMVMDYIPGQNLADLIQSGHNlhpgqavNYIYQIASALSVVHKNGFLHRD 140
Cdd:TIGR03724  46 NEARLLSRARK-AGVNtpvVYDVDPDNKT--IVMEYIEGKPLKDVIEEGND-------ELLREIGRLVGKLHKAGIVHGD 115
                          90       100       110
                  ....*....|....*....|....*....|.
gi 113476931  141 IQPKNIIKRakSNTVVLTDFG---ITCDLTD 168
Cdd:TIGR03724 116 LTTSNIIVR--DDKLYLIDFGlgkYSDEIED 144
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
83-161 4.42e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 52.22  E-value: 4.42e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113476931  83 FFEEEQLFFMVMDYIPGQNLADLIQSGhnlhPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRakSNTVVLTDFG 161
Cdd:PRK14879  67 YFVDPENFIIVMEYIEGEPLKDLINSN----GMEELELSREIGRLVGKLHSAGIIHGDLTTSNMILS--GGKIYLIDFG 139
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
65-161 2.16e-07

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 49.97  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  65 EAHLLANLRHpNIVNVRDFFE-EEQLFFMVMDYIPGQNLADLIQSGhnlhpgqAVNYIYQIASALSVVHKNGFLHRDIQP 143
Cdd:COG3642   49 EARILAKARE-AGVPVPIVYDvDPDNGLIVMEYIEGELLKDALEEA-------RPDLLREVGRLVGKLHKAGIVHGDLTT 120
                         90
                 ....*....|....*...
gi 113476931 144 KNIIKRAKSntVVLTDFG 161
Cdd:COG3642  121 SNIILSGGR--IYFIDFG 136
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
14-265 1.22e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.03  E-value: 1.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931    14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNeslhqHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMV 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-----KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931    94 MDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTDFGITCDLTDGIKQT 173
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LDEDGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931   174 HanlfSVG---YSPPEQYNpQEKLSPSTDIYALTATLYYLLTGNIPTPAALRLSQTVpQTLKFSEKELKDILPNLSSNIE 250
Cdd:smart00220 155 T----FVGtpeYMAPEVLL-GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELF-KKIGKPKPPFPPPEWDISPEAK 228
                          250
                   ....*....|....*
gi 113476931   251 ETIVRGLAIDPQKRP 265
Cdd:smart00220 229 DLIRKLLVKDPEKRL 243
Pkinase pfam00069
Protein kinase domain;
14-265 3.17e-48

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 168.58  E-value: 3.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931   14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNeslhQHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMV 93
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILK----KRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931   94 MDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNI-IKraKSNTVVLTDFGITCDLTDGIKQ 172
Cdd:pfam00069  77 MEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENIlLD--ENGVVKIADFGLAKKLTKSSSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  173 THANLFSVGYSPPEQYNPQEKLSPSTDIYALTATLYYLLTGNIPTPAALRLSQ--TVPQTLKFSEKELKDILPNLSSNIE 250
Cdd:pfam00069 155 LTTFVGTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQlqLIRRILGPPLEFDEPKSDSGSEEAK 234
                         250
                  ....*....|....*
gi 113476931  251 ETIVRGLAIDPQKRP 265
Cdd:pfam00069 235 DLIKKCLNKDPSKRP 249
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
13-353 8.48e-41

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: 151.43  E-value: 8.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  13 KYIIHSILGQGGFGTTYRAiydQLNKIVVLKTLNeslHQHQDFAKFQRQFMAEAHLLANLRHP-NIVNVRDFFEEEQLFF 91
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLA---RDRKLVALKVLA---KKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  92 MVMDYIPGQNLADLIQSGH---NLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFGITCDLTD 168
Cdd:COG0515   75 LVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 169 GIKQTHANLF------SVGYSPPEQY--NPQEKLSPSTDIYALTATLYYLLTGNIPTPaALRLSQTVPQTLK-------- 232
Cdd:COG0515  155 PGSTSSIPALpstsvgTPGYMAPEVLlgLSLAYASSSSDIWSLGITLYELLTGLPPFE-GEKNSSATSQTLKiilelptp 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 233 -FSEKELKDILPNLSSNIEETIVRGLAIDPQKRPQTVEGWLVLLLNKSNILEvkKPNSCLTEKVSRFNNNDQLIMMKSES 311
Cdd:COG0515  234 sLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKE--SDLSDLLKPDDSAPLRLSLPPSLEAL 311
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 113476931 312 SVDLKRGNYCSNEVKSKTVKIKSLGSNKFDFFSPSDRDYKLS 353
Cdd:COG0515  312 ISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLL 353
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-269 5.23e-21

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 95.61  E-value: 5.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  12 GKYIIHSILGQGGFGTTYRAiYDQL-NKIVVLKTLNESLhqhQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLF 90
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLA-YDPVcSRRVALKKIREDL---SENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  91 FMVMDYIPGQNLADLIQS-------GHNLHPGQAV----NYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTD 159
Cdd:PRK13184  78 YYTMPYIEGYTLKSLLKSvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNIL-LGLFGEVVILD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 160 FGitcdLTDGIKQTHANLFSVGYSPPE----------------QYNPQEKL-----SPSTDIYALTATLYYLLTGNIPTP 218
Cdd:PRK13184 157 WG----AAIFKKLEEEDLLDIDVDERNicyssmtipgkivgtpDYMAPERLlgvpaSESTDIYALGVILYQMLTLSFPYR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 113476931 219 AALRLSQTVPQTLKFSEK--ELKDILPNLSsnieETIVRGLAIDPQKRPQTVE 269
Cdd:PRK13184 233 RKKGRKISYRDVILSPIEvaPYREIPPFLS----QIAMKALAVDPAERYSSVQ 281
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
40-213 4.70e-20

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: 92.99  E-value: 4.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931    40 VVLKTLNE-SLHQHQDFAKFQRqfmaEAHLLANLRHPNIVNVRDFFE-EEQLFFMVMDYIPGQNLADLIQSGHNLHPGQA 117
Cdd:TIGR03903    6 VAIKLLRTdAPEEEHQRARFRR----ETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931   118 VNYIYQIASALSVVHKNGFLHRDIQPKNIIKRA---KSNTVVLtDFGITCDLTDG-------IKQTHANLFSVGYSPPEQ 187
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQtgvRPHAKVL-DFGIGTLLPGVrdadvatLTRTTEVLGTPTYCAPEQ 160
                          170       180
                   ....*....|....*....|....*.
gi 113476931   188 YNpQEKLSPSTDIYALTATLYYLLTG 213
Cdd:TIGR03903  161 LR-GEPVTPNSDLYAWGLIFLECLTG 185
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
14-244 4.57e-16

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 78.92  E-value: 4.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  14 YIIHSILGQGGFGTTYRAI-YDQLNKIVVLKTLneslhqhQDFAKFQRQFMaeahLLANLRHPNIVNVRDFF-------E 85
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAIcIDTSEKVAIKKVL-------QDPQYKNRELL----IMKNLNHINIIFLKDYYytecfkkN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  86 EEQLFF-MVMDYIPG---QNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFG 161
Cdd:PTZ00036 137 EKNIFLnVVMEFIPQtvhKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKLCDFG 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 162 ITCDLTDGiKQTHANLFSVGYSPPEQYNPQEKLSPSTDIYALTATL------YYLLTGNIPTPAALRLSQTVPQTlkfSE 235
Cdd:PTZ00036 217 SAKNLLAG-QRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIaemilgYPIFSGQSSVDQLVRIIQVLGTP---TE 292

                 ....*....
gi 113476931 236 KELKDILPN 244
Cdd:PTZ00036 293 DQLKEMNPN 301
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
19-189 6.48e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 68.70  E-value: 6.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  19 ILGQGGFGTTYRAIYDQLNKIVVLKTLnesLHQHQDfaKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMVMDYIP 98
Cdd:PLN00034  81 RIGSGAGGTVYKVIHRPTGRLYALKVI---YGNHED--TVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  99 GQNLadliQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNtVVLTDFGITCDLTDGIKQTHANLF 178
Cdd:PLN00034 156 GGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN-VKIADFGVSRILAQTMDPCNSSVG 230
                        170
                 ....*....|.
gi 113476931 179 SVGYSPPEQYN 189
Cdd:PLN00034 231 TIAYMSPERIN 241
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
66-216 1.05e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 63.72  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  66 AHLLANlrHPNIVNVRDFFEEEQLFFMVMDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKN 145
Cdd:PHA03390  62 HQLMKD--NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLEN 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 146 IIKRAKSNTVVLTDFGI-----TCDLTDGikqTHanlfsVGYSPpeqynpqEKL-----SPSTDIYALTATLYYLLTGNI 215
Cdd:PHA03390 140 VLYDRAKDRIYLCDYGLckiigTPSCYDG---TL-----DYFSP-------EKIkghnyDVSFDWWAVGVLTYELLTGKH 204

                 .
gi 113476931 216 P 216
Cdd:PHA03390 205 P 205
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
20-210 1.55e-47

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: 165.10  E-value: 1.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  20 LGQGGFGTTYRAIYDQLNKIVVLKTLNeslhqHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMVMDYIPG 99
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIK-----KEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 100 QNLADLIQS-GHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFGITCDLTDGIKQTHANLF 178
Cdd:cd00180   76 GSLKDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSDKSLLKTIVG 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 113476931 179 SVGYSPPEQYNPQEKLSPSTDIYALTATLYYL 210
Cdd:cd00180  156 TPAYMAPEVLLGKGYYSEKSDIWSLGVILYEL 187
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
13-269 1.76e-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: 135.70  E-value: 1.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  13 KYIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESlhqhQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFM 92
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDLS----NMSEKEREDALNEVKILKKLNHPNIIKYYESFEEKGKLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  93 VMDYIPGQNLADLIQS----GHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTDFGITCDLTD 168
Cdd:cd08215   77 VMEYADGGDLSQKIKKqkkeGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIF-LTSNGLVKLGDFGISKVLSS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 169 giKQTHANLFsVG---YSPPE-----QYNpqEKlspsTDIYALTATLYYLLTGNIP----TPAALRlsqtvpqtLKFSEK 236
Cdd:cd08215  156 --TVDLAKTV-VGtpyYLSPElcqnkPYN--YK----SDIWSLGCVLYELCTLKHPfegeNLLELA--------LKILKG 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 113476931 237 ELKDILPNLSSNIEETIVRGLAIDPQKRPQTVE 269
Cdd:cd08215  219 QYPPIPSQYSSELRNLVSSLLQKDPEERPSIAQ 251
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
13-242 1.24e-33

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: 127.36  E-value: 1.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  13 KYIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNeslhQHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFM 92
Cdd:cd06627    1 NYQLGDLIGRGAFGVVYKGLNLETGDFVAIKQIS----LEKIKEEALKSIMQEIDLLKNLKHPNIVKYIGSIETSDSLYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  93 VMDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKrAKSNTVVLTDFGITCDLTDgikq 172
Cdd:cd06627   77 ILEYAENGSLRQIIKKFGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILT-TKDGVVKLADFGVATKLND---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 173 THANLFSVGYSP----PEQYNpQEKLSPSTDIYALTATLYYLLTGNIP------TPAALRLSQT----VPQTlkFSEkEL 238
Cdd:cd06627  152 VSKDDASVVGTPywmaPEVIE-MSGASTASDIWSLGCTVIELLTGNPPyydlnpMAALFRIVQDdhppLPEG--ISP-EL 227

                 ....
gi 113476931 239 KDIL 242
Cdd:cd06627  228 KDFL 231
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
10-265 1.18e-31

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: 121.89  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  10 QKGKyiihsILGQGGFGTTYRAIYDQLNKIVVLKTLNESlhqhQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFF--EEE 87
Cdd:cd06606    3 TRGE-----LLGRGSFGSVYLALDKDTGELMAVKSVELS----GDSEEELEALEREIRILSSLQHPNIVRYYGSErdEEK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  88 QLFFMVMDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNtVVLTDFGiTCDLT 167
Cdd:cd06606   74 NTLNIFLEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGV-VKLADFG-CAKRL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 168 DGIKQTHANLFSVG---YSPPEQYNpQEKLSPSTDIYALTATLYYLLTGNIPTPaalRLSQTVPQTLKFSE-KELKDILP 243
Cdd:cd06606  152 GDIETGEGTGSVRGtpyWMAPEVIR-GEEYGRAADIWSLGCTVIEMATGKPPWS---ELGNPMAALYKIGSsGEPPEIPE 227
                        250       260
                 ....*....|....*....|..
gi 113476931 244 NLSSNIEETIVRGLAIDPQKRP 265
Cdd:cd06606  228 HLSEEAKDFLRKCLRRDPKKRP 249
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
15-265 1.56e-27

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: 110.38  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  15 IIHSIlGQGGFGTTYRAIYDQLNKIVVLKTLNESLHQHQdfakfqRQFMAEAHLLANLRHPNIVNVRD-FFEEEQLFfMV 93
Cdd:cd05122    4 ILEKI-GKGGFGEVYKARHKRTGKEVAIKVIKLESKEKK------EKIINEIQILKKCKHPNIVKYYGsYLKKDELW-IV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  94 MDYIPGQNLADLIQSGHNLHPGQAVNYI-YQIASALSVVHKNGFLHRDIQPKNIIkrAKSNTVV-LTDFGITCDLTDGiK 171
Cdd:cd05122   76 MEFCSGGSLKDLLKSTNQTLTESQIAYVcKELLKGLEYLHSNGIIHRDIKAANIL--LTSDGEVkLIDFGLSAQLSDT-K 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 172 QTHANLFSVGYSPPEQYNpQEKLSPSTDIYALTATLYYLLTGNIP------TPAALRLSQTVPQTLKFSEK---ELKDIL 242
Cdd:cd05122  153 ARNTMVGTPYWMAPEVIN-GKPYDYKADIWSLGITAIELAEGKPPyselppMKALFKIATNGPPGLRNPEKwsdEFKDFL 231
                        250       260
                 ....*....|....*....|...
gi 113476931 243 PNLssnieetivrgLAIDPQKRP 265
Cdd:cd05122  232 KKC-----------LQKNPEKRP 243
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
14-269 3.88e-27

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: 109.07  E-value: 3.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  14 YIIHSILGQGGFG--TTYRAIYDqlNKIVVLKTLN-ESLHQHQdfakfQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLF 90
Cdd:cd08221    2 YIPIRVLGKGAFGeaTLYRRTED--DSLVVWKEVNlTRLSEKE-----RRDALNEIVILSLLQHPNIIAYYNHFMDDNTL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  91 FMVMDYIPGQNLADLI--QSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTDFGITCDLTD 168
Cdd:cd08221   75 LIEMEYANGGTLYDKIvrQKGQLFEEEMVLWYLFQIVSAVSYIHKAGILHRDIKTLNIF-LTKAGLIKLGDFGISKILGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 169 GIKQTHANLFSVGYSPPE-----QYNPQeklspsTDIYALTATLYYLLTGNiPTPAALRLSQTVpqtLKFSEKELKDILP 243
Cdd:cd08221  154 EYSMAETVVGTPYYMSPElcqgvKYNFK------SDIWALGCVLYELLTLK-RTFDATNPLNLV---VKIVQGNYTPVVS 223
                        250       260
                 ....*....|....*....|....*.
gi 113476931 244 NLSSNIEETIVRGLAIDPQKRPQTVE 269
Cdd:cd08221  224 VYSSELISLVHSLLQQDPEKRPTADE 249
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
18-269 2.82e-26

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: 106.91  E-value: 2.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  18 SILGQGGFGTTYRAIYDQLNKIVVLKTLNESlhqhqDFAKFQRQFMAEAHLLANLRHPNIVNVRD-FFEEEQLFFmVMDY 96
Cdd:cd06623    7 KVLGQGSSGVVYKVRHKPTGKIYALKKIHVD-----GDEEFRKQLLRELKTLRSCESPYVVKCYGaFYKEGEISI-VLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  97 IPGQNLADLIQSgHNLHPGQAVNYI-YQIASALSVVH-KNGFLHRDIQPKNIIKRAKSNtVVLTDFGITCDLTDGIKQTH 174
Cdd:cd06623   81 MDGGSLADLLKK-VGKIPEPVLAYIaRQILKGLDYLHtKRHIIHRDIKPSNLLINSKGE-VKIADFGISKVLENTLDQCN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 175 ANLFSVGYSPPEQYNPqEKLSPSTDIYALTATLYYLLTGNIPTPAALRLSQ-TVPQTLKFSEKelkdilPNLSSNI--EE 251
Cdd:cd06623  159 TFVGTVTYMSPERIQG-ESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFfELMQAICDGPP------PSLPAEEfsPE 231
                        250       260
                 ....*....|....*....|.
gi 113476931 252 T---IVRGLAIDPQKRPQTVE 269
Cdd:cd06623  232 FrdfISACLQKDPKKRPSAAE 252
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
14-264 2.88e-26

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: 106.63  E-value: 2.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESLHQHQDFAkfqRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMV 93
Cdd:cd05578    2 FELLRVIGKGAFGKVCIVQKRDTKKMFAMKYMNKQKCVEKGSV---RNVLNERRILQELNHPFLVNLWYSFQDEENMYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  94 MDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNtVVLTDFGITCDLTDGiKQT 173
Cdd:cd05578   79 VDLLLGGDLRYHLSQKVKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNILLDEQGH-VHITDFNIATKVTPD-TLT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 174 HANLFSVGYSPPEQYNPQeKLSPSTDIYALTATLYYLLTGNIPTPAALRLSQTvpQTLKFSEKELKDILPNLSSNIEETI 253
Cdd:cd05578  157 TSTSGTPGYMAPEVLCRQ-GYSVAVDWWSLGVTAYECLRGKRPYRGHSRTIRD--QIRAKQETADVLYPATWSTEAIDAI 233
                        250
                 ....*....|.
gi 113476931 254 VRGLAIDPQKR 264
Cdd:cd05578  234 NKLLERDPQKR 244
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
14-270 4.52e-26

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: 106.51  E-value: 4.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESL---HQHQDFAKFQRQFMaeaHLLAnlRHPNIVNVRDFFEEEQLF 90
Cdd:cd05581    3 FKFGKIIGEGSFSTVVLAKEKETNKEYAIKILDKRQlikEKKVKYVKIEKEVL---TRLN--GHPGIIKLYYTFQDEENL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  91 FMVMDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTDFGITCDLTDGI 170
Cdd:cd05581   78 YFVLEYAPNGELLQYIRKYGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENIL-LDKDMHIKITDFGTAKVLDPNS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 171 KQTHANLFSVGYSPPEQYNPQEK-------------------LSPSTDIYALTATLYYLLTGNIPTPAalrlsQTVPQTL 231
Cdd:cd05581  157 SPESNKGDATNIDSQIEKNRRRFasfvgtaeyvspellnekpAGKSSDLWALGCIIYQMLTGKPPFRG-----SNEYLTF 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 113476931 232 KFSEKELKDILPNLSSNIEETIVRGLAIDPQKRPQTVEG 270
Cdd:cd05581  232 QKILKLEYSFPPNFPPDAKDLIEKLLVLDPQDRLGVNEG 270
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
20-264 2.46e-25

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: 104.14  E-value: 2.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  20 LGQGGFGTTYRAIYDQLNKIVVLKTLN-ESLHQHQDfakfQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMVMDYIP 98
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLKkKKIIKRKE----VEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVLEYAP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  99 GQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNtVVLTDFGITCDLTDGIKQTHANLF 178
Cdd:cd05123   77 GGELFSHLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGH-IKLTDFGLAKELSSEGSRTNTFCG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 179 SVGYSPPEQYNpQEKLSPSTDIYALTATLYYLLTGNIPTPAAlRLSQTVPQTLKfseKELKdILPNLSSNIEETIVRGLA 258
Cdd:cd05123  156 TPEYLAPEVLL-GKGYGKAVDWWSLGVLLYEMLTGKPPFYAE-DRKEIYEKILK---DPLR-FPEFLSPEARDLISGLLQ 229

                 ....*.
gi 113476931 259 IDPQKR 264
Cdd:cd05123  230 KDPTKR 235
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
13-269 4.64e-25

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: 103.48  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  13 KYIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESLHQHQDfakfQRQFMAEAHLLANLRHPNIVNV--RDFFEEEQLF 90
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGNMTEKE----KQQLVSEVNILRELKHPNIVRYydRIIDRSNQTL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  91 FMVMDYIPGQNLADLIQSGHNLH---PGQAVNYIY-QIASALSVVH-----KNGFLHRDIQPKNIIKRAKsNTVVLTDFG 161
Cdd:cd08217   77 YIVMEYCEGGDLAQLIQKCKKERkyiEEEFIWRILtQLLLALYECHnrsdpGNTVLHRDLKPANIFLDAN-NNVKLGDFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 162 ITCDLTDGIKQTHAnlfSVG---YSPPEQYNpQEKLSPSTDIYALTATLYYLLTGNIPTPAAlrlSQTVPQTlKFSEKEL 238
Cdd:cd08217  156 LAKILGHDSSFAKT---YVGtpyYMSPEQLN-HMSYDEKSDIWSLGCLIYELCALSPPFTAR---NQLQLAS-KIKEGKF 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 113476931 239 KDILPNLSSNIEETIVRGLAIDPQKRPQTVE 269
Cdd:cd08217  228 RRIPYRYSSELNEVIKSMLNVDPDKRPSTEE 258
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
13-265 1.82e-24

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: 101.57  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  13 KYIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESLHQHQDFAKFQRQFMaeahLLANLRHPNIVNVRDFFEEEQLFFM 92
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVI----LLAKMKHPNIVTFFASFQENGRLFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  93 VMDYIPGQNLADLIQSGHNL--HPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFGITCDLTDGI 170
Cdd:cd08225   77 VMEYCDGGDLMKRINRQRGVlfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGIARQLNDSM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 171 KQTHANLFSVGYSPPE--QYNPQEKlspSTDIYALTATLYYLLTGNIPTPAAlRLSQTVpqtLKFSEKELKDILPNLSSN 248
Cdd:cd08225  157 ELAYTCVGTPYYLSPEicQNRPYNN---KTDIWSLGCVLYELCTLKHPFEGN-NLHQLV---LKICQGYFAPISPNFSRD 229
                        250
                 ....*....|....*..
gi 113476931 249 IEETIVRGLAIDPQKRP 265
Cdd:cd08225  230 LRSLISQLFKVSPRDRP 246
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine ...
14-265 1.19e-22

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


Pssm-ID: 173734 [Multi-domain]  Cd Length: 283  Bit Score: 96.83  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESLHQHQDFAKfqrqfMAEAHLLANL-RHPNIVNVRDFFEEEQLFFM 92
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMN-----LREVKSLRKLnEHPNIVKLKEVFRENDELYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  93 VMDYIPGqNLADLIQS--GHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKrAKSNTVVLTDFGIT------C 164
Cdd:cd07830   76 VFEYMEG-NLYQLMKDrkGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV-SGPEVVKIADFGLAreirsrP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 165 DLTDgikqthanlfSVG---YSPPEQYNPQEKLSPSTDIYAL---TATLYYL------------------LTGNiPT--- 217
Cdd:cd07830  154 PYTD----------YVStrwYRAPEILLRSTSYSSPVDIWALgciMAELYTLrplfpgsseidqlykicsVLGT-PTkqd 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 113476931 218 -PAALRLSQTVPQTL-KFSEKELKDILPNLSSNIEETIVRGLAIDPQKRP 265
Cdd:cd07830  223 wPEGYKLASKLGFRFpQFAPTSLHQLIPNASPEAIDLIKDMLRWDPKKRP 272
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
14-265 1.31e-22

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: 96.36  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  14 YIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLN-ESLHQHQdfakfQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFM 92
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQFYALKEVDlGSMSQKE-----REDAVNEIRILASVNHPNIISYKEAFLDGNKLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  93 VMDYIPGQNLADLIQSGH---NLHPGQAV-NYIYQIASALSVVHKNGFLHRDIQPKNIIkRAKSNTVVLTDFGITCDLTD 168
Cdd:cd08530   77 VMEYAPFGDLSKAISKRKkkrKLIPEQEIwRIFIQLLRGLQALHEQKILHRDLKSANIL-LVANDLVKIGDLGISKVLKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 169 GIKQTHanlfsVG---YSPPEQYNPQEKLSPStDIYALTATLYYLLTGNIPTPA--ALRLSQTVpQTLKFSEkelkdILP 243
Cdd:cd08530  156 NMAKTQ-----IGtphYMAPEVWKGRPYSYKS-DIWSLGCLLYEMATFAPPFEArsMQDLRYKV-QRGKYPP-----IPP 223
                        250       260
                 ....*....|....*....|..
gi 113476931 244 NLSSNIEETIVRGLAIDPQKRP 265
Cdd:cd08530  224 IYSQDLQNFIRSMLQVKPKLRP 245
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; Serine ...
12-265 2.21e-21

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-dependent protein kinase like (CDKL) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDKL subfamily is part of a 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. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory.


Pssm-ID: 143338 [Multi-domain]  Cd Length: 288  Bit Score: 93.15  E-value: 2.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  12 GKYIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNESlhqhQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFF 91
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKES----EDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  92 MVMDYIPgQNLADLIQSGHNLHPGQAVN-YIYQIASALSVVHKNGFLHRDIQPKNIIKrAKSNTVVLTDFGITCDLTDGI 170
Cdd:cd07833   77 LVFEYVE-RTLLELLEASPGGLPPDAVRsYIWQLLQAIAYCHSHNIIHRDIKPENILV-SESGVLKLCDFGFARALRARP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 171 KQTHANLFSVG-YSPPEQYNPQEKLSPSTDIYALTATLYYLLTGN----------------------IPTPAALRLSQTV 227
Cdd:cd07833  155 ASPLTDYVATRwYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEplfpgdsdidqlyliqkclgplPPSHQELFSSNPR 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 113476931 228 PQTLKF---SEKE-LKDILPNLSSNIEETIVRG-LAIDPQKRP 265
Cdd:cd07833  235 FAGVAFpepSQPEsLERRYPGKVSSPALDFLKAcLRMDPKERL 277
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
20-265 2.54e-21

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, 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. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which also contains an insert relative to MAST kinases like MASTL. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 92.70  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  20 LGQGGFGTTYRAIYDQLNKIVVLKTLNeslhqhqdFAKFQR-----QFMAEAHLLANLRHPNIVNVRDFFEEEQLFFMVM 94
Cdd:cd05579    1 ISKGAYGRVFLAKKKSTGDIYAIKVIK--------KADMIRknqvdQVLTERDILSQAQSPYVVKLYYSFQGKKNLYLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  95 DYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKrAKSNTVVLTDFGI--------TCDL 166
Cdd:cd05579   73 EYLPGGDLASLLENVGSLDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNILI-DSNGHLKLTDFGLskvglvrrQINL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 167 TDGIKQTHANLFSVGYSPPEQYNPQeKLSPSTDIYALTATLYYLLTGNIP----TPAALrLSQTVPQTLKFSEKelkdil 242
Cdd:cd05579  152 NDDEKEDKRIVGTPDYIAPEVILGQ-GHSKTVDWWSLGCILYEFLVGIPPfhgeTPEEI-FQNILNGKIEWPED------ 223
                        250       260
                 ....*....|....*....|...
gi 113476931 243 PNLSSNIEETIVRGLAIDPQKRP 265
Cdd:cd05579  224 VEVSDEAIDLISKLLVPDPEKRL 246
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
13-269 8.14e-21

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: 91.07  E-value: 8.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  13 KYIIHSILGQGGFGTTYRAIYDQLNKIVVLKTLNeslhQHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQLFFM 92
Cdd:cd08220    1 KYEKIRVVGRGAFGIVHLCRRKADQKLVIIKQIP----VEQMTKDERLAAQNECQVLKLLSHPNIIEYYENFLEDKALMI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  93 VMDYIPGQNLADLIQSGHN--LHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIKRAKSNTVVLTDFGITCDLTDGI 170
Cdd:cd08220   77 VMEYAPGGTLAEYIQKRCNslLDEDTILHFFVQILLALHHVHTKLILHRDLKTQNILLDKHKMVVKIGDFGISKILSSKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 171 KqTHANLFSVGYSPPE-----QYNPQeklspsTDIYALTATLYYLLTGNIPTPAAlRLSQTVpqtLKFSEKELKDILPNL 245
Cdd:cd08220  157 K-AYTVVGTPCYISPElcegkPYNQK------SDIWALGCVLYELASLKRAFEAA-NLPALV---LKIMSGTFAPISDRY 225
                        250       260
                 ....*....|....*....|....
gi 113476931 246 SSNIEETIVRGLAIDPQKRPQTVE 269
Cdd:cd08220  226 SPDLRQLILSMLNLDPSKRPQLSQ 249
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
10-269 1.01e-20

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: 90.94  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  10 QKGKYIihsilGQGGFGTTYRAIYDQLNKIVVLKTLNeSLHQHQDFAKFQRQFMAEAHLLANLRHPNIVNVRDFFEEEQL 89
Cdd:cd06632    3 RKGELL-----GSGSFGSVYEGLNLDDGDFFAVKEVS-LADDGQTGQEAVKQLEQEIALLSKLQHPNIVQYLGTEREEDN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931  90 FFMVMDYIPGQNLADLIQSGHNLHPGQAVNYIYQIASALSVVHKNGFLHRDIQPKNIIkrAKSNTVV-LTDFGITcdltd 168
Cdd:cd06632   77 LYIFLELVPGGSLAKLLKKYGSFPEPVIRLYTRQILLGLEYLHDRNTVHRDIKGANIL--VDTNGVVkLADFGMA----- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113476931 169 giKQTHANLF--SVGYSP----PEQYNPQEKLSPSTDIYALTATLYYLLTGNIPtpaalrLSQTVPQTLKF---SEKELK 239
Cdd:cd06632  150 --KQVVEFSFakSFKGSPywmaPEVIAQQGGYGLAADIWSLGCTVLEMATGKPP------WSQLEGVAAVFkigRSKELP 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 113476931 240 DILPNLSSNIEETIVRGLAIDPQKRPQTVE 269
Cdd:cd06632  222 PIPDHLSDEAKDFILKCLQRDPSLRPTAAE 251
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; Protein Tyrosine Kinase (PTK) ...
9-225 1.79e-20

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; Protein Tyrosine Kinase (PTK) family; Abelson (Abl) kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) tyr kinase that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl is normally inactive and requires phosphorylation and myristoylation for activation. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders.


Pssm-ID: 173633 [Multi-domain]  Cd Length: 263  Bit Score: 90.29  E-value: 1.79e-20