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Conserved domains on  [gi|15899909|ref|NP_344514|]
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Ser/thr protein kinase [Sulfolobus solfataricus P2]

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List of domain hits

Name Accession Description Interval E-value
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
241-332 2.11e-07

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 49.30  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 241 LIELGWHYVNKRKFEEAVKYFEEAVKRVPTFHNLLLY-AWSLIGNERYREALEVIEKAEKIK-RNAGSAYIKGLALEGLN 318
Cdd:cd00189   3 LLNLGNLYYKLGDYDEALEYYEKALELDPDNADAYYNlAAAYYKLGKYEEALEDYEKALELDpDNAKAYYNLGLAYYKLG 82
                        90
                ....*....|....
gi 15899909 319 APSQAEREFLYACR 332
Cdd:cd00189  83 KYEEALEAYEKALE 96
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
365-609 1.97e-33

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 128.86  E-value: 1.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYT----FIEMLY-EVAKMQEISkrSEYLVKIFASFLDENwtdyf 437
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARdtLLGRPVAIKVLRPELAedeeFRERFLrEARALARLS--HPNIVRVYDVGEDDG----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 438 ssPPAIIMEYMEGGDLRSILvdQEYSALrhsvkWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNIlfnkklprygeda 517
Cdd:cd14014  74 --RPYIVMEYVEGGSLADLL--RERGPL-----PPREALRILAQIADALAAAHRAGIVHRDIKPANI------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 lnsLLNFEVVPKLSDLGSSVKIGTPVMH------YTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPF------- 584
Cdd:cd14014 132 ---LLTEDGRVKLTDFGIARALGDSGLTqtgsvlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdgdspaa 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15899909 585 --------------------PEWLENEIEEAV-KNPEKRKQALDDF 609
Cdd:cd14014 209 vlakhlqeappppsplnpdvPPALDAIILRALaKDPEERPQSAAEL 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
366-648 4.02e-30

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 119.56  E-value: 4.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    366 YEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYT--FIEMLY-EVAKMQEIskRSEYLVKIFASFLDENwtDYFssp 440
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARdkKTGKLVAIKVIKKKKIkkDRERILrEIKILKKL--KHPNIVRLYDVFEDED--KLY--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    441 paIIMEYMEGGDLRSILvdQEYSALRhsvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlprygedalNS 520
Cdd:smart00220  74 --LVMEYCEGGDLFDLL--KKRGRLS-----EDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDED---------GH 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    521 LlnfevvpKLSDLGSSVKIGTPVMHY----TPYYAHP----LQRFGNRAetmfDVYSFSVSLYVSLTNNFPFPEwlENEI 592
Cdd:smart00220 136 V-------KLADFGLARQLDPGEKLTtfvgTPEYMAPevllGKGYGKAV----DIWSLGVILYELLTGKPPFPG--DDQL 202
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    593 EEAVKNPEKRKQALDDFHnatprlDYVPAEFKDLITmglkgeiSMLEIN--KRL--EEIL 648
Cdd:smart00220 203 LELFKKIGKPKPPFPPPE------WDISPEAKDLIR-------KLLVKDpeKRLtaEEAL 249
Apc3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
250-324 5.61e-07

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


:

Pssm-ID: 257383 [Multi-domain]  Cd Length: 81  Bit Score: 48.04  E-value: 5.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15899909   250 NKRKFEEAVKYFEEAVKRVPTFHNLLLYAWSLIGNERYREALEVIEKAEKIKRNAGSAYIKGLALEGLNAPSQAE 324
Cdd:pfam12895   1 DQHNYKNAIFLAEKLLALTPSNEDAYLLAQCYFLQGQYKRAYELLRKLKLNNSSLGCRYLLAQCLLKLKKYDEAI 75
 
Name Accession Description Interval E-value
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
241-332 2.11e-07

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 49.30  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 241 LIELGWHYVNKRKFEEAVKYFEEAVKRVPTFHNLLLY-AWSLIGNERYREALEVIEKAEKIK-RNAGSAYIKGLALEGLN 318
Cdd:cd00189   3 LLNLGNLYYKLGDYDEALEYYEKALELDPDNADAYYNlAAAYYKLGKYEEALEDYEKALELDpDNAKAYYNLGLAYYKLG 82
                        90
                ....*....|....
gi 15899909 319 APSQAEREFLYACR 332
Cdd:cd00189  83 KYEEALEAYEKALE 96
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
365-609 1.97e-33

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 128.86  E-value: 1.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYT----FIEMLY-EVAKMQEISkrSEYLVKIFASFLDENwtdyf 437
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARdtLLGRPVAIKVLRPELAedeeFRERFLrEARALARLS--HPNIVRVYDVGEDDG----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 438 ssPPAIIMEYMEGGDLRSILvdQEYSALrhsvkWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNIlfnkklprygeda 517
Cdd:cd14014  74 --RPYIVMEYVEGGSLADLL--RERGPL-----PPREALRILAQIADALAAAHRAGIVHRDIKPANI------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 lnsLLNFEVVPKLSDLGSSVKIGTPVMH------YTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPF------- 584
Cdd:cd14014 132 ---LLTEDGRVKLTDFGIARALGDSGLTqtgsvlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdgdspaa 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15899909 585 --------------------PEWLENEIEEAV-KNPEKRKQALDDF 609
Cdd:cd14014 209 vlakhlqeappppsplnpdvPPALDAIILRALaKDPEERPQSAAEL 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
366-648 4.02e-30

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 119.56  E-value: 4.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    366 YEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYT--FIEMLY-EVAKMQEIskRSEYLVKIFASFLDENwtDYFssp 440
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARdkKTGKLVAIKVIKKKKIkkDRERILrEIKILKKL--KHPNIVRLYDVFEDED--KLY--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    441 paIIMEYMEGGDLRSILvdQEYSALRhsvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlprygedalNS 520
Cdd:smart00220  74 --LVMEYCEGGDLFDLL--KKRGRLS-----EDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDED---------GH 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    521 LlnfevvpKLSDLGSSVKIGTPVMHY----TPYYAHP----LQRFGNRAetmfDVYSFSVSLYVSLTNNFPFPEwlENEI 592
Cdd:smart00220 136 V-------KLADFGLARQLDPGEKLTtfvgTPEYMAPevllGKGYGKAV----DIWSLGVILYELLTGKPPFPG--DDQL 202
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909    593 EEAVKNPEKRKQALDDFHnatprlDYVPAEFKDLITmglkgeiSMLEIN--KRL--EEIL 648
Cdd:smart00220 203 LELFKKIGKPKPPFPPPE------WDISPEAKDLIR-------KLLVKDpeKRLtaEEAL 249
Apc3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
250-324 5.61e-07

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


Pssm-ID: 257383 [Multi-domain]  Cd Length: 81  Bit Score: 48.04  E-value: 5.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15899909   250 NKRKFEEAVKYFEEAVKRVPTFHNLLLYAWSLIGNERYREALEVIEKAEKIKRNAGSAYIKGLALEGLNAPSQAE 324
Cdd:pfam12895   1 DQHNYKNAIFLAEKLLALTPSNEDAYLLAQCYFLQGQYKRAYELLRKLKLNNSSLGCRYLLAQCLLKLKKYDEAI 75
Pkinase pfam00069
Protein kinase domain;
366-648 1.52e-28

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 115.04  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909   366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEYTFIEMLYEVAKMQEISKR--SEYLVKIFASFLDENWtdyfsspP 441
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHkgTGKIVAVKILKKRSEKSKKDQTARREIRILRRlsHPNIVRLIDAFEDKDH-------L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909   442 AIIMEYMEGGDLRSILvdQEYSALRhsvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLprygedalnsl 521
Cdd:pfam00069  74 YLVMEYCEGGDLFDYL--SRGGPLS-----EDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENG----------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909   522 lnfevVPKLSDLGSSVKIGTPVMHY-----TPYYAHP-LQRFGNRAETMFDVYSFSVSLYVSLTNNFPFPEwlENEIEEA 595
Cdd:pfam00069 136 -----VVKIADFGLAKKLTKSSSSLttfvgTPEYMAPeVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSG--ESILDQL 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15899909   596 VKNPEKRKqalDDFHNATPRLDYVPAEFKDLITmglkgeiSMLEIN--KRL--EEIL 648
Cdd:pfam00069 209 QLIRRILG---PPLEFDEPKSDSGSEEAKDLIK-------KCLNKDpsKRPtaEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
365-665 6.64e-24

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: 103.28  E-value: 6.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVERNgKKYAMKVMKKEYT----FIEMLYEVAKMQEISKRSEYLVKIFASFLDENwtdyfssP 440
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR-KLVALKVLAKKLEskskEVERFLREIQILASLNHPPNIVKLYDFFQDEG-------S 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 441 PAIIMEYMEGGDLRSILvDQEYSALRHSvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPRYgedalnS 520
Cdd:COG0515  73 LYLVMEYVDGGSLEDLL-KKIGRKGPLS---ESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVV------K 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 521 LLNFEVVPKLSDLGSSVKIG--TPVMHYTPYYAHPLQRFGNRAETMF---DVYSFSVSLYVSLTNNFPFP-EWLENEIEE 594
Cdd:COG0515 143 LIDFGLAKLLPDPGSTSSIPalPSTSVGTPGYMAPEVLLGLSLAYASsssDIWSLGITLYELLTGLPPFEgEKNSSATSQ 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15899909 595 AVKNPEKRKQALDDFHNATPRLDYVPAEFKDLITmglkgeiSMLEINKRLEEILVEDYNIDINNLNSEAEK 665
Cdd:COG0515 223 TLKIILELPTPSLASPLSPSNPELISKAASDLLK-------KLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
pknD PRK13184
serine/threonine-protein kinase; Reviewed
366-584 5.24e-09

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 58.24  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  366 YEVKQLLGNGGMGYVLLV--ERNGKKYAMKVMKKEYTFIEMLYevakmqeisKRSEYLVKIFASFLDENWTDYFS----- 438
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAydPVCSRRVALKKIREDLSENPLLK---------KRFLREAKIAADLIHPGIVPVYSicsdg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  439 SPPAIIMEYMEGGDLRSIL--VDQEYSALRHSVKWPQVVAL--IFSKIAKAVIEVHKEGYTHCDIKPSNILFNKklprYG 514
Cdd:PRK13184  75 DPVYYTMPYIEGYTLKSLLksVWQKESLSKELAEKTSVGAFlsIFHKICATIEYVHSKGVLHRDLKPDNILLGL----FG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  515 E-------DALNSLLNFEV-----VPKLSDLGSSVKIGTPVMHyTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNF 582
Cdd:PRK13184 151 EvvildwgAAIFKKLEEEDlldidVDERNICYSSMTIPGKIVG-TPDYMAPERLLGVPASESTDIYALGVILYQMLTLSF 229

                 ..
gi 15899909  583 PF 584
Cdd:PRK13184 230 PY 231
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
354-509 1.17e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 55.98  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  354 DATAWlsyVLYGYEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEyTFIEM------LYEVAKMQEISKrsEYLVKIF 425
Cdd:PTZ00263  11 DTSSW---KLSDFEMGETLGTGSFGRVRIAKHkgTGEYYAIKCLKKR-EILKMkqvqhvAQEKSILMELSH--PFIVNMM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  426 ASFLDENWTdYFssppaiIMEYMEGGDLrsilvdqeYSALRHSVKWPQVVALIFS-KIAKAVIEVHKEGYTHCDIKPSNI 504
Cdd:PTZ00263  85 CSFQDENRV-YF------LLEFVVGGEL--------FTHLRKAGRFPNDVAKFYHaELVLAFEYLHSKDIIYRDLKPENL 149

                 ....*
gi 15899909  505 LFNKK 509
Cdd:PTZ00263 150 LLDNK 154
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
443-644 3.75e-06

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 47.54  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  443 IIMEYMEGGDLRSILVDQEysALRHsvkwpQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPRYgedalnsll 522
Cdd:PHA03390  86 LIMDYIKDGDLFDLLKKEG--KLSE-----AEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDRI--------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909  523 nfevvpKLSDLGSSVKIGTPVMHY-TPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPFPEWLENEIEeaVKNPEK 601
Cdd:PHA03390 150 ------YLCDYGLCKIIGTPSCYDgTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELD--LESLLK 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15899909  602 RKQalddfhNATPRLDYVPAEFKDLITmglkgeiSMLE--INKRL 644
Cdd:PHA03390 222 RQQ------KKLPFIKNVSKNANDFVQ-------SMLKynINYRL 253
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
224-308 5.85e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 38.53  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909   224 VKLLIDSVKMLPTYDAPLIELGWHYVnKRKFEEAVKYFEEAVKRVPTFHNLL-LYAWSLIGNERYREALEVIEKAEKIKR 302
Cdd:TIGR02917 790 IKHYQTVVKKAPDNAVVLNNLAWLYL-ELKDPRALEYAERALKLAPNIPAILdTLGWLLVEKGEADRALPLLRKAVNIAP 868

                  ....*.
gi 15899909   303 NAGSAY 308
Cdd:TIGR02917 869 EAAAIR 874
 
Name Accession Description Interval E-value
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
241-332 2.11e-07

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 49.30  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 241 LIELGWHYVNKRKFEEAVKYFEEAVKRVPTFHNLLLY-AWSLIGNERYREALEVIEKAEKIK-RNAGSAYIKGLALEGLN 318
Cdd:cd00189   3 LLNLGNLYYKLGDYDEALEYYEKALELDPDNADAYYNlAAAYYKLGKYEEALEDYEKALELDpDNAKAYYNLGLAYYKLG 82
                        90
                ....*....|....
gi 15899909 319 APSQAEREFLYACR 332
Cdd:cd00189  83 KYEEALEAYEKALE 96
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
365-609 1.97e-33

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 128.86  E-value: 1.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYT----FIEMLY-EVAKMQEISkrSEYLVKIFASFLDENwtdyf 437
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARdtLLGRPVAIKVLRPELAedeeFRERFLrEARALARLS--HPNIVRVYDVGEDDG----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 438 ssPPAIIMEYMEGGDLRSILvdQEYSALrhsvkWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNIlfnkklprygeda 517
Cdd:cd14014  74 --RPYIVMEYVEGGSLADLL--RERGPL-----PPREALRILAQIADALAAAHRAGIVHRDIKPANI------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 lnsLLNFEVVPKLSDLGSSVKIGTPVMH------YTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPF------- 584
Cdd:cd14014 132 ---LLTEDGRVKLTDFGIARALGDSGLTqtgsvlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdgdspaa 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15899909 585 --------------------PEWLENEIEEAV-KNPEKRKQALDDF 609
Cdd:cd14014 209 vlakhlqeappppsplnpdvPPALDAIILRALaKDPEERPQSAAEL 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
372-602 1.04e-24

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 102.73  E-value: 1.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVER--NGKKYAMKVMKKEYT---FIEMLYEVAKMQEIskRSEYLVKIFASFLDENWTdyfssppAIIME 446
Cdd:cd00180   1 LGKGSFGKVYKARDkeTGKKVAVKVIPKEKLkklLEELLREIEILKKL--NHPNIVKLYDVFETENFL-------YLVME 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 447 YMEGGDLRSILVdqeysalRHSVKWPQVVAL-IFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLprygedalnsllnfe 525
Cdd:cd00180  72 YCEGGSLKDLLK-------ENKGPLSEEEALsILRQLLSALEYLHSNGIIHRDLKPENILLDSDG--------------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 526 vVPKLSDLGSSVKIGTPVMHY-------TPYYAHPLQRFGNRAETMFDVYSFSVSLYvsltnnfpfpewlenEIEEA--- 595
Cdd:cd00180 130 -TVKLADFGLAKDLDSDDSLLkttggttPPYYAPPELLGGRYYGPKVDIWSLGVILY---------------ELEELkdl 193
                       250
                ....*....|..
gi 15899909 596 -----VKNPEKR 602
Cdd:cd00180 194 irrmlQYDPKKR 205
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
366-644 2.51e-22

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 96.78  E-value: 2.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKE---YTFIEMLY-EVAKMQEISKrsEYLVKIFASFLDEnwtDYFSs 439
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHkkTGEEYAVKIIDKKklkSEDEEMLRrEIEILKRLDH--PNIVKLYEVFEDD---KNLY- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 440 ppaIIMEYMEGGDLRSILVDQE-YSAlrhsvkwpQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPrygedal 518
Cdd:cd05117  76 ---LVMELCTGGELFDRIVKKGsFSE--------REAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDP------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 519 NSLLnfevvpKLSDLGSSVKIG-TPVMH---YTPYYAHP--LQRFGNRAETmfDVYSFSVSLYVSLTNNFPFPEWLENEI 592
Cdd:cd05117 138 DSPI------KIIDFGLAKIFEeGEKLKtvcGTPYYVAPevLKGKGYGKKC--DIWSLGVILYILLCGYPPFYGETEQEL 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15899909 593 EEAVKNpekrkqalDDFHNATPRLDYVPAEFKDLITmglkgeiSMLEIN--KRL 644
Cdd:cd05117 210 FEKILK--------GKYSFDSPEWKNVSEEAKDLIK-------RLLVVDpkKRL 248
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
366-540 5.80e-19

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 87.34  E-value: 5.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVERN--GKKYAMKVMKKEytfiEMLyevaKMQEIS-----------KRSEYLVKIFASFLDEN 432
Cdd:cd05573   3 FEVIKVIGRGAFGEVWLVRDKdtGQVYAMKILRKS----DML----KREQIAhvraerdiladADSPWIVRLHYAFQDED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 433 WTdYFssppaiIMEYMEGGDLRSILVDQEysalRHSVKWPQvvaLIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlpr 512
Cdd:cd05573  75 HL-YL------VMEYMPGGDLMNLLIKYD----VFPEETAR---FYIAELVLALDSLHKLGFIHRDIKPDNILLDAD--- 137
                       170       180
                ....*....|....*....|....*...
gi 15899909 513 yGEdalnsllnfevvPKLSDLGSSVKIG 540
Cdd:cd05573 138 -GH------------IKLADFGLCTKMN 152
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
366-648 6.02e-18

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 83.34  E-value: 6.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLV--ERNGKKYAMKVMKKEYTFIEMLYEVAKMQEISK--RSEYLVKIFASFLDENwtDYFsspp 441
Cdd:cd14003   2 YELGKTLGEGSFGKVKLArhKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKllNHPNIIKLYEVIETEN--KIY---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 442 aIIMEYMEGGDLRSILVD----QEYSALRhsvkwpqvvalIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKklprygeda 517
Cdd:cd14003  76 -LVMEYASGGELFDYIVNngrlSEDEARR-----------FFQQLISAVDYCHSNGIVHRDLKLENILLDK--------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 lnsllNFEVvpKLSDLGSSVKIGTPVMHYT----PYYAHP--LQRFGNRAEtMFDVYSFSVSLYVSLTNNFPFpewlene 591
Cdd:cd14003 135 -----NGNL--KIIDFGLSNEFRGGSLLKTfcgtPAYAAPevLLGRKYDGP-KADVWSLGVILYAMLTGYLPF------- 199
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15899909 592 ieEAVKNPEKRKQALddfhNATPRL-DYVPAEFKDLITmglkgeiSMLEIN--KR--LEEIL 648
Cdd:cd14003 200 --DDDNDSKLFRKIL----KGKYPIpSHLSPDARDLIR-------RMLVVDpsKRitIEEIL 248
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
372-603 7.07e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 83.27  E-value: 7.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLV---ERNGKkYAMKVMKKEYTFIEMLYEVAKMQEISKR--SEYLVKIFASFldeNWTDYFSsppaIIME 446
Cdd:cd13978   1 LGSGGFGTVSKArhvSWFGM-VAIKCLHSSPNCIEERKALLKEAEKMERarHSYVLPLLGVC---VERRSLG----LVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 447 YMEGGDLRSILvdqeySALRHSVKWPqVVALIFSKIAKAVIEVH--KEGYTHCDIKPSNILFNKklprygedalnsllNF 524
Cdd:cd13978  73 YMENGSLKSLL-----EREIQDVPWS-LRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDN--------------HF 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 525 EVvpKLSDLGSSV----------KIGTPVMHYTPYYAHP--LQRFGNRAETMFDVYSFSVSLYVSLTNNFPFPewleNEI 592
Cdd:cd13978 133 HV--KISDFGLSKlgmksisanrRRGTENLGGTPIYMAPeaFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFE----NAI 206
                       250
                ....*....|.
gi 15899909 593 EEAVKNPEKRK 603
Cdd:cd13978 207 NPLLIMQIVSK 217
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
372-583 1.43e-17

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 82.37  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVE--RNGKKYAMKVMKKEYT-FIEMLYEVAKMQEISKrSEYLVKIFAsfldenwtDYFSSPPAII--ME 446
Cdd:cd13987   1 LGEGTYGKVLLAVhkGSGTKMALKFVPKPSTkLKDFLREYNISLELSV-HPHIIKTYD--------VAFETEDYYVfaQE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 447 YMEGGDLRSILVDQeysalrhsVKWPQ-VVALIFSKIAKAVIEVHKEGYTHCDIKPSNIL-FNKklprygedalnsllNF 524
Cdd:cd13987  72 YAPYGDLFSIIPPQ--------VGLPEeRVKRCAAQLASALDFMHSKNLVHRDIKPENVLlFDK--------------DC 129
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15899909 525 EVVpKLSDLGSSVKIGTPV--MHYT-PYYAHPL------QRFgnRAETMFDVYSFSVSLYVSLTNNFP 583
Cdd:cd13987 130 RRV-KLCDFGLTRRVGSTVkrVSGTiPYTAPEVceakknEGF--VVDPSIDVWAFGVLLFCCLTGNFP 194
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
367-585 6.89e-17

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 80.33  E-value: 6.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 367 EVKQLLGNGGMGYVLLV--ERNGKKYAMKVmkkeytfIEMLYEVAKMQEISK--------RSEYLVKIFASFLDEnwtdy 436
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVrhKPTGKIYALKK-------IHVDGDEEFRKQLLRelktlrscESPYVVKCYGAFYKE----- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 437 fsSPPAIIMEYMEGGDLRSILVDQEysalrhsvKWP-QVVALIFSKIAKAVIEVHKEGY-THCDIKPSNILFNKKlpryG 514
Cdd:cd06623  72 --GEISIVLEYMDGGSLADLLKKVG--------KIPePVLAYIARQILKGLDYLHTKRHiIHRDIKPSNLLINSK----G 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15899909 515 EdalnsllnfevvPKLSDLG-SSVKIGTPVMHY----TPYYAHPlQRFGNRAETM-FDVYSFSVSLYVSLTNNFPFP 585
Cdd:cd06623 138 E------------VKIADFGiSKVLENTLDQCNtfvgTVTYMSP-ERIQGESYSYaADIWSLGLTLLECALGKFPFL 201
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
374-553 4.07e-16

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 78.03  E-value: 4.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 374 NGGMGYVLLVERN--GKKYAMKVMKKEYTFIEMLYEVAKMQE---ISKRSEYLVKIFASFLDENwTDYFssppaiIMEYM 448
Cdd:cd05579   3 RGAYGRVYLAKKKstGDLYAIKVIKKRDMIRKNQVDSVLAERnilSQAQNPFVVKLYYSFQGKK-NLYL------VMEYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 449 EGGDLRSILvdQEYSALRHSVkwpqvVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNK----KLPRYG--EDALNSLL 522
Cdd:cd05579  76 PGGDLYSLL--ENVGALDEDV-----ARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAnghlKLTDFGlsKVGLVRRQ 148
                       170       180       190
                ....*....|....*....|....*....|.
gi 15899909 523 NFEVVPKLSDLGSSVKIGTPVMhyTPYYAHP 553
Cdd:cd05579 149 IKLSIQKKSNGAPEKEDRRIVG--TPDYLAP 177
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
366-602 9.65e-16

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 76.47  E-value: 9.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLV--ERNGKKYAMKVMK----KEYTFIemLYEVAKMQEISkrSEYLVKIFASFL--DENWtdyf 437
Cdd:cd05122   2 FEILEKIGKGGFGVVYKArhKKTGQIVAIKKINleskEKKESI--LNEIAILKKCK--HPNIVKYYGSYLkkDELW---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 438 ssppaIIMEYMEGGDLRSILvdqeySALRHSVKwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNkklprygeda 517
Cdd:cd05122  74 -----IVMEFCSGGSLKDLL-----KNTNKTLT-EQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLT---------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 lnslLNFEVvpKLSDLGSSVKI--GTPVMHY--TPYYAHPLQRFGNRAETMFDVYSFSVS-------------------L 574
Cdd:cd05122 133 ----SDGEV--KLIDFGLSAQLsdGKTRNTFvgTPYWMAPEVIQGKPYGFKADIWSLGITaiemaegkppyselppmkaL 206
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15899909 575 YVSLTNNFPF---PEWLENEIEEAV-----KNPEKR 602
Cdd:cd05122 207 FLIATNGPPGlrnPKKWSKEFKDFLkkclqKDPEKR 242
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
366-586 1.05e-14

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 73.58  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLV--ERNGKKYAMKVMKKEYTFIEMLYEVAKMQEISKRSEYLVKIFASFL--DENWtdyFSSPP 441
Cdd:cd14084   8 YIMSRTLGSGACGEVKLAydKSTCKKVAIKIINKRKFTIGSRREINKPRNIETEIEILKKLSHPCIikIEDF---FDAED 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 442 A--IIMEYMEGGDLrsilvdqeYSALRHSVKWPQ-VVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlprygedal 518
Cdd:cd14084  85 DyyIVLELMEGGEL--------FDRVVSNKRLKEaICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQ--------- 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15899909 519 nsllNFEVVPKLSDLGSSVKIG-TPVMHY---TPYYAHP--LQRFGNRAET-MFDVYSFSVSLYVSLTNNFPFPE 586
Cdd:cd14084 148 ----EEECLIKITDFGLSKILGeTSLMKTlcgTPTYLAPevLRSFGTEGYTrAVDCWSLGVILFICLSGYPPFSE 218
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
372-644 1.43e-14

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 72.96  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVERNGKKYAMKVMKKEYT---FIEMLY-EVAKMQEIskRSEYLVKIFASFLDENwtdyfssPPAIIMEY 447
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDndeLLKEFRrEVSILSKL--RHPNIVQFIGACLSPP-------PLCIVTEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 448 MEGGDLRSILVDQeysalRHSVKWPQVVALIFSkIAKAVIEVHKEGYTHCDIKPSNILFNKklprygedalnsllnfEVV 527
Cdd:cd13999  72 MPGGSLYDLLHKK-----KIPLSWSLRLKIALD-IARGMNYLHSPPIIHRDLKSLNILLDE----------------NFT 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 528 PKLSDLG-SSVKIGTPVMH----YTPYYAHP----LQRFGNRAetmfDVYSFSVSLYVSLTNNFPFPEwleneieeavKN 598
Cdd:cd13999 130 VKIADFGlSRIKNSTTEKMtgvvGTPRWMAPevlrGEPYTEKA----DVYSFGIVLWELLTGEVPFKE----------LS 195
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15899909 599 PEKRKQALDDFHNATPRLDYVPAEFKDLITMGLKGEI----SMLEINKRL 644
Cdd:cd13999 196 PIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPekrpSFSEIVKRL 245
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
372-647 2.35e-14

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 72.31  E-value: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVE-RNGKKYAMKVMKKEYT---FIEMLYEVAKMQEIskRSEYLVKIFASFLDenwtdyfSSPPAIIMEY 447
Cdd:cd14066   1 IGSGGFGTVYKGVlENGTVVAVKRLNEMNCaasKKEFLTELEMLGRL--RHPNLVRLLGYCLE-------SDEKLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 448 MEGGDLRSILvdqeySALRHSV--KWPQVVAlIFSKIAKAVIEVHKEGYT---HCDIKPSNIlfnkklprygedalnsLL 522
Cdd:cd14066  72 MPNGSLEDRL-----HCHKGSPplPWPQRLK-IAKGIARGLEYLHEECPPpiiHGDIKSSNI----------------LL 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 523 NFEVVPKLSDLGSSvKIGTP------------VMHYT-PYYAHplqrfGNRAETMFDVYSFSVSLYVSLTNNFPF----P 585
Cdd:cd14066 130 DEDFEPKLTDFGLA-RLIPPsesvsktsavkgTIGYLaPEYIR-----TGRVSTKSDVYSFGVVLLELLTGKPAVdenrE 203
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15899909 586 EWLENEIEEAVKnpEKRKQALDDFHNATPRLDYV--PAEFKDLITMGL-------KGEISMLEINKRLEEI 647
Cdd:cd14066 204 NASRKDLVEWVE--SKGKEELEDILDKRLVDDDGveEEEVEALLRLALlctrsdpSLRPSMKEVVQMLEKL 272
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
366-586 6.74e-14

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 71.96  E-value: 6.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLV-ERN-GKKYAMKVMKKEYTFIEMlyEVAKMQE----ISKR-SEYLVKIFASFLDENWTdYFs 438
Cdd:cd05601   3 FEVKNVIGRGHFGEVQVVkEKAtGDIYAMKVLKKSETLAQE--EVSFFEEerdiMAKAnSPWITKLQYAFQDSENL-YL- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 439 sppaiIMEYMEGGDLRSILVdqeysalRHSVKWPQVVALIF-SKIAKAVIEVHKEGYTHCDIKPSNILfnkkLPRYGEda 517
Cdd:cd05601  79 -----VMEYHPGGDLLSLLS-------RYDDIFEESMARFYlAELVLAIHSLHSMGYVHRDIKPENIL----IDRTGH-- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 lnsllnfevvPKLSDLGSSVKI--------GTPVMhyTPYYAHP--LQRFGNRAETMFDV----YSFSVSLYVSLTNNFP 583
Cdd:cd05601 141 ----------IKLADFGSAAKLssdktvtsKMPVG--TPDYIAPevLTSMNGGSKGTYGVecdwWSLGIVAYEMLYGKTP 208

                ...
gi 15899909 584 FPE 586
Cdd:cd05601 209 FTE 211
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
366-647 7.48e-14

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 70.97  E-value: 7.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYV-LLVERN-GKKYAMK-VMKKEYTFIEMLYE-VAKMQEISKRSEY--LVKIFASFldENWTDYFss 439
Cdd:cd14098   2 YQIIDRLGSGTFAEVkKAVEVEtGKMRAIKqIVKRKVAGNDKNLQlFQREINILKSLEHpgIVRLIDWY--EDDQHIY-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 440 ppaIIMEYMEGGDLRSILVDqeysalrHSVKWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPrygedaln 519
Cdd:cd14098  78 ---LVMEYVEGGDLMDFIMA-------WGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDP-------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 520 sllnfeVVPKLSDLGSSVKIGTPVMHY----TPYYAHPL------QRFGNRAETMFDVYSFSVSLYVSLTNNFPFPEWLE 589
Cdd:cd14098 140 ------VIVKISDFGLAKVIHTGTFLVtfcgTMAYLAPEilmskeQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQ 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 590 NEIEEAVKNPEKRKQALDDFHnatprldyVPAEFKDLITmglkgeiSMLEIN--KRLEEI 647
Cdd:cd14098 214 LPVEKRIRKGRYTQPPLVDFN--------ISEEAIDFIL-------RLLDVDpeKRMTAA 258
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
366-573 8.07e-14

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 72.19  E-value: 8.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEYTFI-EMLYEVAKMQEISKRSE--YLVKIFASFLDENWTdyfssp 440
Cdd:cd05629   3 FHTVKVIGKGAFGEVRLVQKkdTGKIYAMKTLLKSEMFKkDQLAHVKAERDVLAESDspWVVSLYYSFQDAQYL------ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 441 pAIIMEYMEGGDLRSILVdqeysalRHSVKWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlpryGEdalns 520
Cdd:cd05629  77 -YLIMEFLPGGDLMTMLI-------KYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRG----GH----- 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15899909 521 llnfevvPKLSDLGSSVkiGTPVMHYTPYYAHPLQ------RFGNRAETMFDVYSFSVS 573
Cdd:cd05629 140 -------IKLSDFGLST--GFHKQHDSAYYQKLLQgksnknRIDNRNSVAVDSINLTMS 189
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
365-507 1.07e-13

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 70.46  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYTFIEMLYEVAK---MQEIS-----KRSEYLVKIFASFLDENWT 434
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVdlRTGRKYAIKCLYKSGPNSKDGNDFQKlpqLREIDlhrrvSRHPNIITLHDVFETEVAI 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15899909 435 dyfssppAIIMEYMEGGDLRSILVDQeysalRHSVKWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFN 507
Cdd:cd13993  81 -------YIVLEYCPNGDLFEAITEN-----RIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLS 141
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
372-507 1.36e-13

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 69.85  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVERN--GKKYAMKVMKKEYTFIE-----MLYEVAKMQEISkrSEYLVKIFASFLDENWTdYFssppaiI 444
Cdd:cd05123   1 LGKGSFGKVLLVRKKdtGKLYAMKVLRKKEIIKRkevehTLNERNILERVN--HPFIVKLHYAFQTEEKL-YL------V 71
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15899909 445 MEYMEGGDLRSILvdqeYSALRHSVKWpqvVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFN 507
Cdd:cd05123  72 LDYVPGGELFSHL----SKEGRFPEER---ARFYAAEIVLALEYLHSLGIIYRDLKPENILLD 127
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
366-642 2.25e-13

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 69.28  E-value: 2.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYV--LLVERNGKKYAMKVMKKEY-----TFIEMlyEVAKMQEIskRSEYLVKIFASFldENWTDYFs 438
Cdd:cd14095   2 YDIGRVIGDGNFAVVkeCRDKATDKEYALKIIDKAKckgkeHMIEN--EVAILRRV--KHPNIVQLIEEY--DTDTELY- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 439 sppaIIMEYMEGGDLrsilvdqeYSALRHSVKWPQVVA-LIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlprygEDA 517
Cdd:cd14095  75 ----LVMELVKGGDL--------FDAITSSTKFTERDAsRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEH-----EDG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 LNSLlnfevvpKLSDLGSSVKIGTPVMHY--TPYYAHP--LqrfgnrAETMF----DVYSFSVSLYVSLTNNFPF--PEW 587
Cdd:cd14095 138 SKSL-------KLADFGLATEVKEPLFTVcgTPTYVAPeiL------AETGYglkvDIWAAGVITYILLCGFPPFrsPDR 204
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15899909 588 LENEIEEAVKNPEkrkqalddFHNATPRLDYVPAEFKDLITMglkgeisMLEINK 642
Cdd:cd14095 205 DQEELFDLILAGE--------FEFLSPYWDNISDSAKDLISR-------MLVVDP 244
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
366-514 3.09e-13

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 70.04  E-value: 3.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEytfiemlyEVAKMQEIS----KR-------SEYLVKIFASFLDEN 432
Cdd:cd05598   3 FEKIKTIGVGAFGEVSLVRKkdTNALYAMKTLRKK--------DVLKRNQVAhvkaERdilaeadNEWVVKLYYSFQDKE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 433 wTDYFssppaiIMEYMEGGDLRSILVDQEYsalrhsvkWPQVVALIFskIAK---AVIEVHKEGYTHCDIKPSNILFNK- 508
Cdd:cd05598  75 -NLYF------VMDYIPGGDLMSLLIKKGI--------FEEDLARFY--IAElvcAIESVHKMGFIHRDIKPDNILIDRd 137

                ....*....
gi 15899909 509 ---KLPRYG 514
Cdd:cd05598 138 ghiKLTDFG 146
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
366-607 3.33e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 68.86  E-value: 3.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKkeYTFIEMLYEVAkMQEiskrseylVKIFASFLDENWTDYFSS---- 439
Cdd:cd13996   8 FEEIELLGSGGFGSVYKVRNkvDGVTYAIKKIR--LTEKSSASEKV-LRE--------VKALAKLNHPNIVRYYTAwvee 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 440 PPAII-MEYMEGGDLRSILVdqeySALRHSVKWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNK--KLPRYG-- 514
Cdd:cd13996  77 PPLYIqMELCEGGTLRDWID----RRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNddLQVKIGdf 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 515 ------EDALNSLLNFEVVPKLSDLGSSVKIGTPVmhytpyYAHPLQRFGNRAETMFDVYSFSV---SLYVS-------- 577
Cdd:cd13996 153 glatsiGNQKRELNNLNNNNNGNTSNNSVGIGTPL------YASPEQLDGENYNEKADIYSLGIilfEMLHPfktamers 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15899909 578 --LTN--NFPFPEWLENE-IEEAV-------KNPEKRKQALD 607
Cdd:cd13996 227 tiLTDlrNGILPESFKAKhPKEADliqsllsKNPEERPSAEQ 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
370-584 3.61e-13

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 68.95  E-value: 3.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 370 QLLGNGGMGYVLLVERNGKKYAMKVMKKEYTFIEMLYEV-AKMQEISKRSEYLVKIFASfldENWTDyFSSPPAIIMEYM 448
Cdd:cd13979   9 EPLGSGGFGSVYKATYKGETVAVKIVRRRRKNRASRQSFwAELNAARLRHENIVRVLAA---ETGTD-FASLGLIIMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 449 EGGDLRSILvDQEYSALrHSVKWpqvvALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKklprYGedalnsllnfevVP 528
Cdd:cd13979  85 GNGTLQQLI-YEGSEPL-PLAHR----ILISLDIARALRFCHSHGIVHLDVKPANILISE----QG------------VC 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15899909 529 KLSDLGSSVKIG------TPVMHY--TPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPF 584
Cdd:cd13979 143 KLCDFGCSVKLGegnevgTPRSHIggTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY 206
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
366-509 3.72e-13

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 69.57  E-value: 3.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEytfiEMLYevaKMQEISKRSE----------YLVKIFASFLDENW 433
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVRKkdTGHVYAMKKLRKS----EMLE---KEQVAHVRAErdilaeadnpWVVKLYYSFQDEEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 434 TdYFssppaiIMEYMEGGDLRSILVDQEysalrhsvkwpqvvalIFSK------IAKAV--IE-VHKEGYTHCDIKPSNI 504
Cdd:cd05599  76 L-YL------IMEFLPGGDMMTLLMKKD----------------TLTEeetrfyIAETVlaIEsIHKLGYIHRDIKPDNL 132

                ....*
gi 15899909 505 LFNKK 509
Cdd:cd05599 133 LLDAR 137
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
372-626 6.23e-13

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 68.02  E-value: 6.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVE--RNGKKYAMKVMKK----EYTFIEMLY-EVAKMQEISkrSEYLVKIFASFLDENWTdYFssppaiI 444
Cdd:cd05572   1 LGVGGFGRVELVQlkSKGRTFALKCVKKrhivQTRQQEHIFsEKEILEECN--SPFIVKLYRTFKDKKYL-YM------L 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 445 MEYMEGGDLRSILVD---------QEYSAlrhsvkwpQVVaLIFSKIakavievHKEGYTHCDIKPSNILFNKKlpRYge 515
Cdd:cd05572  72 MEYCLGGELWTILRDrglfdeytaRFYTA--------CVV-LAFEYL-------HSRGIIYRDLKPENLLLDSN--GY-- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 516 dalnsllnfevvPKLSDLGSSVKIGTPVMHYT----PYYAHP---LQRFGNRAEtmfDVYSFSVSLYVSLTNNFPF---- 584
Cdd:cd05572 132 ------------VKLVDFGFAKKLGSGRKTWTfcgtPEYVAPeiiLNKGYDFSV---DYWSLGILLYELLTGRPPFggdd 196
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15899909 585 --PEWLENEI---EEAVKNPEKRKQALDDF------HNATPRLDYVPAEFKDL 626
Cdd:cd05572 197 edPMKIYNIIlkgIDKIEFPKYIDKNAKNLikqllrRNPEERLGYLKGGIRDI 249
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
372-600 7.88e-13

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 68.23  E-value: 7.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVERNGKKyamKVMKKEYTFIE--------MLYEVAKMQEIskRSEYLVKIFASFLDENwtdyfsspPAI 443
Cdd:cd06620  13 LGAGNGGSVSKVLHIPTG---TIMAKKVIHIDakssvrkqILRELQILHEC--HSPYIVSFYGAFLNEN--------NNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 444 I--MEYMEGGDLRSILvdqeysalrhSVKWPqVVALIFSKIAKAVIE-------VHKegYTHCDIKPSNILFNKKlpryG 514
Cdd:cd06620  80 IicMEYMDCGSLDKIL----------KKKGP-FPEEVLGKIAVAVLEgltylynVHR--IIHRDIKPSNILVNSK----G 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 515 EdalnsllnfevvPKLSDLGSSVK-IGTPVMHY--TPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPFpeWLENE 591
Cdd:cd06620 143 Q------------IKLCDFGVSGElINSIADTFvgTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF--AGSND 208

                ....*....
gi 15899909 592 IEEAVKNPE 600
Cdd:cd06620 209 DDDGYNGPM 217
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
372-585 1.21e-12

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 67.45  E-value: 1.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVE-RNGKK-YAMKV-------MKKEYTFIEMlyEVAKmqeiSKRSEYLVKIFASFLDENwtdyfSSPPA 442
Cdd:cd06621   9 LGEGAGGSVTKCRlRNTKTiFALKTittdpnpDVQKQILREL--EINK----SCASPYIVKYYGAFLDEQ-----DSSIG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 443 IIMEYMEGGDLRSILVDQEYSALRHSVKwpqvvalIFSKIAKAVIE----VHKEGYTHCDIKPSNILFNKKlpryGEdal 518
Cdd:cd06621  78 IAMEYCEGGSLDSIYKKVKKKGGRIGEK-------VLGKIAESVLKglsyLHSRKIIHRDIKPSNILLTRK----GQ--- 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15899909 519 nsllnfevvPKLSDLGSSVKIGTPVMHY---TPYYAHPlQRFGNRAETMF-DVYSFSVSLYVSLTNNFPFP 585
Cdd:cd06621 144 ---------VKLCDFGVSGELVNSLAGTftgTSYYMAP-ERIQGGPYSITsDVWSLGLTLLEVAQNRFPFP 204
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
370-550 1.47e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 66.78  E-value: 1.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 370 QLLGNGGMG--YVLLVERNGKKYAMKVMK------KEYTFIEMlyEVAKMQEISkrSEYLVKIFASFLDENwtdYFSspp 441
Cdd:cd06606   6 ELLGKGSFGsvYLALNLDTGELMAVKEVElsgdseEELEALER--EIRILSSLK--HPNIVRYLGTERTEN---TLN--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 442 aIIMEYMEGGDLRSILvdQEYSALRhsvkwPQVVAlIFSK-IAKAVIEVHKEGYTHCDIKPSNIlfnkklprygedalns 520
Cdd:cd06606  76 -IFLEYVPGGSLASLL--KKFGKLP-----EPVVR-KYTRqILEGLEYLHSNGIVHRDIKGANI---------------- 130
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15899909 521 LLNFEVVPKLSDLGSSVKI-------GTPVMHYTPYY 550
Cdd:cd06606 131 LVDSDGVVKLADFGCAKRLaeiatgeGTKSLRGTPYW 167
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
366-627 2.07e-12

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 67.37  E-value: 2.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKeytfIEMLY--EVAKMQE-----ISKRSEYLVKIFASFLDENWTdY 436
Cdd:cd05597   3 FEILKVIGRGAFGEVAVVKlkSTEKVYAMKILNK----WEMLKraETACFREerdvlVNGDRRWITKLHYAFQDENYL-Y 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 437 FssppaiIMEYMEGGDLRSILVdqeysalRHSVKWPQVVALIF-SKIAKAVIEVHKEGYTHCDIKPSNILFNK----KLP 511
Cdd:cd05597  78 L------VMDYYCGGDLLTLLS-------KFEDRLPEEMARFYlAEMVLAIDSIHQLGYVHRDIKPDNVLLDRnghiRLA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 512 RYGedalnSLLnfevvpKLSDLG---SSVKIGtpvmhyTPYYAHP--LQ-------RFGNRAetmfDVYSFSVSLYVSLT 579
Cdd:cd05597 145 DFG-----SCL------KLREDGtvqSSVAVG------TPDYISPeiLQamedgkgRYGPEC----DWWSLGVCMYEMLY 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15899909 580 NNFPFpeWLENEIEEAVK--NPEKRKQALDDfhnatprLDYVPAEFKDLI 627
Cdd:cd05597 204 GETPF--YAESLVETYGKimNHKEHFSFPDD-------EDDVSEEAKDLI 244
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
366-602 5.12e-12

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 65.39  E-value: 5.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEV-KQLLGNGGMGYVLLV--ERNGKKYAMKVmkkeytfiemLYEVAKMQ---EISKRS---EYLVKIFASFldENwtdY 436
Cdd:cd14089   2 YTIsKQVLGLGINGKVLECfhKKTGEKFALKV----------LRDNPKARrevELHWRAsgcPHIVRIIDVY--EN---T 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 437 FSSPPA--IIMEYMEGGDLRSILVDQEYSALRHSVkwpqvVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPryg 514
Cdd:cd14089  67 YQGRKCllVVMECMEGGELFSRIQERADSAFTERE-----AAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGP--- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 515 edalNSLLnfevvpKLSDLG------SSVKIGTPVmhYTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSL-------TNN 581
Cdd:cd14089 139 ----NAIL------KLTDFGfakettTKKSLQTPC--YTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLcgyppfySNH 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15899909 582 ------------------FPFPEWleNEIEEAVK---------NPEKR 602
Cdd:cd14089 207 glaispgmkkrirngqyeFPNPEW--SNVSEEAKdlirgllktDPSER 252
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
365-550 5.25e-12

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 65.18  E-value: 5.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVERN--GKKYAMKVMKkeytfiemlyeVAKMQEISKRS---EylVKIFA------------S 427
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKsdGKLYVLKEID-----------LSNMSEKEREEalnE--VKLLSklkhpnivkyyeS 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 428 FLDEnwtDYFSsppaIIMEYMEGGDLRSILvdQEYSALRHSVKWPQVVAlIFSKIAKAVIEVHKEGYTHCDIKPSNILFN 507
Cdd:cd08215  68 FEEN---GKLC----IVMEYADGGDLAQKI--KKQKKKGQPFPEEQILD-WFVQICLALKYLHSRKILHRDLKTQNIFLT 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15899909 508 KKLprygedalnsllnfevVPKLSDLGSSvKIGTPVMHY------TPYY 550
Cdd:cd08215 138 KDG----------------VVKLGDFGIS-KVLESTTDLaktvvgTPYY 169
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
366-628 8.85e-12

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 64.58  E-value: 8.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKK-----EYTFIEMlyEVAKMQEISKRSeyLVKIFASFLDEnwtdyfs 438
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRhwNENQEYAMKIIDKsklkgKEDMIES--EILIIKSLSHPN--IVKLFEVYETE------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 439 SPPAIIMEYMEGGDLrsilvdqeYSALRHSVKWPQV-VALIFSKIAKAVIEVHKEGYTHCDIKPSNILFnkklpRYGEDA 517
Cdd:cd14185  71 KEIYLILEYVRGGDL--------FDAIIESVKFTEHdAALMIIDLCEALVYIHSKHIVHRDLKPENLLV-----QHNPDK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 518 LNSLlnfevvpKLSDLGSSVKIGTPVMHY--TPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPF--PEWLENEIE 593
Cdd:cd14185 138 STTL-------KLADFGLAKYVTGPIFTVcgTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrsPERDQEELF 210
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15899909 594 EAVKnpekrkqaLDDFHNATPRLDYVPAEFKDLIT 628
Cdd:cd14185 211 QIIQ--------LGHYEFLPPYWDNISEAAKDLIS 237
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
366-509 1.32e-11

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 64.48  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEYTFIE---MLYEVAKMQEIsKRSEYLVKIFASFLdENWTDYFssp 440
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNkeTGELVAIKKMKKKFYSWEecmNLREVKSLRKL-NEHPNIVKLKEVFR-ENDELYF--- 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15899909 441 paiIMEYMEGgDLRSILVDQEYSALRhsvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKK 509
Cdd:cd07830  76 ---VFEYMEG-NLYQLMKDRKGKPFS-----ESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGP 135
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
366-584 1.59e-11

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 63.58  E-value: 1.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMK---------VMKKEytfieMLYEVAKMQEIskRSEYLVKIFASFLDENWT 434
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRkvDGRVYALKqidisrmsrKMREE-----AIDEARVLSKL--NSPYVIKYYDSFVDKGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 435 DyfssppaIIMEYMEGGDLRSILVDQEYSALRHSVKWPqvvalIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKklpryg 514
Cdd:cd08529  75 N-------IVMEYAENGDLHSLIKSQRGRPLPEDQIWK-----FFIQTLLGLSHLHSKKILHRDIKSMNIFLDK------ 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15899909 515 EDALnsllnfevvpKLSDLGSSvKIGTPVMHY------TPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPF 584
Cdd:cd08529 137 GDNV----------KIGDLGVA-KILSDTTNFaqtivgTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPF 201
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
366-549 1.74e-11

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 63.41  E-value: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVE--RNGKKYAMKVMKKEYTFIEM-LYEVAKMQEISK--RSEYLVKIFASFLDENWTDyfssp 440
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARdkVTGEKVAIKKIKNDFRHPKAaLREIKLLKHLNDveGHPNIVKLLDVFEHRGGNH----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 441 PAIIMEYMeGGDLRSILVDQEYsalRHSvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPrygedalns 520
Cdd:cd05118  76 LCLVFELM-GMNLYELIKDYPR---GLP---LDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELG--------- 139
                       170       180
                ....*....|....*....|....*....
gi 15899909 521 llnfevVPKLSDLGSSVKIGTPvmHYTPY 549
Cdd:cd05118 140 ------QLKLADFGLARSFTSP--PYTPY 160
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
366-604 1.91e-11

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 65.03  E-value: 1.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVERNGKK--YAMKVMKKeytfIEML--YEVAKMQE-----ISKRSEYLVKIFASFLDENWTdy 436
Cdd:cd05624  74 FEIIKVIGRGAFGEVAVVKMKNTEriYAMKILNK----WEMLkrAETACFREernvlVNGDCQWITTLHYAFQDENYL-- 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 437 fssppAIIMEYMEGGDLRSILVDQEYsalrhsvKWPQVVALIF-SKIAKAVIEVHKEGYTHCDIKPSNILFNkklpryge 515
Cdd:cd05624 148 -----YLVMDYYVGGDLLTLLSKFED-------KLPEDMARFYiGEMVLAIHSIHQLHYVHRDIKPDNVLLD-------- 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 516 daLNS---LLNFEVVPKLSDLG---SSVKIGTPvMHYTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPFpeWLE 589
Cdd:cd05624 208 --MNGhirLADFGSCLKMNDDGtvqSSVAVGTP-DYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPF--YAE 282
                       250
                ....*....|....*..
gi 15899909 590 NEIEE--AVKNPEKRKQ 604
Cdd:cd05624 283 SLVETygKIMNHEERFQ 299
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
366-602 2.19e-11

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 63.17  E-value: 2.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKE---------YTFIEMLYEVAKmQEISKRSEYLvkifasfldENWT 434
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHilTGEKVAIKIMDKKalgddlprvKTEIEALKNLSH-QHICRLYHVI---------ETDN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 435 DYFssppaIIMEYMEGGDLRSILVDQEY---SALRHsvkwpqvvalIFSKIAKAVIEVHKEGYTHCDIKPSNILF----N 507
Cdd:cd14078  75 KIF-----MVLEYCPGGELFDYIVAKDRlseDEARV----------FFRQIVSAVAYVHSQGYAHRDLKPENLLLdedqN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 508 KKLPRYG-----EDALNSLLNfevvpklSDLGSsvkigtpvmhytPYYAHP-----LQRFGNRAetmfDVYSFSVSLYVS 577
Cdd:cd14078 140 LKLIDFGlcakpKGGMDHHLE-------TCCGS------------PAYAAPeliqgKPYIGSEA----DVWSMGVLLYAL 196
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15899909 578 LTNNFPF-------------------PEWLENEIEEAVK-----NPEKR 602
Cdd:cd14078 197 LCGFLPFdddnvmalyrkiqsgkyeePEWLSPSSKLLLDqmlqvDPKKR 245
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
366-584 2.79e-11

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 64.32  E-value: 2.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKeytfIEML--YEVAKMQE-----ISKRSEYLVKIFASFLDENWTdY 436
Cdd:cd05596  28 FDVIKVIGRGAFGEVQLVRHksTKKVYAMKLLSK----FEMIkrSDSAFFWEerdimAHANSEWIVQLHYAFQDDKYL-Y 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 437 fssppaIIMEYMEGGDLRSILVDQEYSalrhsVKWpqvVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFnkklprygeD 516
Cdd:cd05596 103 ------MVMDYMPGGDLVNLMSNYDVP-----EKW---ARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL---------D 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 517 ALNSLlnfevvpKLSDLGSSVKIG--------TPVMhyTPYYAHP--LQRFGNRAE--TMFDVYSFSVSLYVSLTNNFPF 584
Cdd:cd05596 160 ASGHL-------KLADFGTCMKMDkdglvrsdTAVG--TPDYISPevLKSQGGDGVygRECDWWSVGVFLYEMLVGDTPF 230
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
372-649 3.50e-11

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 62.96  E-value: 3.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVE--RNGKKYAMKVMKK------------EYTFIEMLYEVakMQEIS--K--RSEYLVKIFASFLDENW 433
Cdd:cd14008   1 LGRGSFGKVKLALdtETGQLYAIKIFNKsrlrkrregkndRGKIKNALDDV--RREIAimKklDHPNIVRLYEVIDDPES 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 434 TDYFssppaIIMEYMEGGDLRSILVDQEYSALRhsvkwPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlpry 513
Cdd:cd14008  79 DKLY-----LVLEYCEGGPVMELDSGDRVPPLP-----EETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTAD---- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 514 gedalnsllnfEVVpKLSDLGSSV-----------KIGTPVmhytpYYAHPLQRFGNRAETMF--DVYSFSVSLYVSLTN 580
Cdd:cd14008 145 -----------GTV-KISDFGVSEmfedgndtlqkTAGTPA-----FLAPELCDGDSKTYSGKaaDIWALGVTLYCLVFG 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15899909 581 NFPFPEWLENEIEEAVKNPEkrkqalddfhNATPRLDYVPAEFKDLITmglkgeiSMLEIN--KR--LEEILV 649
Cdd:cd14008 208 RLPFNGDNILELYEAIQNQN----------DEFPIPPELSPELKDLLR-------RMLEKDpeKRitLKEIKE 263
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
370-634 5.32e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 62.74  E-value: 5.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 370 QLLGNGGMGYVL--LVERNGKKYAMKVMK---KEYTFIEMLYEVAKMQEISKRSEYLVKIFASfldenwtdyfSSPPAII 444
Cdd:cd14170   8 QVLGLGINGKVLqiFNKRTQEKFALKMLQdcpKARREVELHWRASQCPHIVRIVDVYENLYAG----------RKCLLIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 445 MEYMEGGDLRSILVDQEYSALRHsvkwpQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPrygedalNSLLnf 524
Cdd:cd14170  78 MECLDGGELFSRIQDRGDQAFTE-----REASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRP-------NAIL-- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 525 evvpKLSDLG------SSVKIGTPVmhYTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNnfpFPEWLENEiEEAVKN 598
Cdd:cd14170 144 ----KLTDFGfakettSHNSLTTPC--YTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCG---YPPFYSNH-GLAISP 213
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15899909 599 PEKRKQALDDFHNATPRLDYVPAEFKDLITMGLKGE 634
Cdd:cd14170 214 GMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTE 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
366-553 5.68e-11

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 61.86  E-value: 5.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVL--LVERNGKKYAMKVMKKEYTFIEMLYEVakMQEI---SK-RSEYLVKIFASFLDEnwtDYFSs 439
Cdd:cd06627   2 YQLGDLIGRGAFGSVYkgLNLNTGEFVAIKQISLEKIPKSDLKSV--MGEIdllKKlNHPNIVKYIGSVKTK---DSLY- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 440 ppaIIMEYMEGGDLRSILvdqeysalRHSVKWPQ-VVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKklprygedal 518
Cdd:cd06627  76 ---IILEYVENGSLASII--------KKFGKFPEsLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTK---------- 134
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15899909 519 nsllnfEVVPKLSDLGSSVKIG-----TPVMHYTPYYAHP 553
Cdd:cd06627 135 ------DGLVKLADFGVATKLNevekdENSVVGTPYWMAP 168
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
366-542 6.82e-11

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 61.90  E-value: 6.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVL--LVERNGKKYAMKVMKKEYTFIEMLYEVAKMQEIskRSEYLVKIFASFLDEN--Wtdyfsspp 441
Cdd:cd06612   5 FDILEKLGEGSYGSVYkaIHKETGQVVAIKVVPVEEDLQEIIKEISILKQC--DSPYIVKYYGSYFKNTdlW-------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 442 aIIMEYMEGGDLRSILvdqeysALRHSVKWPQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNkklprygEDALNSL 521
Cdd:cd06612  75 -IVMEYCGAGSVSDIM------KITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLN-------EEGQAKL 140
                       170       180
                ....*....|....*....|...
gi 15899909 522 LNFEVVPKLSDLG--SSVKIGTP 542
Cdd:cd06612 141 ADFGVSGQLTDTMakRNTVIGTP 163
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
365-509 1.20e-10

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 61.12  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 365 GYEVKQLLGNGGMGYVLLVER--NGKKYAMKVMKKEyTFIE------MLYEVAKMQEIskRSEYLVKIFASFLDEnwTDY 436
Cdd:cd05578   1 HFQILRVIGKGSFGKVCIVQKkdTKKMFAMKYMNKQ-KCIEkdsvrnVLNELEILQEL--EHPFLVNLWYSFQDE--EDM 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15899909 437 FssppaIIMEYMEGGDLRsilvdqeYSaLRHSVKWPQ-VVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKK 509
Cdd:cd05578  76 Y-----MVVDLLLGGDLR-------YH-LQQKVKFSEeTVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQ 136
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
387-584 1.86e-10

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 60.83  E-value: 1.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 387 GKKYAMKVMKK----EYTFIEMLYEVAkMQEISKRSEYLVKIFASFldENwtdyfSSPPAIIMEYMEGGDLRSILVDQEy 462
Cdd:cd14106  33 GKEYAAKFLRKrrrgQDCRNEILHEIA-VLELCKDCPRVVNLHEVY--ET-----RSELILILELAAGGELQTLLDEEE- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 463 salrhSVKWPQVVALIfSKIAKAVIEVHKEGYTHCDIKPSNILFNKKLPryGEDAlnsllnfevvpKLSDLGSSVKI--- 539
Cdd:cd14106 104 -----CLTEADVRRLM-RQILEGVQYLHERNIVHLDLKPQNILLTSEFP--LGDI-----------KLCDFGISRVIgeg 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15899909 540 -------GTP------VMHYTPYyahplqrfgnraETMFDVYSFSVSLYVSLTNNFPF 584
Cdd:cd14106 165 eeireilGTPdyvapeILSYEPI------------SLATDMWSIGVLTYVLLTGHSPF 210
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
372-509 2.03e-10

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 61.59  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVER--NGKKYAMKVMKKEYTFiemlyevaKMQEISK-----------RSEYLVKIFASFLDENWTdYFS 438
Cdd:cd05600  19 VGQGGYGSVFLARKkdTGEICALKIMKKKVLF--------KLNEVNHvlterdiltttNSPWLVKLLYAFQDPENV-YLA 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15899909 439 sppaiiMEYMEGGDLRSILVDQEYsaLRHsvkwpQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKK 509
Cdd:cd05600  90 ------MEYVPGGDFRTLLNNSGI--LSE-----EHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSS 147
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
366-632 2.06e-10

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 60.77  E-value: 2.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEV-KQLLGNGGMGYVL--LVERNGKKYAMKVmkkeytfiemLYEVAKMQ---EISKRS---EYLVKIFASFldENwTDY 436
Cdd:cd14172   5 YKLsKQVLGLGVNGKVLecFHRRTGQKCALKL----------LYDSPKARrevEHHWRAsggPHIVHILDVY--EN-MHH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 437 FSSPPAIIMEYMEGGDLRSILV---DQEYSAlrhsvkwpQVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNKKlpry 513
Cdd:cd14172  72 GKRCLLIIMECMEGGELFSRIQergDQAFTE--------REASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSK---- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 514 gedalnsllNFEVVPKLSDLGSSVK------IGTPVmhYTPYYAHPLQRFGNRAETMFDVYSFSVSLYVSLTNnfpFPEW 587
Cdd:cd14172 140 ---------EKDAVLKLTDFGFAKEttvqnaLQTPC--YTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCG---FPPF 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15899909 588 LENeIEEAVKNPEKRKQALDDFHNATPRLDYVPAEFKDLITMGLK 632
Cdd:cd14172 206 YSN-TGQAISPGMKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLK 249
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
370-587 2.12e-10

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 60.59  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 370 QLLGNGGMGYVLLVERNGKK--YAMK------VMKKEYtfIEMLYEVAKMQEISKRseYLVKIFASFldenwtdyfSSPP 441
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKtwLAIKcppslhVDDSER--MELLEEAKKMEMAKFR--HILPVYGIC---------SEPV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 442 AIIMEYMEGGDLRSILVDqeysalrHSVKWPQVVALIFsKIAKAVIEVH--KEGYTHCDIKPSNILFnkklprygeDAln 519
Cdd:cd14025  69 GLVMEYMETGSLEKLLAS-------EPLPWELRFRIIH-ETAVGMNFLHcmKPPLLHLDLKPANILL---------DA-- 129
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15899909 520 sllNFEVvpKLSDLG--------SSVKIGTPVMHYTPYYAHPlQRF--GNRA-ETMFDVYSFSVSLYVSLTNNFPFPEW 587
Cdd:cd14025 130 ---HYHV--KISDFGlakwnglsHSHDLSRDGLRGTIAYLPP-ERFkeKNRCpDTKHDVYSFAIVIWGILTQKKPFAGE 202
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
372-507 2.22e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 61.57  E-value: 2.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 372 LGNGGMGYVLLVER--NGKKYAMKVM-KKEYTFIEMLYEVAKMQEI--SKRSEYLVKIFASFLDENwTDYFssppaiIME 446
Cdd:cd05626   9 LGIGAFGEVCLACKvdTHALYAMKTLrKKDVLNRNQVAHVKAERDIlaEADNEWVVKLYYSFQDKD-NLYF------VMD 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15899909 447 YMEGGDLRSILVDQEYsalrhsvkWPQVVALIF-SKIAKAVIEVHKEGYTHCDIKPSNILFN 507
Cdd:cd05626  82 YIPGGDMMSLLIRMEV--------FPEVLARFYiAELTLAIESVHKMGFIHRDIKPDNILID 135
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
366-538 3.41e-10

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 60.00  E-value: 3.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLVE--RNGKKYAMKvmKKEYTFIEMLYEVAKMQEISKR--SEYLVKIFASFL----DENWTDYf 437
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEdlSTGRLYALK--KILCHSKEDVKEAMREIENYRLfnHPNILRLLDSQIvkeaGGKKEVY- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 438 ssppaIIMEYMEGGDLRsilvDQEYSALRHSVKWPQV-VALIFSKIAKAVIEVHKE---GYTHCDIKPSNILFnkklpry 513
Cdd:cd13986  79 -----LLLPYYKRGSLQ----DEIERRLVKGTFFPEDrILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLL------- 142
                       170       180
                ....*....|....*....|....*
gi 15899909 514 GEDALnsllnfevvPKLSDLGSSVK 538
Cdd:cd13986 143 SEDDE---------PILMDLGSMNP 158
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
366-648 3.54e-10

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 59.80  E-value: 3.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 366 YEVKQLLGNGGMGYVLLV--ERNGKKYAMKVMKKEyTFIEmlYEVAKM--QEI----SKRSEYLVKIFASFLDEnwTDYF 437
Cdd:cd14007   2 FEIGKPLGKGKFGNVYLAreKKSGFIVALKVISKS-QLQK--SGLEHQlrREIeiqsHLRHPNILRLYGYFEDK--KRIY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 438 ssppaIIMEYMEGGDLrsilvdqeYSALRHSVKWP-QVVALIFSKIAKAVIEVHKEGYTHCDIKPSNILFNkklpryged 516
Cdd:cd14007  77 -----LILEYAPNGEL--------YKELKKQKRFDeKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG--------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15899909 517 alnslLNFEVvpKLSDLGSSVKI---------GTpvMHYTPyyahPLQRFGNRAETMFDVYSFSVSLYVSLTNNFPFPEW 587
Cdd:cd14007 135 -----SNGEL--KLADFGWSVHA