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Conserved domains on  [gi|32474612|ref|NP_867606|]
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serine/threonine kinase [Rhodopirellula baltica SH 1]

Protein Classification

serine/threonine protein kinase (domain architecture ID 12037397)

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
419-681 1.60e-91

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  Cd Length: 260  Bit Score: 289.87  E-value: 1.60e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVND-TSIARFEREVQITCQLNHSNTIAIYDYGRTpEGVFYYAM 497
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDeEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 498 EYLDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRTEG 577
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDSGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 578 SPAnegSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSKRgNVKVSS 657
Cdd:cd14014 156 TQT---GSVLGTPAYMAPEQARG-GPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPL-NPDVPP 230
                       250       260
                ....*....|....*....|....
gi 32474612 658 QLEDAIMGCLEKSRAKRPQTARDL 681
Cdd:cd14014 231 ALDAIILRALAKDPEERPQSAAEL 254
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
211-309 3.27e-07

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains.


:

Pssm-ID: 308398  Cd Length: 195  Bit Score: 51.05  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   211 GVPTMYVCAPIRDPSFQVVGVLALQIRPErEFIPILQLGRTGESGETYAFNEDGIMISNSRFDEELILMGLLPDQPHSHS 290
Cdd:pfam02743  82 GKPVLSIARPIYDDSGEVIGVLVADLDLE-TLQELLSQLKLGETGSVFIVDSDGTILAHSDPDLIGKNLRDSNKSKLSAR 160
                          90       100
                  ....*....|....*....|....
gi 32474612   291 ILQ-----MSVRDPGVDMTRGFRP 309
Cdd:pfam02743 161 LAKtesgvFSVTLDGEDYLVAYAP 184
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
419-681 1.60e-91

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  Cd Length: 260  Bit Score: 289.87  E-value: 1.60e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVND-TSIARFEREVQITCQLNHSNTIAIYDYGRTpEGVFYYAM 497
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDeEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 498 EYLDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRTEG 577
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDSGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 578 SPAnegSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSKRgNVKVSS 657
Cdd:cd14014 156 TQT---GSVLGTPAYMAPEQARG-GPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPL-NPDVPP 230
                       250       260
                ....*....|....*....|....
gi 32474612 658 QLEDAIMGCLEKSRAKRPQTARDL 681
Cdd:cd14014 231 ALDAIILRALAKDPEERPQSAAEL 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
420-681 2.84e-59

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 203.15  E-value: 2.84e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    420 YTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVnDTSIARFEREVQITCQLNHSNTIAIYDYGRTPeGVFYYAMEY 499
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI-KKDRERILREIKILKKLKHPNIVRLYDVFEDE-DKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    500 LDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRTEGSp 579
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG----HVKLADFGLARQLDPGEKL- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    580 anegSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSKRgNVKVSSQL 659
Cdd:smart00220 154 ----TTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPP-EWDISPEA 227
                          250       260
                   ....*....|....*....|..
gi 32474612    660 EDAIMGCLEKSRAKRPqTARDL 681
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-TAEEA 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
420-689 4.45e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 181.09  E-value: 4.45e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 420 YTLDQKLGEGAMGVVYKGHHsmlRRPTAIKLLHADKVND-TSIARFEREVQITCQLNHSNTIA-IYDYGRTPEGvFYYAM 497
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKsKEVERFLREIQILASLNHPPNIVkLYDFFQDEGS-LYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 498 EYLDGIDLQDLVNKYGTQ---SEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepDVVKVLDFGLVKAVDR 574
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRKgplSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDG---RVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 575 TEGSPANEG--SSMSGTPLYMSPESIQAPMT--VDACSDIYAVGAVGYFLLTGKPVFEA---ANLVDLCQKHIEESPVP- 646
Cdd:COG0515 155 PGSTSSIPAlpSTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYELLTGLPPFEGeknSSATSQTLKIILELPTPs 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 32474612 647 ----PSKRGNVKVSSQLEDAIMGCLEKSRAKRPQTARDLGILISKCA 689
Cdd:COG0515 235 laspLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHL 281
Pkinase pfam00069
Protein kinase domain;
420-681 1.51e-49

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 175.48  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   420 YTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTPeGVFYYAMEY 499
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDK-DNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   500 LDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRteGSP 579
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDG----NLKITDFGLARQLNS--GSS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   580 ANegsSMSGTPLYMSPESIQAPMTvDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEE---SPVPPSkrgnvkVS 656
Cdd:pfam00069 154 LT---SFVGTPWYMAPEVLRGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQdfdSPRPSS------IS 223
                         250       260
                  ....*....|....*....|....*
gi 32474612   657 SQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:pfam00069 224 EEAKDLLKKLLKKDPSKRL-TATEA 247
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
447-681 3.02e-31

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


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 131.51  E-value: 3.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    447 AIKLLHADKVNDT-SIARFEREVQITCQLNHSNTIAIYDYGRTPEGVFYYAMEYLDGIDLQDLVNKYGTQSEARVIHILL 525
Cdd:TIGR03903    7 AIKLLRTDAPEEEhQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLML 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    526 QICGSLFEAHSQGLVHRDIKPANVMLNRRGCEPDvVKVLDFGL------VKAVDRTEGSPANEgssMSGTPLYMSPESIQ 599
Cdd:TIGR03903   87 QVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPH-AKVLDFGIgtllpgVRDADVATLTRTTE---VLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    600 A-PMTvdACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPV--PPSKRGNvkvssQLEDAIMGCLEKSRAKRPQ 676
Cdd:TIGR03903  163 GePVT--PNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVslPPWIAGH-----PLGQVLRKALNKDPRQRAA 235

                   ....*
gi 32474612    677 TARDL 681
Cdd:TIGR03903  236 SAPAL 240
pknD PRK13184
serine/threonine-protein kinase; Reviewed
417-622 2.58e-23

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 105.62  E-value: 2.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612  417 LGQYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKV-NDTSIARFEREVQITCQLNHSNTIAIYDYGRTPEGVfYY 495
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSeNPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPV-YY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612  496 AMEYLDGIDLQDLVNKYGTQ-----------SEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepDVVkVL 564
Cdd:PRK13184  80 TMPYIEGYTLKSLLKSVWQKeslskelaektSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG---EVV-IL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32474612  565 DFGLVKAVDRTE--------GSPANEGSSMS------GTPLYMSPESIQ-APMTVDacSDIYAVGAVGYFLLT 622
Cdd:PRK13184 156 DWGAAIFKKLEEedlldidvDERNICYSSMTipgkivGTPDYMAPERLLgVPASES--TDIYALGVILYQMLT 226
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
211-309 3.27e-07

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains.


Pssm-ID: 308398  Cd Length: 195  Bit Score: 51.05  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   211 GVPTMYVCAPIRDPSFQVVGVLALQIRPErEFIPILQLGRTGESGETYAFNEDGIMISNSRFDEELILMGLLPDQPHSHS 290
Cdd:pfam02743  82 GKPVLSIARPIYDDSGEVIGVLVADLDLE-TLQELLSQLKLGETGSVFIVDSDGTILAHSDPDLIGKNLRDSNKSKLSAR 160
                          90       100
                  ....*....|....*....|....
gi 32474612   291 ILQ-----MSVRDPGVDMTRGFRP 309
Cdd:pfam02743 161 LAKtesgvFSVTLDGEDYLVAYAP 184
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
419-681 1.60e-91

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  Cd Length: 260  Bit Score: 289.87  E-value: 1.60e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVND-TSIARFEREVQITCQLNHSNTIAIYDYGRTpEGVFYYAM 497
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDeEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 498 EYLDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRTEG 577
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDSGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 578 SPAnegSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSKRgNVKVSS 657
Cdd:cd14014 156 TQT---GSVLGTPAYMAPEQARG-GPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPL-NPDVPP 230
                       250       260
                ....*....|....*....|....
gi 32474612 658 QLEDAIMGCLEKSRAKRPQTARDL 681
Cdd:cd14014 231 ALDAIILRALAKDPEERPQSAAEL 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
420-681 2.84e-59

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 203.15  E-value: 2.84e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    420 YTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVnDTSIARFEREVQITCQLNHSNTIAIYDYGRTPeGVFYYAMEY 499
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI-KKDRERILREIKILKKLKHPNIVRLYDVFEDE-DKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    500 LDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRTEGSp 579
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG----HVKLADFGLARQLDPGEKL- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612    580 anegSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSKRgNVKVSSQL 659
Cdd:smart00220 154 ----TTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPP-EWDISPEA 227
                          250       260
                   ....*....|....*....|..
gi 32474612    660 EDAIMGCLEKSRAKRPqTARDL 681
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-TAEEA 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
420-689 4.45e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 181.09  E-value: 4.45e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 420 YTLDQKLGEGAMGVVYKGHHsmlRRPTAIKLLHADKVND-TSIARFEREVQITCQLNHSNTIA-IYDYGRTPEGvFYYAM 497
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKsKEVERFLREIQILASLNHPPNIVkLYDFFQDEGS-LYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 498 EYLDGIDLQDLVNKYGTQ---SEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepDVVKVLDFGLVKAVDR 574
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRKgplSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDG---RVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 575 TEGSPANEG--SSMSGTPLYMSPESIQAPMT--VDACSDIYAVGAVGYFLLTGKPVFEA---ANLVDLCQKHIEESPVP- 646
Cdd:COG0515 155 PGSTSSIPAlpSTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYELLTGLPPFEGeknSSATSQTLKIILELPTPs 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 32474612 647 ----PSKRGNVKVSSQLEDAIMGCLEKSRAKRPQTARDLGILISKCA 689
Cdd:COG0515 235 laspLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHL 281
Pkinase pfam00069
Protein kinase domain;
420-681 1.51e-49

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 175.48  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   420 YTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTPeGVFYYAMEY 499
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDK-DNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   500 LDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRteGSP 579
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDG----NLKITDFGLARQLNS--GSS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612   580 ANegsSMSGTPLYMSPESIQAPMTvDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEE---SPVPPSkrgnvkVS 656
Cdd:pfam00069 154 LT---SFVGTPWYMAPEVLRGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQdfdSPRPSS------IS 223
                         250       260
                  ....*....|....*....|....*
gi 32474612   657 SQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:pfam00069 224 EEAKDLLKKLLKKDPSKRL-TATEA 247
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
419-681 7.73e-45

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  Cd Length: 258  Bit Score: 162.63  E-value: 7.73e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTpEGVFYYAME 498
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEE-NGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 499 YLDGIDLQDLVNKYGTQ----SEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDR 574
Cdd:cd08215  80 YADGGDLAQKIKKQKKKgqpfPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG----VVKLGDFGISKVLES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 575 TEgspaNEGSSMSGTPLYMSPESIQ-APMTVDacSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSKRgnv 653
Cdd:cd08215 156 TT----DLAKTVVGTPYYLSPELCEnKPYNYK--SDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQ--- 226
                       250       260
                ....*....|....*....|....*...
gi 32474612 654 kVSSQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:cd08215 227 -YSSELRDLVNSMLQKDPEKRP-SANEI 252
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
426-674 2.35e-43

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


Pssm-ID: 270911  Cd Length: 251  Bit Score: 158.15  E-value: 2.35e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 426 LGEGAMGVVYKGHHSMLRRPTAIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTPEGVfYYAMEYLDGIDL 505
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFI-YLVLEYCAGGDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 506 QDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGCEPdVVKVLDFGLVKAVdrtegSPANEGSS 585
Cdd:cd14009  80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDP-VLKIADFGFARSL-----QPASMAET 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 586 MSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKhIEESPVPPSKRGNVKVSSQLEDAIMG 665
Cdd:cd14009 154 LCGSPLYMAPEILQF-QKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRN-IERSDAVIPFPIAAQLSPDCKDLLRR 231

                ....*....
gi 32474612 666 CLEKSRAKR 674
Cdd:cd14009 232 LLRRDPAER 240
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
419-681 1.19e-41

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  Cd Length: 258  Bit Score: 153.79  E-value: 1.19e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHsmlrRPT----AIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTPEGvFY 494
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVH----KKTgeeyAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKN-LY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 495 YAMEYLDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcEPDVVKVLDFGLvkAVDR 574
Cdd:cd05117  76 LVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD-PDSPIKIIDFGL--AKIF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 575 TEGSPANEgssMSGTPLYMSPESIQAPMTVDACsDIYAVGAVGYFLLTGKPVFEAANLVDLCQKhIEESPVP-PSKRGNv 653
Cdd:cd05117 153 EEGEKLKT---VCGTPYYVAPEVLKGKGYGKKC-DIWSLGVILYILLCGYPPFYGETEQELFEK-ILKGKYSfDSPEWK- 226
                       250       260
                ....*....|....*....|....*...
gi 32474612 654 KVSSQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:cd05117 227 NVSEEAKDLIKRLLVVDPKKRL-TAAEA 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
419-675 3.83e-41

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  Cd Length: 252  Bit Score: 151.90  E-value: 3.83e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTPeGVFYYAME 498
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETE-NKIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 499 YLDGIDLQDLVNKYG--TQSEARviHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGCepdvVKVLDFGLVKAVDRte 576
Cdd:cd14003  80 YASGGELFDYIVNNGrlSEDEAR--RFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN----LKIIDFGLSNEFRG-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 577 GSPANegsSMSGTPLYMSPESIQAPMTVDACSDIYAVGAVGYFLLTGKPVFEAANLVDLCQKHIEESPVPPSkrgnvKVS 656
Cdd:cd14003 152 GSLLK---TFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS-----HLS 223
                       250
                ....*....|....*....
gi 32474612 657 SQLEDAIMGCLEKSRAKRP 675
Cdd:cd14003 224 PDARDLIRRMLVVDPSKRI 242
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
419-681 2.20e-40

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  Cd Length: 258  Bit Score: 149.98  E-value: 2.20e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGhhsmLRRPT----AIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTpEGVFY 494
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLA----LNLDTgelmAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERT-ENTLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 495 YAMEYLDGIDLQDLVNKYGTQSEARVIHILLQIcgslFEA----HSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVK 570
Cdd:cd06606  76 IFLEYVPGGSLASLLKKFGKLPEPVVRKYTRQI----LEGleylHSNGIVHRDIKGANILVDSDG----VVKLADFGCAK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 571 AVDrtEGSPANEGSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVF-EAANLVDLCqKHI---EESPVP 646
Cdd:cd06606 148 RLA--EIATGEGTKSLRGTPYWMAPEVIRG-EGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAAL-FKIgssGEPPPI 223
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32474612 647 PSkrgnvKVSSQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:cd06606 224 PE-----HLSEEAKDFLRKCLQRDPKKRP-TADEL 252
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
420-681 3.61e-38

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  Cd Length: 254  Bit Score: 143.88  E-value: 3.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 420 YTLDQKLGEGAMGVVYKGHHSMLRRPTAIKllhadKVNDTSIARFE---REVQITCQLNHSNTIAIYDYGRTPEGVfYYA 496
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIK-----KINLESKEKKEsilNEIAILKKCKHPNIVKYYGSYLKKDEL-WIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 497 MEYLDGIDLQDLVNKY-GTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVkavdrT 575
Cdd:cd05122  76 MEFCSGGSLKDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG----EVKLIDFGLS-----A 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 576 EGSPANEGSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPvfeaanlvdlcqKHIEESPV---------- 645
Cdd:cd05122 147 QLSDGKTRNTFVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKP------------PYSELPPMkalfliatng 213
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32474612 646 PPSKRGNVKVSSQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:cd05122 214 PPGLRNPKKWSKEFKDFLKKCLQKDPEKRP-TAEQL 248
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
426-674 6.95e-38

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022  Cd Length: 256  Bit Score: 143.28  E-value: 6.95e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 426 LGEGAMGVVYKGHHSMLR-RPTAIKLlhadkVNDTSIAR----FEREVQITCQLNHSNTIAIYDYGRTPEGVfYYAMEYL 500
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKPdLPVAIKC-----ITKKNLSKsqnlLGKEIKILKELSHENVVALLDCQETSSSV-YLVMEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 501 DGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLN---RRGCEPD--VVKVLDFGLVKAVDrt 575
Cdd:cd14120  75 NGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShnsGRKPSPNdiRLKIADFGFARFLQ-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 576 EGSPAnegSSMSGTPLYMSPESIQApMTVDACSDIYAVGAVGYFLLTGKPVFEAAN---LVDLCQKHIEESPVPPSkrgn 652
Cdd:cd14120 153 DGMMA---ATLCGSPMYMAPEVIMS-LQYDAKADLWSIGTIVYQCLTGKAPFQAQTpqeLKAFYEKNANLRPNIPS---- 224
                       250       260
                ....*....|....*....|..
gi 32474612 653 vKVSSQLEDAIMGCLEKSRAKR 674
Cdd:cd14120 225 -GTSPALKDLLLGLLKRNPKDR 245
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
419-681 1.11e-36

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  Cd Length: 254  Bit Score: 139.67  E-value: 1.11e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 419 QYTLDQKLGEGAMGVVYKGHHSMLRRPTAIKLLHADKVNDTSIARFEREVQITCQLNHSNTIAIYDYGRTPEgVFYYAME 498
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKD-SLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 499 YLDGIDLQDLVNKYGTQSEARVIHILLQICGSLFEAHSQGLVHRDIKPANVMLNRRGcepdVVKVLDFGLVKAVDRTEGS 578
Cdd:cd06627  80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG----LVKLADFGVATKLNEVEKD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474612 579 PAnegsSMSGTPLYMSPESIQapMT-VDACSDIYAVGAVGYFLLTGKPVF----EAANLVDLCQKhiEESPVPPSkrgnv 653
Cdd:cd06627 156 EN----SVVGTPYWMAPEVIE--MSgVTTASDIWSVGCTVIELLTGNPPYydlqPMAALFRIVQD--DHPPLPEN----- 222
                       250       260
                ....*....|....*....|....*...
gi 32474612 654 kVSSQLEDAIMGCLEKSRAKRPqTARDL 681
Cdd:cd06627 223 -ISPELRDFLLQCFQKDPTLRP-SAKEL 248
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
426-636 7.15e-36

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, tis