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Conserved domains on  [gi|32477546|ref|NP_870540|]
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serine/threonine protein kinase [Rhodopirellula baltica SH 1]

Protein Classification

serine/threonine protein kinase (domain architecture ID 10195858)

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 ...
82-348 4.02e-98

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: 300.66  E-value: 4.02e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  82 GYELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMP 161
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGQHLGDWLAGlSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqttsGELRKPVVLDFGLCAHTDSTV 241
Cdd:cd14014  81 YVEGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL-----TEDGRVKLTDFGIARALGDSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 242 ATTT-RIAGTPRYIAPEQAMfgDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSDAM 320
Cdd:cd14014 155 LTQTgSVLGTPAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|....*...
gi 32477546 321 QAICLKCLRRDPDLRYESASALAADLQR 348
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAELLAALRA 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
82-348 4.02e-98

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: 300.66  E-value: 4.02e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  82 GYELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMP 161
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGQHLGDWLAGlSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqttsGELRKPVVLDFGLCAHTDSTV 241
Cdd:cd14014  81 YVEGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL-----TEDGRVKLTDFGIARALGDSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 242 ATTT-RIAGTPRYIAPEQAMfgDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSDAM 320
Cdd:cd14014 155 LTQTgSVLGTPAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|....*...
gi 32477546 321 QAICLKCLRRDPDLRYESASALAADLQR 348
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-343 8.24e-63

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 208.54  E-value: 8.24e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546     83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVavRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMPY 162
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR--ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    163 LTGQHLGDWLAGLSaPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCAHTDSTVA 242
Cdd:smart00220  79 CEGGDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL--DEDGHVK---LADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    243 TTTRIaGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSDAMQA 322
Cdd:smart00220 153 LTTFV-GTPEYMAPE--VLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKD 229
                          250       260
                   ....*....|....*....|.
gi 32477546    323 ICLKCLRRDPDLRYESASALA 343
Cdd:smart00220 230 LIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
82-351 5.03e-58

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 199.97  E-value: 5.03e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  82 GYELVKEIGRGGFGIVYLAHDqklKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPG-IISIYDCGVQDDLHYYVM 160
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 161 PYLTGQHLGDWLA--GLSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMQQttsgELRKPVVLDFGLCAHTD 238
Cdd:COG0515  78 EYVDGGSLEDLLKkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR----DGRVVKLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 239 STVAT------TTRIAGTPRYIAPEQAMFG-DRQITPKSDIYSLGVMLYQMLTGTTPL-APENFAEAVLMLHHASIDGPQ 310
Cdd:COG0515 154 DPGSTssipalPSTSVGTPGYMAPEVLLGLsLAYASSSSDIWSLGITLYELLTGLPPFeGEKNSSATSQTLKIILELPTP 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32477546 311 KHRPELSD--------AMQAICLKCLRRDPDLRYESASALAADLQRLIE 351
Cdd:COG0515 234 SLASPLSPsnpeliskAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLK 282
Pkinase pfam00069
Protein kinase domain;
83-343 5.00e-55

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 187.81  E-value: 5.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAvRRFQDEAQSAARLDHPGIISIYDCgVQDDLHYY-VMP 161
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDA-FEDKDNLYlVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546   162 YLTGQHLGDWLAGlSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMQQTtsGELRkpvVLDFGLCAHTDSTV 241
Cdd:pfam00069  79 YVEGGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDED--GNLK---ITDFGLARQLNSGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546   242 ATTTRiAGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENfaEAVLMLHHASIDGPQKHRPELSDAMQ 321
Cdd:pfam00069 153 SLTSF-VGTPWYMAPE--VLRGNPYGPKVDVWSLGCILYELLTGKPPFPGIN--GNEIYEKIIDQDFDSPRPSSISEEAK 227
                         250       260
                  ....*....|....*....|..
gi 32477546   322 AICLKCLRRDPDLRYESASALA 343
Cdd:pfam00069 228 DLLKKLLKKDPSKRLTATEALQ 249
pknD PRK13184
serine/threonine-protein kinase; Reviewed
80-354 5.54e-48

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 179.20  E-value: 5.54e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546   80 VGGYELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYV 159
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  160 MPYLTGQHLGDWLAG------LSAPMSELQAA----ELMIQIAGAVQYGHESGIIHRDLKPQNILMqqttsGELRKPVVL 229
Cdd:PRK13184  81 MPYIEGYTLKSLLKSvwqkesLSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILL-----GLFGEVVIL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  230 DFGLC--------------------AHTDSTVAttTRIAGTPRYIAPEQAMfgDRQITPKSDIYSLGVMLYQMLTGTTPL 289
Cdd:PRK13184 156 DWGAAifkkleeedlldidvderniCYSSMTIP--GKIVGTPDYMAPERLL--GVPASESTDIYALGVILYQMLTLSFPY 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32477546  290 APENFAEavLMLHHaSIDGPQKHRP--ELSDAMQAICLKCLRRDPDLRYESASALAADLQRLIEGEP 354
Cdd:PRK13184 232 RRKKGRK--ISYRD-VILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSP 295
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
109-343 5.09e-29

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: 121.88  E-value: 5.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    109 VAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGV-QDDLHYYVMPYLTGQHLGDWLAGlSAPMSELQAAEL 187
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAA-DGALPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    188 MIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRKPVVLDFGLCA------HTDSTVAT-TTRIAGTPRYIAPEQam 260
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMV--SQTGVRPHAKVLDFGIGTllpgvrDADVATLTrTTEVLGTPTYCAPEQ-- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    261 FGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEaVLMLHHASID-----GPQKHRpelsdaMQAICLKCLRRDPDLR 335
Cdd:TIGR03903  161 LRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAE-ILYQQLSPVDvslppWIAGHP------LGQVLRKALNKDPRQR 233

                   ....*...
gi 32477546    336 YESASALA 343
Cdd:TIGR03903  234 AASAPALA 241
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
82-348 4.02e-98

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: 300.66  E-value: 4.02e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  82 GYELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMP 161
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGQHLGDWLAGlSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqttsGELRKPVVLDFGLCAHTDSTV 241
Cdd:cd14014  81 YVEGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL-----TEDGRVKLTDFGIARALGDSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 242 ATTT-RIAGTPRYIAPEQAMfgDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSDAM 320
Cdd:cd14014 155 LTQTgSVLGTPAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|....*...
gi 32477546 321 QAICLKCLRRDPDLRYESASALAADLQR 348
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-343 8.24e-63

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 208.54  E-value: 8.24e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546     83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVavRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMPY 162
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR--ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    163 LTGQHLGDWLAGLSaPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCAHTDSTVA 242
Cdd:smart00220  79 CEGGDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL--DEDGHVK---LADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    243 TTTRIaGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSDAMQA 322
Cdd:smart00220 153 LTTFV-GTPEYMAPE--VLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKD 229
                          250       260
                   ....*....|....*....|.
gi 32477546    323 ICLKCLRRDPDLRYESASALA 343
Cdd:smart00220 230 LIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
82-351 5.03e-58

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 199.97  E-value: 5.03e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  82 GYELVKEIGRGGFGIVYLAHDqklKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPG-IISIYDCGVQDDLHYYVM 160
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 161 PYLTGQHLGDWLA--GLSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMQQttsgELRKPVVLDFGLCAHTD 238
Cdd:COG0515  78 EYVDGGSLEDLLKkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR----DGRVVKLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 239 STVAT------TTRIAGTPRYIAPEQAMFG-DRQITPKSDIYSLGVMLYQMLTGTTPL-APENFAEAVLMLHHASIDGPQ 310
Cdd:COG0515 154 DPGSTssipalPSTSVGTPGYMAPEVLLGLsLAYASSSSDIWSLGITLYELLTGLPPFeGEKNSSATSQTLKIILELPTP 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32477546 311 KHRPELSD--------AMQAICLKCLRRDPDLRYESASALAADLQRLIE 351
Cdd:COG0515 234 SLASPLSPsnpeliskAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLK 282
Pkinase pfam00069
Protein kinase domain;
83-343 5.00e-55

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 187.81  E-value: 5.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546    83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAvRRFQDEAQSAARLDHPGIISIYDCgVQDDLHYY-VMP 161
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDA-FEDKDNLYlVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546   162 YLTGQHLGDWLAGlSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMQQTtsGELRkpvVLDFGLCAHTDSTV 241
Cdd:pfam00069  79 YVEGGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDED--GNLK---ITDFGLARQLNSGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546   242 ATTTRiAGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENfaEAVLMLHHASIDGPQKHRPELSDAMQ 321
Cdd:pfam00069 153 SLTSF-VGTPWYMAPE--VLRGNPYGPKVDVWSLGCILYELLTGKPPFPGIN--GNEIYEKIIDQDFDSPRPSSISEEAK 227
                         250       260
                  ....*....|....*....|..
gi 32477546   322 AICLKCLRRDPDLRYESASALA 343
Cdd:pfam00069 228 DLLKKLLKKDPSKRLTATEALQ 249
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
83-343 1.62e-52

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: 181.14  E-value: 1.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKvAVRRFQDEAQSAARLDHPGIISIYDCgVQDDLHYY-VMP 161
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRLDHPNIVKLYEV-FEDDKNLYlVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGQHLGDWLAGLSApMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqQTTSGELrkPVVL-DFGLCAHTDST 240
Cdd:cd05117  80 LCTGGELFDRIVKKGS-FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILL-ASKDPDS--PIKIiDFGLAKIFEEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 241 VATTTRiAGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSD-A 319
Cdd:cd05117 156 EKLKTV-CGTPYYVAPE--VLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEeA 232
                       250       260
                ....*....|....*....|....
gi 32477546 320 MQAIClKCLRRDPDLRYESASALA 343
Cdd:cd05117 233 KDLIK-RLLVVDPKKRLTAAEALN 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
83-335 6.08e-51

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: 177.01  E-value: 6.08e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKvavRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMPY 162
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKK---ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 163 LTGQHLGDWLAGLSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCAHTDSTVA 242
Cdd:cd05122  79 CSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILL--TSDGEVK---LIDFGLSAQLSDGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 243 TTTRIaGTPRYIAPEQAMfgDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLML---HHASIDGPQKHRPELSDa 319
Cdd:cd05122 154 RNTFV-GTPYWMAPEVIQ--GKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIatnGPPGLRNPKKWSKEFKD- 229
                       250
                ....*....|....*.
gi 32477546 320 mqaICLKCLRRDPDLR 335
Cdd:cd05122 230 ---FLKKCLQKDPEKR 242
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
89-342 8.87e-49

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  Cd Length: 215  Bit Score: 169.76  E-value: 8.87e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  89 IGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVavRRFQDEAQSAARLDHPGIISIYDCgVQDDLHYY-VMPYLTGQH 167
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLL--EELLREIEILKKLNHPNIVKLYDV-FETENFLYlVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 168 LGDWLAGLSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqttsGELRKPVVLDFGLCAHTDSTVATTTRI 247
Cdd:cd00180  78 LKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL-----DSDGTVKLADFGLAKDLDSDDSLLKTT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 248 AGTPRYIAPEQAMFGDRQITPKSDIYSLGVMLYQMltgttplapenfaeavlmlhhasidgpqkhrPELSDAMQaiclKC 327
Cdd:cd00180 153 GGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIR----RM 197
                       250
                ....*....|....*
gi 32477546 328 LRRDPDLRYeSASAL 342
Cdd:cd00180 198 LQYDPKKRP-SAKEL 211
pknD PRK13184
serine/threonine-protein kinase; Reviewed
80-354 5.54e-48

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 179.20  E-value: 5.54e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546   80 VGGYELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYV 159
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  160 MPYLTGQHLGDWLAG------LSAPMSELQAA----ELMIQIAGAVQYGHESGIIHRDLKPQNILMqqttsGELRKPVVL 229
Cdd:PRK13184  81 MPYIEGYTLKSLLKSvwqkesLSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILL-----GLFGEVVIL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  230 DFGLC--------------------AHTDSTVAttTRIAGTPRYIAPEQAMfgDRQITPKSDIYSLGVMLYQMLTGTTPL 289
Cdd:PRK13184 156 DWGAAifkkleeedlldidvderniCYSSMTIP--GKIVGTPDYMAPERLL--GVPASESTDIYALGVILYQMLTLSFPY 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32477546  290 APENFAEavLMLHHaSIDGPQKHRP--ELSDAMQAICLKCLRRDPDLRYESASALAADLQRLIEGEP 354
Cdd:PRK13184 232 RRKKGRK--ISYRD-VILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSP 295
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
83-336 9.04e-46

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: 162.69  E-value: 9.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVaVRRFQDEAQSAARLDHPGIISIYDCgVQDDLHYY-VMP 161
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEI-EEKIKREIEIMKLLNHPNIIKLYEV-IETENKIYlVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGQHLGDWL--AGlsaPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCAHTDS 239
Cdd:cd14003  80 YASGGELFDYIvnNG---RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL--DKNGNLK---IIDFGLSNEFRG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 240 TVATTTRIaGTPRYIAPEqaMFGDRQ-ITPKSDIYSLGVMLYQMLTGTTPLAPENFAEavlmLHHASIDGPQKHRPELSD 318
Cdd:cd14003 152 GSLLKTFC-GTPAYAAPE--VLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSK----LFRKILKGKYPIPSHLSP 224
                       250
                ....*....|....*...
gi 32477546 319 AMQAICLKCLRRDPDLRY 336
Cdd:cd14003 225 DARDLIRRMLVVDPSKRI 242
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
89-335 3.26e-42

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  Cd Length: 245  Bit Score: 152.69  E-value: 3.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  89 IGRGGFGIVYLAhdqKLK-RDVAIKIARPEVVSDKVaVRRFQDEAQSAARLDHPGIISIYdcGV-QDDLHYY-VMPYLTG 165
Cdd:cd13999   1 IGSGSFGEVYKG---KWRgTDVAIKKLKVEDDNDEL-LKEFRREVSILSKLRHPNIVQFI--GAcLSPPPLCiVTEYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 166 QHLGDWLAGLSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMQqttsgELRKPVVLDFGLCAHTDSTVATTT 245
Cdd:cd13999  75 GSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLD-----ENFTVKIADFGLSRIKNSTTEKMT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 246 RIAGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTP---LAPENFAEAVLMlhhasiDGPQKHRPE-LSDAMQ 321
Cdd:cd13999 150 GVVGTPRWMAPE--VLRGEPYTEKADVYSFGIVLWELLTGEVPfkeLSPIQIAAAVVQ------KGLRPPIPPdCPPELS 221
                       250
                ....*....|....
gi 32477546 322 AICLKCLRRDPDLR 335
Cdd:cd13999 222 KLIKRCWNEDPEKR 235
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
83-335 5.87e-41

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  Cd Length: 253  Bit Score: 149.55  E-value: 5.87e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCgVQDDLH-YYVMP 161
Cdd:cd14007   2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGY-FEDKKRiYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGQHLGDWLAGLsAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCAHTDSTV 241
Cdd:cd14007  81 YAPNGELYKELKKQ-KRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILL--GSNGELK---LADFGWSVHAPSNR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 242 ATTtrIAGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHRPELSDamq 321
Cdd:cd14007 155 RKT--FCGTLDYLPPE--MVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKD--- 227
                       250
                ....*....|....
gi 32477546 322 aICLKCLRRDPDLR 335
Cdd:cd14007 228 -LISKLLQKDPSKR 240
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
82-335 1.08e-39

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: 146.07  E-value: 1.08e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  82 GYELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKvAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMP 161
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEK-EREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162 YLTGqhlGDWLAGLSA------PMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCA 235
Cdd:cd08215  80 YADG---GDLAQKIKKqkkkgqPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFL--TKDGVVK---LGDFGISK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 236 HTDSTVATTTRIAGTPRYIAPEqaMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKHrpe 315
Cdd:cd08215 152 VLESTTDLAKTVVGTPYYLSPE--LCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQ--- 226
                       250       260
                ....*....|....*....|
gi 32477546 316 LSDAMQAICLKCLRRDPDLR 335
Cdd:cd08215 227 YSSELRDLVNSMLQKDPEKR 246
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
83-335 1.20e-39

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001  Cd Length: 258  Bit Score: 145.77  E-value: 1.20e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIARPEVVSDKVAVRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMPY 162
Cdd:cd14099   3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 163 LTGQHLGDWLAGlSAPMSELQAAELMIQIAGAVQYGHESGIIHRDLKPQNILMqqTTSGELRkpvVLDFGLCAHTDSTVA 242
Cdd:cd14099  83 CSNGSLMELLKR-RKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL--DENMNVK---IGDFGLAARLEYDGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 243 TTTRIAGTPRYIAPEqAMFGDRQITPKSDIYSLGVMLYQMLTGTTPLAPENFAEAVLMLHHASIDGPQKhrPELSDAMQA 322
Cdd:cd14099 157 RKKTLCGTPNYIAPE-VLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAKD 233
                       250
                ....*....|...
gi 32477546 323 ICLKCLRRDPDLR 335
Cdd:cd14099 234 LIRSMLQPDPTKR 246
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
83-342 2.41e-39

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: 144.97  E-value: 2.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546  83 YELVKEIGRGGFGIVYLAHDQKLKRDVAIKIArpEVVSDKVA-VRRFQDEAQSAARLDHPGIISIYDCGVQDDLHYYVMP 161
Cdd:cd06606   2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEV--ELSGDSEEeLEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477546 162