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Conserved domains on  [gi|568973183|ref|XP_006533023|]
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serine/threonine-protein kinase TAO1 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
11-70 1.80e-30

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd06635:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 317  Bit Score: 122.47  E-value: 1.80e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 70
Cdd:cd06635  258 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 317
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-499 4.13e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   201 RQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLE-NKLKAEMDEHRLRLdKDLETQRNNFAAEMEKL---IKKHQAAMEK 276
Cdd:TIGR02168  200 RQLKSLERQAEKAERYKELKAELRELELALLVLRlEELREELEELQEEL-KEAEEELEELTAELQELeekLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   277 EAKVMANEEKKFQQHIQAQQKkelnsfLESQKREYKLRKEQLK-------EELNENQSTpKKEKQEWLSKQKENIQhfQA 349
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISR------LEQQKQILRERLANLErqleeleAQLEELESK-LDELAEELAELEEKLE--EL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   350 EEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQdlVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCEL 429
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLET--LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   430 IRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKAlRNHLLET 499
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLER 496
PRP super family cl46992
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
656-713 9.41e-04

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.


The actual alignment was detected with superfamily member smart00157:

Pssm-ID: 197548 [Multi-domain]  Cd Length: 218  Bit Score: 41.39  E-value: 9.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568973183   656 YPGASSWSHNPTGGPGPHWGHPMGGtpqAWGHPMQGGpqpWGHPSGPMQGVPRGSSMG 713
Cdd:smart00157  17 YPGQGSPGGNRYPPQGGGWGQPHGG---GWGQPHGGG---WGQPHGGGWGQPHGGGWG 68
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
521-637 2.28e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 521 AILAEQYDHSINEMLSTqALRLDEAQEAECQVLK---MQLQQELELLNAYQSKIKMQAEAQhDRELRELEQRVSLRRALL 597
Cdd:COG2433  380 EALEELIEKELPEEEPE-AEREKEHEERELTEEEeeiRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEE 457
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568973183 598 EQKI--EEEMLALQNErTERIRSLLERQAREIEAFDSESMRL 637
Cdd:COG2433  458 RREIrkDREISRLDRE-IERLERELEEERERIEELKRKLERL 498
 
Name Accession Description Interval E-value
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
11-70 1.80e-30

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 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: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 122.47  E-value: 1.80e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 70
Cdd:cd06635  258 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 317
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-499 4.13e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   201 RQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLE-NKLKAEMDEHRLRLdKDLETQRNNFAAEMEKL---IKKHQAAMEK 276
Cdd:TIGR02168  200 RQLKSLERQAEKAERYKELKAELRELELALLVLRlEELREELEELQEEL-KEAEEELEELTAELQELeekLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   277 EAKVMANEEKKFQQHIQAQQKkelnsfLESQKREYKLRKEQLK-------EELNENQSTpKKEKQEWLSKQKENIQhfQA 349
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISR------LEQQKQILRERLANLErqleeleAQLEELESK-LDELAEELAELEEKLE--EL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   350 EEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQdlVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCEL 429
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLET--LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   430 IRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKAlRNHLLET 499
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLER 496
PTZ00121 PTZ00121
MAEBL; Provisional
152-628 4.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  152 KPEEENYQEEgdpRTRASDPQSPPQVSRHKSHYRNREH---FATIRTASLVTRQM----QEHEQDSELR--EQMSGYKRM 222
Cdd:PTZ00121 1219 KAEDAKKAEA---VKKAEEAKKDAEEAKKAEEERNNEEirkFEEARMAHFARRQAaikaEEARKADELKkaEEKKKADEA 1295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  223 RRQHQKQLMTlENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKL--IKKHQAAMEKEAKVMANEEKKFQQHIQAQQKK-- 298
Cdd:PTZ00121 1296 KKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKke 1374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  299 -------ELNSFLESQKR--EYKLRKEQLKEELNE-NQSTPKKEKQEWLSKQKENIQhfQAEEEANLLRRQRQYLELECR 368
Cdd:PTZ00121 1375 eakkkadAAKKKAEEKKKadEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKADEAKKK 1452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  369 -RFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKR 447
Cdd:PTZ00121 1453 aEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  448 RERELRRKHVMEVRQQPKSLKSKEL---QIKKQFQDTCKIQTRQYKALRN-HLLETTPKSEHKAVLKRLKEEQTRKlail 523
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELkkaEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMK---- 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  524 AEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQEL---ELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQK 600
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
                         490       500
                  ....*....|....*....|....*...
gi 568973183  601 IEEEMLALQNERTERIRSLLERQAREIE 628
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKK 1716
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
217-572 5.66e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   217 SGYKRMRRQHQKQLM-TLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVmaNEEKKFQQHIQAQ 295
Cdd:pfam02463  165 SRLKRKKKEALKKLIeETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL--DYLKLNEERIDLL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   296 QKKELNsflESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANllrrQRQYLELECRRFKRRML 375
Cdd:pfam02463  243 QELLRD---EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL----KSELLKLERRKVDDEEK 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   376 LGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRcELIRLQHQTELTNQLEYNKRRERELRRK 455
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE-KLEQLEEELLAKKKLESERLSSAAKLKE 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   456 HVMEVRQQPKSLKSKELQIKKQFQDtckiqtrQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEML 535
Cdd:pfam02463  395 EELELKSEEEKEAQLLLELARQLED-------LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568973183   536 STQAlrlDEAQEAECQVLKMQLQQELELLNAYQSKIK 572
Cdd:pfam02463  468 KKSE---DLLKETQLVKLQEQLELLLSRQKLEERSQK 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
304-626 1.57e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 304 LESQK---REYKlrkeQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHN 380
Cdd:COG1196  205 LERQAekaERYR----ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 381 LEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEfrhlNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEV 460
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 461 RQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLlettpkSEHKAVLKRLKEEQTRKLAILAEQydhsinEMLSTQAL 540
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERL------ERLEEELE 424
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 541 RLDEAQEAECQVLKMQLQQELELLnayqskikmQAEAQHDRELRELEQRVSLRRALLEQkieeemlaLQNERTERIRSLL 620
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAA---------EEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELA 487

                 ....*.
gi 568973183 621 ERQARE 626
Cdd:COG1196  488 EAAARL 493
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
656-713 9.41e-04

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.


Pssm-ID: 197548 [Multi-domain]  Cd Length: 218  Bit Score: 41.39  E-value: 9.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568973183   656 YPGASSWSHNPTGGPGPHWGHPMGGtpqAWGHPMQGGpqpWGHPSGPMQGVPRGSSMG 713
Cdd:smart00157  17 YPGQGSPGGNRYPPQGGGWGQPHGG---GWGQPHGGG---WGQPHGGGWGQPHGGGWG 68
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
521-637 2.28e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 521 AILAEQYDHSINEMLSTqALRLDEAQEAECQVLK---MQLQQELELLNAYQSKIKMQAEAQhDRELRELEQRVSLRRALL 597
Cdd:COG2433  380 EALEELIEKELPEEEPE-AEREKEHEERELTEEEeeiRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEE 457
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568973183 598 EQKI--EEEMLALQNErTERIRSLLERQAREIEAFDSESMRL 637
Cdd:COG2433  458 RREIrkDREISRLDRE-IERLERELEEERERIEELKRKLERL 498
PRK12704 PRK12704
phosphodiesterase; Provisional
515-627 7.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 7.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 515 EQTRKLAILA--EQYDHSINEMLSTQALRLDEAQEAECQVL--KMQLQQELELLNAYQSKIKmqaeaQHDRELRELEQRV 590
Cdd:PRK12704  52 EAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLqkEENLDRKLELLEKREEELE-----KKEKELEQKQQEL 126
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568973183 591 SLRRALLEQKIEEemlalQNERTERIRSLLERQAREI 627
Cdd:PRK12704 127 EKKEEELEELIEE-----QLQELERISGLTAEEAKEI 158
 
Name Accession Description Interval E-value
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
11-70 1.80e-30

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 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: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 122.47  E-value: 1.80e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 70
Cdd:cd06635  258 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 317
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
11-70 4.12e-28

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 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: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 115.52  E-value: 4.12e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQ 70
Cdd:cd06633  254 DYCLQKIPQERPSSAELLRHDFVRRERPPRVLIDLIQRTKDAVRELDNLQYRKMKKILFQ 313
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
11-71 2.23e-27

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 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: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 113.19  E-value: 2.23e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQE 71
Cdd:cd06634  248 DSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLIQRTKDAVRELDNLQYRKMKKILFQE 308
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
11-35 2.52e-07

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO 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: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 52.84  E-value: 2.52e-07
                         10        20
                 ....*....|....*....|....*
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLR 35
Cdd:cd06607  234 DSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
11-50 3.34e-06

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-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: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 49.55  E-value: 3.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTK 50
Cdd:cd06609  232 ELCLNKDPKERPSAKELLKHKFIKKAKKTSYLTLLIERIK 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-499 4.13e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   201 RQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLE-NKLKAEMDEHRLRLdKDLETQRNNFAAEMEKL---IKKHQAAMEK 276
Cdd:TIGR02168  200 RQLKSLERQAEKAERYKELKAELRELELALLVLRlEELREELEELQEEL-KEAEEELEELTAELQELeekLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   277 EAKVMANEEKKFQQHIQAQQKkelnsfLESQKREYKLRKEQLK-------EELNENQSTpKKEKQEWLSKQKENIQhfQA 349
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISR------LEQQKQILRERLANLErqleeleAQLEELESK-LDELAEELAELEEKLE--EL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   350 EEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQdlVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCEL 429
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLET--LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   430 IRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKAlRNHLLET 499
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLER 496
PTZ00121 PTZ00121
MAEBL; Provisional
152-628 4.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  152 KPEEENYQEEgdpRTRASDPQSPPQVSRHKSHYRNREH---FATIRTASLVTRQM----QEHEQDSELR--EQMSGYKRM 222
Cdd:PTZ00121 1219 KAEDAKKAEA---VKKAEEAKKDAEEAKKAEEERNNEEirkFEEARMAHFARRQAaikaEEARKADELKkaEEKKKADEA 1295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  223 RRQHQKQLMTlENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKL--IKKHQAAMEKEAKVMANEEKKFQQHIQAQQKK-- 298
Cdd:PTZ00121 1296 KKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKke 1374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  299 -------ELNSFLESQKR--EYKLRKEQLKEELNE-NQSTPKKEKQEWLSKQKENIQhfQAEEEANLLRRQRQYLELECR 368
Cdd:PTZ00121 1375 eakkkadAAKKKAEEKKKadEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKADEAKKK 1452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  369 -RFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKR 447
Cdd:PTZ00121 1453 aEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  448 RERELRRKHVMEVRQQPKSLKSKEL---QIKKQFQDTCKIQTRQYKALRN-HLLETTPKSEHKAVLKRLKEEQTRKlail 523
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELkkaEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMK---- 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  524 AEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQEL---ELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQK 600
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
                         490       500
                  ....*....|....*....|....*...
gi 568973183  601 IEEEMLALQNERTERIRSLLERQAREIE 628
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKK 1716
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
217-572 5.66e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   217 SGYKRMRRQHQKQLM-TLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVmaNEEKKFQQHIQAQ 295
Cdd:pfam02463  165 SRLKRKKKEALKKLIeETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL--DYLKLNEERIDLL 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   296 QKKELNsflESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANllrrQRQYLELECRRFKRRML 375
Cdd:pfam02463  243 QELLRD---EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL----KSELLKLERRKVDDEEK 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   376 LGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRcELIRLQHQTELTNQLEYNKRRERELRRK 455
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE-KLEQLEEELLAKKKLESERLSSAAKLKE 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   456 HVMEVRQQPKSLKSKELQIKKQFQDtckiqtrQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEML 535
Cdd:pfam02463  395 EELELKSEEEKEAQLLLELARQLED-------LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568973183   536 STQAlrlDEAQEAECQVLKMQLQQELELLNAYQSKIK 572
Cdd:pfam02463  468 KKSE---DLLKETQLVKLQEQLELLLSRQKLEERSQK 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
304-626 1.57e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 304 LESQK---REYKlrkeQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHN 380
Cdd:COG1196  205 LERQAekaERYR----ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 381 LEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEfrhlNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEV 460
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 461 RQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLlettpkSEHKAVLKRLKEEQTRKLAILAEQydhsinEMLSTQAL 540
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERL------ERLEEELE 424
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 541 RLDEAQEAECQVLKMQLQQELELLnayqskikmQAEAQHDRELRELEQRVSLRRALLEQkieeemlaLQNERTERIRSLL 620
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAA---------EEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELA 487

                 ....*.
gi 568973183 621 ERQARE 626
Cdd:COG1196  488 EAAARL 493
PTZ00121 PTZ00121
MAEBL; Provisional
201-443 2.00e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  201 RQMQEHEQDSELR--EQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRlRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEA 278
Cdd:PTZ00121 1546 KKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  279 KVMANEEKKFQQHIQAQQKKELNSFLESQKRE--YKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLL 356
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  357 RRQRQYLELECRRFKRRmllgRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESmQELEFRHLNTIQKMRCELIRLQHQT 436
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-EKKKIAHLKKEEEKKAEEIRKEKEA 1779

                  ....*..
gi 568973183  437 ELTNQLE 443
Cdd:PTZ00121 1780 VIEEELD 1786
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
223-629 7.29e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 223 RRQHQKQLMTLENKLKAEMDEHRLrLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMANEEKKFQQHIQAQQKKELNS 302
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 303 FLESQKREYKLRKEQLKEELNENQstpkkEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRmllgrhNLE 382
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELE-----EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA------EEL 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 383 QDLVREELNKRQTQKDLEhamllRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQ 462
Cdd:COG1196  389 LEALRAAAELAAQLEELE-----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 463 QPKSLKSKELQIKKQFQDTcKIQTRQYKALRNHLLETTPKSEHK--AVLKRLKEEQTRKLAIL----------AEQYDHS 530
Cdd:COG1196  464 LLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGFleGVKAALLLAGLRGLAGAvavligveaaYEAALEA 542
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 531 INEMLSTQALRLDEAQEAEC-QVLKMQLQQELELLNAyqSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQ 609
Cdd:COG1196  543 ALAAALQNIVVEDDEVAAAAiEYLKAAKAGRATFLPL--DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
                        410       420
                 ....*....|....*....|
gi 568973183 610 NERTERIRSLLERQAREIEA 629
Cdd:COG1196  621 TLLGRTLVAARLEAALRRAV 640
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
204-496 1.10e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   204 QEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEhrlrldkdLETQRNNFAAEMEKLIKkhqaamEKEAKVMAN 283
Cdd:pfam02463  213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE--------IESSKQEIEKEEEKLAQ------VLKENKEEE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   284 EEKKFQQHIQAQQKKELNSfLESQKREYKLRKEQLKEELNENQSTPKKEKQEwLSKQKENIQHFQAEEEanLLRRQRQYL 363
Cdd:pfam02463  279 KEKKLQEEELKLLAKEEEE-LKSELLKLERRKVDDEEKLKESEKEKKKAEKE-LKKEKEEIEELEKELK--ELEIKREAE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   364 ELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLE 443
Cdd:pfam02463  355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   444 ynKRRERELRRKHVMEVRQQPKSLKSKEL-------QIKKQFQDTCKIQTRQYKALRNHL 496
Cdd:pfam02463  435 --EEESIELKQGKLTEEKEELEKQELKLLkdelelkKSEDLLKETQLVKLQEQLELLLSR 492
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
201-353 2.39e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 201 RQMQEHEQDSELRE-QMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAK 279
Cdd:PRK09510  81 RKKKEQQQAEELQQkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973183 280 VMANEEKKFQQHIQAQQKKElnsfLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEA 353
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAA----AEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA 230
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
226-376 3.28e-04

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 41.39  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  226 HQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHqaamekeakvmANEEKKFQQHIQAQQKKELNSFLE 305
Cdd:pfam12474   1 HQLQKEQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQ-----------TQELRRLPKRIRAEQKKRLKMFRE 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568973183  306 SQKREYKLRKeqlkeelNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRF---KRRMLL 376
Cdd:pfam12474  70 SLKQEKKELK-------QEVEKLPKFQRKEAKRQRKEELELEQKHEELEFLQAQSEALERELQQLqneKRKELA 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
238-603 4.11e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   238 KAEMDEHRLRLdKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMANEEKKFQQHIQAQQKKElnsFLESQKREYKLRKEQ 317
Cdd:TIGR02168  676 RREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA---RLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   318 LKEELNEnqstpKKEKQEWLSKQKEniqhfQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLE--QDLVREeLNKRQT 395
Cdd:TIGR02168  752 LSKELTE-----LEAEIEELEERLE-----EAEEELAEAEAEIEELEAQIEQLKEELKALREALDelRAELTL-LNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   396 QKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTEltnQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIK 475
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE---ELEELIEELESELEALLNERASLEEALALLRSELE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   476 KQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVlkM 555
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL--K 975
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568973183   556 QLQQELELLNAyqskIKMQAEAQHdRELRE-----LEQRVSLRRAL--LEQKIEE 603
Cdd:TIGR02168  976 RLENKIKELGP----VNLAAIEEY-EELKErydflTAQKEDLTEAKetLEEAIEE 1025
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
11-33 5.32e-04

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 42.58  E-value: 5.32e-04
                         10        20
                 ....*....|....*....|...
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFV 33
Cdd:cd05122  232 KKCLQKDPEKRPTAEQLLKHPFI 254
PTZ00121 PTZ00121
MAEBL; Provisional
152-614 5.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  152 KPEEENYQEEGDPRTRASDPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQlm 231
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK-- 1399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  232 TLENKLKAEmdehRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMANEEKKFQQhiQAQQKKELNSFLESQKREY 311
Cdd:PTZ00121 1400 AEEDKKKAD----ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKAD 1473
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  312 KLRK---EQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVR- 387
Cdd:PTZ00121 1474 EAKKkaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  388 -EELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRErelrrkhvmEVRQQPKS 466
Cdd:PTZ00121 1554 aEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE---------EAKIKAEE 1624
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  467 LKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEhKAVLKRLKEEQTRKlailaeqydhsinemlstqALRLDEAQ 546
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKAEEDKKK-------------------AEEAKKAE 1684
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973183  547 EAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTE 614
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
172-424 7.78e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  172 QSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLM--TLENKLKAEMDEHRLRLD 249
Cdd:pfam17380 303 QEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELerIRQEEIAMEISRMRELER 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  250 KDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMANEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTP 329
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  330 KKEKQEWLSKQKENIQHFQAEEEANLLRRQ-RQYLELECRRFKRRMLlgRHNLEQDLVREELNKRQTQKDLEHAMLLRQH 408
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQrRKILEKELEERKQAMI--EEERKRKLLEKEMEERQKAIYEEERRREAEE 540
                         250
                  ....*....|....*.
gi 568973183  409 ESMQELEFRHLNTIQK 424
Cdd:pfam17380 541 ERRKQQEMEERRRIQE 556
PRP smart00157
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ...
656-713 9.41e-04

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.


Pssm-ID: 197548 [Multi-domain]  Cd Length: 218  Bit Score: 41.39  E-value: 9.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568973183   656 YPGASSWSHNPTGGPGPHWGHPMGGtpqAWGHPMQGGpqpWGHPSGPMQGVPRGSSMG 713
Cdd:smart00157  17 YPGQGSPGGNRYPPQGGGWGQPHGG---GWGQPHGGG---WGQPHGGGWGQPHGGGWG 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
198-475 1.28e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   198 LVTRQMQEHEQDSELREQMSGYKRMRRQHQKQlmtlenklkAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKe 277
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQL---------EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE- 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   278 akvMANEEKKFQQhiQAQQKKELNSFLESQKREYKLRKE-----QLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEE 352
Cdd:TIGR02168  784 ---IEELEAQIEQ--LKEELKALREALDELRAELTLLNEeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   353 ANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREEL-NKRQTQKDLEHAM--LLRQHESMQELEFRHLNTIQKMRCEL 429
Cdd:TIGR02168  859 AEIEELEELIEELESELEALLNERASLEEALALLRSELeELSEELRELESKRseLRRELEELREKLAQLELRLEGLEVRI 938
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 568973183   430 IRLQHQteLTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIK 475
Cdd:TIGR02168  939 DNLQER--LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
201-637 1.54e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   201 RQMQEHEQDSELREQMSGYKRMRRQHQKQlmTLENKLKAEMDEHRLRLDKDLETQRNNFA-------------AEMEKLI 267
Cdd:pfam02463  246 LRDEQEEIESSKQEIEKEEEKLAQVLKEN--KEEEKEKKLQEEELKLLAKEEEELKSELLklerrkvddeeklKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   268 KKHQAAMEKEAKVMANEEK--KFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQK---- 341
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKelKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELksee 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   342 -----ENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDlehaMLLRQHESMQELEF 416
Cdd:pfam02463  404 ekeaqLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL----ELKKSEDLLKETQL 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   417 RHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVmEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHL 496
Cdd:pfam02463  480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV-GGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   497 LETTPKSEHKAVLKRLKEEQTRKLAILAEQ---YDHSINEMLSTQALRLDEAQEAECQ------VLKMQLQQELELLNAY 567
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKlplKSIAVLEIDPILNLAQLDKATLEADeddkraKVVEGILKDTELTKLK 638
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   568 QSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRL 637
Cdd:pfam02463  639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
9-32 1.57e-03

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK 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: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 41.19  E-value: 1.57e-03
                         10        20
                 ....*....|....*....|....
gi 568973183   9 MNDSCLQKIPQDRPTSEELLKHMF 32
Cdd:cd06610  243 MISLCLQKDPSKRPTAEELLKHKF 266
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
11-50 1.85e-03

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 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: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 40.81  E-value: 1.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568973183  11 DSCLQKIPQDRPTSEELLKHMFVLRERPET-VLIDLIQRTK 50
Cdd:cd06642  234 EACLNKDPRFRPTAKELLKHKFITRYTKKTsFLTELIDRYK 274
PRK12704 PRK12704
phosphodiesterase; Provisional
263-437 2.19e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 263 MEKLIKKHQAAMEKEAKVMANEEKKFQQHIqaQQKKELNsflesQKREYKLRKEQLKEELNENQStpKKEKQEWLSKQKE 342
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAI--KKEALLE-----AKEEIHKLRNEFEKELRERRN--ELQKLEKRLLQKE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 343 NiqhfQAEEEANLLRRQRQYLELECRRFKRRMllgrHNLEQdlVREELNKRQTQ--KDLEHAMLLRQHESMQELefrhL- 419
Cdd:PRK12704  96 E----NLDRKLELLEKREEELEKKEKELEQKQ----QELEK--KEEELEELIEEqlQELERISGLTAEEAKEIL----Le 161
                        170
                 ....*....|....*...
gi 568973183 420 NTIQKMRCELIRLQHQTE 437
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIE 179
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
521-637 2.28e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 521 AILAEQYDHSINEMLSTqALRLDEAQEAECQVLK---MQLQQELELLNAYQSKIKMQAEAQhDRELRELEQRVSLRRALL 597
Cdd:COG2433  380 EALEELIEKELPEEEPE-AEREKEHEERELTEEEeeiRRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEE 457
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568973183 598 EQKI--EEEMLALQNErTERIRSLLERQAREIEAFDSESMRL 637
Cdd:COG2433  458 RREIrkDREISRLDRE-IERLERELEEERERIEELKRKLERL 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
349-622 3.81e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   349 AEEEANLLRRQRQYLELE--CRRFKRRMLLGRHNLEQDLV-REELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKM 425
Cdd:TIGR02168  666 AKTNSSILERRREIEELEekIEELEEKIAELEKALAELRKeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   426 RCELIRLQHQ-TELTNQLEyNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSE 504
Cdd:TIGR02168  746 EERIAQLSKElTELEAEIE-ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183   505 HKAVLKRLKEEQTRKLAILAEQ----------YDHSINEMlsTQALRLDEAQEAECQVLKMQLQQELELLNAyqskikmq 574
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQieelsediesLAAEIEEL--EELIEELESELEALLNERASLEEALALLRS-------- 894
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 568973183   575 AEAQHDRELRELEQRVS-LRRALLEQKIEEEMLALQNERTE-RIRSLLER 622
Cdd:TIGR02168  895 ELEELSEELRELESKRSeLRRELEELREKLAQLELRLEGLEvRIDNLQER 944
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
236-325 3.81e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.98  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183  236 KLKAEMDEHRLR-LDKDLETQRNNFAAEMEKLIKKHQaAMEKEAKVMANEEKKFQQHIQAQQKKELNSFLESQKREYKLR 314
Cdd:pfam03961 144 EIEVGVDFPELKeKLEELEKELEELEEELEKLKKRLK-KLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEELKEL 222
                          90
                  ....*....|.
gi 568973183  315 KEQLKEELNEN 325
Cdd:pfam03961 223 KEELESLLGEG 233
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
459-617 3.85e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 459 EVRQQPKSLKSKELQIKKQFQDTCKI-----QTRQYKALRNHLLETtpKSEHKAVLKRLKEEQTRKLAILAEQydHSINE 533
Cdd:COG3206  230 EARAELAEAEARLAALRAQLGSGPDAlpellQSPVIQQLRAQLAEL--EAELAELSARYTPNHPDVIALRAQI--AALRA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 534 MLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQhdRELRELEQRVSLRRALLE---QKIEEEMLAlQN 610
Cdd:COG3206  306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE--AELRRLEREVEVARELYEsllQRLEEARLA-EA 382

                 ....*..
gi 568973183 611 ERTERIR 617
Cdd:COG3206  383 LTVGNVR 389
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
12-47 4.64e-03

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-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: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 39.73  E-value: 4.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 568973183  12 SCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQ 47
Cdd:cd06611  244 SCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLLA 279
PRK12704 PRK12704
phosphodiesterase; Provisional
515-627 7.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 7.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973183 515 EQTRKLAILA--EQYDHSINEMLSTQALRLDEAQEAECQVL--KMQLQQELELLNAYQSKIKmqaeaQHDRELRELEQRV 590
Cdd:PRK12704  52 EAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLqkEENLDRKLELLEKREEELE-----KKEKELEQKQQEL 126
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568973183 591 SLRRALLEQKIEEemlalQNERTERIRSLLERQAREI 627
Cdd:PRK12704 127 EKKEEELEELIEE-----QLQELERISGLTAEEAKEI 158
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
13-33 9.51e-03

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. 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. The plant MEKK1 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: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 38.54  E-value: 9.51e-03
                         10        20
                 ....*....|....*....|.
gi 568973183  13 CLQKIPQDRPTSEELLKHMFV 33
Cdd:cd06632  239 CLQRDPEDRPTASQLLEHPFV 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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