|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
1269-1392 |
1.60e-46 |
|
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365.
Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 163.70 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 1269 MDLRWQIHHREKNWNREKVELLERLDNERQEWGRQKEELLWRVEQLQKEKSPRRS------------GSFLCSPREDDNR 1336
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRKinmnerakvidgEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958805813 1337 PYPHQGSLHPSR--PVSMWPCEDTDSIPFEDRPLSKLKESDRCSASENLYLDALSLDD 1392
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
633-725 |
3.70e-42 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 149.76 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 633 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQESGWLGDGVSKGPGAS--APLQEELKSARLQIDE 710
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSreAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1958805813 711 LSGKVLKLQCENRLL 725
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
504-598 |
1.77e-37 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 136.27 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 504 DSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASI 583
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1958805813 584 LGRKIVELEVENRGL 598
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-659 |
2.61e-11 |
|
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: 69.32 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:TIGR02168 689 LEEKIAELEKALAELRKE-LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 422 DvsvRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQ---ALQNELERLRESSLKRRGSREiykekklvnqiTLPRAV 498
Cdd:TIGR02168 768 E---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLE-----------SLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 499 LAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstreAELKLRLKLVE 578
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------------ALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 579 EEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMEsstELRRHLQFVEEEAELLRRSISEI 658
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRL 977
|
.
gi 1958805813 659 E 659
Cdd:TIGR02168 978 E 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-602 |
2.30e-09 |
|
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: 62.77 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 345 ELDELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDVS 424
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 425 VRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGsreiyKEKKLVNQITLPRAVLAWQDD 504
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL-----QIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 505 SADlKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAggppstREAELKLRLKLVEEEASIL 584
Cdd:TIGR02168 415 RRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE------ELEEAEQALDAAERELAQL 487
|
250 260
....*....|....*....|....*
gi 1958805813 585 GRKIVELEV-------ENRGLKAEM 602
Cdd:TIGR02168 488 QARLDSLERlqenlegFSEGVKALL 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-611 |
2.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 343 KDELDELRAEMEEMrDSYLEEDGYQLQELRRELDRANKNcRILQYRLRKAEQ----KSLKVAETG--QVDGEL------- 409
Cdd:TIGR02169 176 LEELEEVEENIERL-DLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGyellKEKEALERQkeAIERQLasleeel 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 410 -------------IRSLEQDLK-VAKDV-------SVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELER 468
Cdd:TIGR02169 254 eklteeiselekrLEEIEQLLEeLNKKIkdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 469 LRESslKRRGSREIYKEKKLVNQITlpRAVLAWQDDSADLKCQLQ-------FAKEEASLMRKKMAKLGREKDELEQELQ 541
Cdd:TIGR02169 334 LLAE--IEELEREIEEERKRRDKLT--EEYAELKEELEDLRAELEevdkefaETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 542 KYKSLYGDVDSPLPTGEAggppstREAELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHER 611
Cdd:TIGR02169 410 RLQEELQRLSEELADLNA------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
337-612 |
1.01e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 337 SENDYLKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILqyrlrkAEQKSLKVAETGQVDGELirsleQD 416
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELRE--------EIEELKEKRDELNEELKEL------AEKRDELNAQVKELREEA-----QE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 417 LKVAKDvsvrlhhEL-ETVEEKRAKAEDDNETLRQHMIEV-EISRQALQNELERLRESSLKRRGSREIY----------K 484
Cdd:COG1340 62 LREKRD-------ELnEKVKELKEERDELNEKLNELREELdELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlspeE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 485 EKKLVNQITLPRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYK----SLYGDVDSplptgeag 560
Cdd:COG1340 135 EKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHeemiELYKEADE-------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 561 gppSTREA--------ELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHERE 612
Cdd:COG1340 207 ---LRKEAdelhkeivEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
340-612 |
1.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 340 DYLKDELDELRAEMEEMRDSY------LEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSL 413
Cdd:COG1196 235 RELEAELEELEAELEELEAELeeleaeLAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 414 EQDLKvakdvsvRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRgsreiykekklvnqit 493
Cdd:COG1196 315 EERLE-------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 494 lpRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLpTGEAGGPPSTREAELKLR 573
Cdd:COG1196 372 --AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL-AELEEEEEEEEEALEEAA 448
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958805813 574 LKLVEEEASILG--RKIVELEVENRGLKAEMEDIRVQHERE 612
Cdd:COG1196 449 EEEAELEEEEEAllELLAELLEEAALLEAALAELLEELAEA 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-665 |
2.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLE--------EDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGqvdgELIRSL 413
Cdd:COG4717 93 LQEELEELEEELEELEAELEElreeleklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE----EELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 414 EQDLKVAK--------DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKE 485
Cdd:COG4717 169 EAELAELQeeleelleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 486 KKLVNQITLPRAVLAWQDDSAD--------LKCQLQFAKEEASLMRKKMAKLGREKDEL----------EQELQKYKSLY 547
Cdd:COG4717 249 RLLLLIAAALLALLGLGGSLLSliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleeleEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 548 GdVDSPLPTGEAGGPPST-----------REAELKLRLKLVEEEASILG-----------RKIVELEVENRGLKAEMEDI 605
Cdd:COG4717 329 G-LPPDLSPEELLELLDRieelqellreaEELEEELQLEELEQEIAALLaeagvedeeelRAALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 606 RVQHEREGTSRDHVPGIPTspFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQL 665
Cdd:COG4717 408 EEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-681 |
2.10e-07 |
|
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: 56.22 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 346 LDELRAEMEEMRDsYLEEDGYQLQELRRELDRANKncrilqYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVAKDVSV 425
Cdd:TIGR02168 181 LERTRENLDRLED-ILNELERQLKSLERQAEKAER------YKELKAELRELELALLVLRLEELREELEE-LQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 426 RLHHELETveeKRAKAEDDNETLRQHMIEVEISRQALQNELERLRE--SSLKRRgsREIYKEKKLVNQITLPRAvlawQD 503
Cdd:TIGR02168 253 EELEELTA---ELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQ--KQILRERLANLERQLEEL----EA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 504 DSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYgdvdsplptgeaggppstreAELKLRLKLVEEEASI 583
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------------------EELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 584 LGRKIVELEVE---NRG----LKAEMEDIRVQHEREGTS-RDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRSI 655
Cdd:TIGR02168 384 LRSKVAQLELQiasLNNeierLEARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
330 340
....*....|....*....|....*.
gi 1958805813 656 SEIEDHNRQLTHELSKFKFEPHQESG 681
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-592 |
2.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLEEDGY-------------QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGE 408
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAElarleqdiarleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 409 LIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEveisRQALQNELERLRESSLKRRGSREIYKEKKL 488
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE----LAAQLEELEEAEEALLERLERLEEELEELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 489 VNQITLPRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGD------VDSPLPTGEAGGP 562
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaaarllLLLEAEADYEGFL 507
|
250 260 270
....*....|....*....|....*....|
gi 1958805813 563 PSTREAELKLRLKLVEEEASILGRKIVELE 592
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
340-585 |
2.96e-07 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 340 DYLKDELDELRAEMEEM--RDSYLEEDGYQLQELRRELDRankncRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 747 SSLEQEIENVKSELKELeaRIEELEEDLHKLEEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 418 KvakdvsvRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLrESSLKRRGSREIYKEKKLVNqitLPRA 497
Cdd:TIGR02169 822 N-------RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGD---LKKE 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 498 VLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYkslygdvDSPLPTGEAGGPPSTREAELKLRLKLV 577
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-------EDPKGEDEEIPEEELSLEDVQAELQRV 963
|
....*...
gi 1958805813 578 EEEASILG 585
Cdd:TIGR02169 964 EEEIRALE 971
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-721 |
3.12e-07 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 435 EEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQITLPRAVLAWQDDSADLKCQLQF 514
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 515 AKEEASLMRKKMAKLGREKDELEQELQ----KYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKlvEEEASILGRKIVE 590
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEelnkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK--ERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 591 LEVENRGLKAEMEDIRVQHEREGTSRDHVpgipTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELs 670
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI- 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958805813 671 kfkfEPHQ-ESGWLGDGVSKGPGASAPLQEELKSARLQIDELSGKVLKLQCE 721
Cdd:TIGR02169 402 ----NELKrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-480 |
7.86e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKncrilqyRLRKAEQKSLKVAetgqvdgELIRSLEQDLKVAK 421
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLE-------ALLAALGLPLPASA 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805813 422 DVSVRLHHEletVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRE--SSLKRRGSR 480
Cdd:COG4913 380 EEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiASLERRKSN 437
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-545 |
9.45e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDsyleedgyqlqELRRELDRANKNCRILQYRLRKAEqKSLKVAETG------QVD--GELIRSL 413
Cdd:pfam05483 546 LRDELESVREEFIQKGD-----------EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKcnnlkkQIEnkNKNIEEL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 414 EQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQAlQNELERLRESSLkrrgSREIYKEKKLVNQ-I 492
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKL----LEEVEKAKAIADEaV 688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958805813 493 TLPRAVlawqddsaDLKCQLQFAkEEASLMRKKMAKLGREKDELEQELQKYKS 545
Cdd:pfam05483 689 KLQKEI--------DKRCQHKIA-EMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
340-671 |
1.03e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 340 DYLKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKsLKVAETGQvdgeliRSLEQDLKV 419
Cdd:COG4372 41 DKLQEELEQLREELEQARE--------ELEQLEEELEQARSELEQLEEELEELNEQ-LQAAQAEL------AQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 420 AKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQITLPRAVL 499
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 500 AWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEE 579
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 580 EASILGR-KIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEI 658
Cdd:COG4372 266 AILVEKDtEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
330
....*....|...
gi 1958805813 659 EDHNRQLTHELSK 671
Cdd:COG4372 346 LLVGLLDNDVLEL 358
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-728 |
1.06e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRD------SYLEEDGYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKvaetGQVDGELIRSL 413
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTqlnqlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN----NQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 414 EQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNEL-ERLRE-SSLKRRgsREIYKE--KKLV 489
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELeEKQNEiEKLKKE--NQSYKQeiKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 490 NQITlpravlawqddsaDLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEaggppsTREAE 569
Cdd:TIGR04523 391 SQIN-------------DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT------NQDSV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 570 LKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVpgipTSPFGDSMESSTELRRHLQFVEEEAE 649
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 650 LLRRSISEIEDHNRQLTHELSKFKFephqesgwlgdgvskgpgasaplqeELKSARL--QIDELSGKVLKLQCENRLLLS 727
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDF-------------------------ELKKENLekEIDEKNKEIEELKQTQKSLKK 582
|
.
gi 1958805813 728 N 728
Cdd:TIGR04523 583 K 583
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
342-619 |
1.84e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSylEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKsLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:TIGR00618 224 LEKELKHLREALQQTQQS--HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 422 DVS------VRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQN---ELERLRESSLKRRGSREIYKEkklvnQI 492
Cdd:TIGR00618 301 AVTqieqqaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSIREISCQ-----QH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 493 TLPRAVLAWQDDSADLKCQLQFAKeeaslmrKKMAKLGREKDELEQELQKYKSLYGDvdspLPTGEAGGPPSTREAELKl 572
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLC-------KELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRYAELC- 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958805813 573 rLKLVEEEASILGRKIVELEVENRGLKAE------MEDIRVQHEREGTSRDHV 619
Cdd:TIGR00618 444 -AAAITCTAQCEKLEKIHLQESAQSLKEReqqlqtKEQIHLQETRKKAVVLAR 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
344-630 |
2.85e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 344 DELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDv 423
Cdd:COG4942 20 DAAAEAEAELEQLQQ--------EIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 424 svrlhhELETVEEKRAKAEDDNETLRQHMIEV--EISRQALQNELERLressLKRRGSREIYKEKKLVNQITLPRAVLA- 500
Cdd:COG4942 84 ------ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 501 -WQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeaggppstrEAELKLRLKLVEE 579
Cdd:COG4942 154 eLRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL--------------------LARLEKELAELAA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805813 580 EASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDH------VPGIPTSPFGDS 630
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKgklpwpVSGRVVRRFGER 270
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-544 |
6.90e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 350 RAEMEEMRDSYLEEDGYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHH 429
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 430 ELETVEEKRAKAEDdnetLRQHMIEVEISRQALQNELERLRES-SLKRRGSREIYKEKKL--VNQITLPRAVLAWQDDSA 506
Cdd:PTZ00121 1666 EAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEE 1741
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958805813 507 DLKCQLQFAKEEASlmRKKMAKLGREKDELEQELQKYK 544
Cdd:PTZ00121 1742 DKKKAEEAKKDEEE--KKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-612 |
1.09e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRILQYRLR---------KAEQKSL--KVAETGQVDG--- 407
Cdd:PRK03918 219 LREELEKLEKEVKE-----LEELKEEIEELEKELESLEGSKRKLEEKIReleerieelKKEIEELeeKVKELKELKEkae 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 408 ---ELIRSLEQDLKVAKDVSVRL---HHELETVEEKRAKAEDDNETLRqhmiEVEISRQALQNELERLRESSLKRRGSRE 481
Cdd:PRK03918 294 eyiKLSEFYEEYLDELREIEKRLsrlEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 482 IYKEKklvNQITLPRAVLAWQDDSADLKcQLQFAKEEaslMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGG 561
Cdd:PRK03918 370 KKEEL---ERLKKRLTGLTPEKLEKELE-ELEKAKEE---IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958805813 562 PPSTREAELKLRLKLVEEEASILGRKIvELEVENRGLKAEMEDIRVQHERE 612
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKE 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-477 |
1.24e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDG---ElIRSLEQDLK 418
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqkE-IESLKRRIS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958805813 419 VAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRR 477
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
337-608 |
1.58e-05 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 337 SENDYLKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQD 416
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASR--------KIGEIEKEIEQLEQEEEKLKERLEELEED--------------LSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 417 LKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEIsrQALQNELERLREsSLKRRGSREIYKEKKLvNQITLPR 496
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEE-EVSRIEARLREIEQKL-NRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 497 AVLawQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLRLKL 576
Cdd:TIGR02169 829 EYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA--------------------ALRDLESRLGD 886
|
250 260 270
....*....|....*....|....*....|..
gi 1958805813 577 VEEEASILGRKIVELEVENRGLKAEMEDIRVQ 608
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
330-1111 |
2.27e-05 |
|
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: 49.58 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 330 REMEELRSENDYLKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRankncRILQYRLRKAEQKSLKvaetgqVDGEL 409
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE-----YLLYLDYLKLNEERID------LLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 410 IRSLEQDLKVAKDVSvrlhhELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLV 489
Cdd:pfam02463 246 LRDEQEEIESSKQEI-----EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 490 NQITLPRAVLawqddSADLKCQLQFAKEEASLMRKKmAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppSTREAE 569
Cdd:pfam02463 321 KEKKKAEKEL-----KKEKEEIEELEKELKELEIKR-EAEEEEEEELEKLQEKLEQLEEELLAKK---------KLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 570 LKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDhvpgiptspfgDSMESSTELRRHLQFVEEEAE 649
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE-----------EEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 650 LLRRSISEIEDHNRQLTHELSKFKFEPHQESGWLGDGVSKGPGASAPLQEELKS-ARLQIDELSGKVLKLQCENRLLLSN 728
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 729 AQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEEGRlPQPKREGPVGGESDSEDMFEKTSGFGSGKPSEASEPCPTELL 808
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 809 RVRED--TECLVTMKLEAQRLERTVERLISDTDGFIRDSGLrgngsaspgvqgegEGSLNEPHLLETINGRMKAFRKELQ 886
Cdd:pfam02463 614 EADEDdkRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL--------------EEGLAEKSEVKASLSELTKELLEIQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 887 AFLEQMSRIVDGLSPLSHLTESSSFLSTVTSVSRDspigtLGKELGPDLQSKLREQLEWQLGQDRGDEREGLRLRATREL 966
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKK-----LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 967 HRHadgdSGSHGLGGQSCFNLELRgspVLPEQSVSVEELQGQLQQAARLHQEETETYTNKIRKMEEDHLYALRWKELEMH 1046
Cdd:pfam02463 755 SRL----KKEEKEEEKSELSLKEK---ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE 827
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958805813 1047 SLALQNTLHKRTWSDEKNMLQQELRSLKQNIFLFYVKLRWLLKHWRQGKQMEEGGEDFAESEHPE 1111
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-476 |
2.35e-05 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 338 ENDYLKDELDELRAEMEEMRdSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLR-AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805813 418 KVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERL--RESSLKR 476
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVekELSKLQR 490
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
7-290 |
2.70e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 7 PAGGGAPDPKPqPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKdLHTRPATATPSAGRAPTPAAPRSPSLTGKAPPSPG 86
Cdd:PHA03307 152 PPAAGASPAAV-ASDAASSRQAALPLSSPEETARAPSSPPAEPP-PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 87 SPAAPGRLSRRSGVVPGAKD-------KPPPGAGARSAGGAKAAPGTRRATRAGPAEPlsrVGRPAGAEPPPALSKGRKA 159
Cdd:PHA03307 230 DDAGASSSDSSSSESSGCGWgpenecpLPRPAPITLPTRIWEASGWNGPSSRPGPASS---SSSPRERSPSPSPSSPGSG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 160 KRGPGTPPARavvppapaarvpavtlSVTSVAGTRISHTDSSSDLSDCASEPLSDEQRLLPAASSDAESGTGSSDREPLR 239
Cdd:PHA03307 307 PAPSSPRASS----------------SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPR 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958805813 240 GAPTPSSGSRGPPPGSPEPPTLLAA----------------PPVAGACLGGRSS------PGGTPSGSPGPGS 290
Cdd:PHA03307 371 PSRAPSSPAASAGRPTRRRARAAVAgrarrrdatgrfpagrPRPSPLDAGAASGafyaryPLLTPSGEPWPGS 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
367-562 |
4.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 367 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAkdvsvRLHHELETVEEKRAKAEDDN- 445
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 446 --ETLRQHMIEVEISRQALQNELERLR------ESSLKRRgSREIYKEKKLVNQItlPRAVLAWQDDSADLKCQLQFAKE 517
Cdd:COG4913 686 dlAALEEQLEELEAELEELEEELDELKgeigrlEKELEQA-EEELDELQDRLEAA--EDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958805813 518 EASLMRKKM--------AKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGP 562
Cdd:COG4913 763 VERELRENLeeridalrARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
13-317 |
4.92e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 13 PDPKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKDLHTRPATAtpsAGRAPTPAAPRSPSLtgkappsPGSPAAPG 92
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA---AQASSPPQRPRRRAA-------RPTVGSLT 2696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 93 RLSRrsgvvPGAKDKPPPGAGARSAGGAKAAPGTRRATRAGPAEPLSRVGRPAGAEPPPALSKGRKAKRgPGTPPARAVV 172
Cdd:PHA03247 2697 SLAD-----PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-PTTAGPPAPA 2770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 173 PPAPAARVPAVTLSVTSVAgtrishtdsssdlsdcasePLSDEQRLLPAASSDAESGTGSSDREP-LRGAPTPSSGSRGP 251
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVA-------------------SLSESRESLPSPWDPADPPAAVLAPAAaLPPAASPAGPLPPP 2831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958805813 252 PPGSPEPPTLLAAPPVAGACLGGRSSPGGTPS--GSPGPGSQEDVGGRAPPERTILGTPKEPSLGEQP 317
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
31-312 |
5.67e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.24 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 31 PLAERRRLHRAPSPARPFLKDLHTRPATATPSAGRAPTPAAPRSPSLTGKAPPSPGSPAAPGRLSRRSGVVPGAKDKPPP 110
Cdd:PHA03307 77 TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 111 gagarsagGAKAAPGTRRATRAGPAEPLSRVGRPAGAEPPPALSKGRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSV 190
Cdd:PHA03307 157 --------ASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 191 AGTRISHTDSS--SDLSDCASEPLSDEQRLLPA-----ASSDAESGTGSSDREPLRGAPTPSSGSRGPPPGSPEPPTLLA 263
Cdd:PHA03307 229 ADDAGASSSDSssSESSGCGWGPENECPLPRPApitlpTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958805813 264 APPVAGACLGGRSSPGGTPSGSPGPGSQEDVGGRAPPERTILGTPKEPS 312
Cdd:PHA03307 309 PSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPP 357
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
367-542 |
5.80e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 367 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAE 442
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 443 DDNETLRQHMI-EVEISRQALQN---ELE-RLRE--SSLKRR---GSREIYKEKKLVNQITlPRAVLAWQDDSADLKCQL 512
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRlneARREQAKAVVSLRQIQ-HRATQEKERNQELRRLQD 637
|
170 180 190
....*....|....*....|....*....|
gi 1958805813 513 QFAKEEASLMRKKMAKLGREKDELEQELQK 542
Cdd:pfam07111 638 EARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-609 |
6.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 350 RAEME-EMRDSYLEedgyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQvdgELIRSLeQDLKVAKDvsvRLH 428
Cdd:pfam15921 592 KAQLEkEINDRRLE-----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS---ERLRAV-KDIKQERD---QLL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 429 HELETVEEKRAKAEDDNETLRQHMI----EVEISRQAL-------QNELERLRESSLKRRGS--REIYKEKKLVNQITLP 495
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYEVLKRNFRnkseEMETTTNKLkmqlksaQSELEQTRNTLKSMEGSdgHAMKVAMGMQKQITAK 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 496 RAvlawQDDSadLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeAGGPPSTREAELKLRLK 575
Cdd:pfam15921 740 RG----QIDA--LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM--------AGELEVLRSQERRLKEK 805
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958805813 576 LVEEEASILGRKIVELEVENRGLKAEMEDIR--VQH 609
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRQEQESVRlkLQH 841
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
342-611 |
7.42e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRdsyleedgYQLQELRRELDRANKNCRILQYRLRKAEQkslkvaetgqvdgeLIRSLEQDLKVAK 421
Cdd:pfam05557 109 LKNELSELRRQIQRAE--------LELQSTNSELEELQERLDLLKAKASEAEQ--------------LRQNLEKQQSSLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 422 DVSVRlhheLETVEEKRAKAEDDNETLRQHMIEVEiSRQALQNELERLRESSLKRR---GSREIYKEKKlvnqitlprav 498
Cdd:pfam05557 167 EAEQR----IKELEFEIQSQEQDSEIVKNSKSELA-RIPELEKELERLREHNKHLNeniENKLLLKEEV----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 499 lawqddsADLKCQLQfaKEEAslMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPP----STREAELKLRL 574
Cdd:pfam05557 231 -------EDLKRKLE--REEK--YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlQQREIVLKEEN 299
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958805813 575 KLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHER 611
Cdd:pfam05557 300 SSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-547 |
1.22e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 341 YLKDELDELRAEMEEMRDsYLEEdgyQLQELRRELDRANKncRILQYRlrkAEQKSLKVAETGQVDGELIRSLEQDLKVA 420
Cdd:COG3206 161 YLEQNLELRREEARKALE-FLEE---QLPELRKELEEAEA--ALEEFR---QKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 421 KDVSVRLHHELETVEEKRAKAEDDNETLRQHmieveisrQALQNELERLRESSLKRRGSREIYKE-----KKLVNQIT-- 493
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS--------PVIQQLRAQLAELEAELAELSARYTPnhpdvIALRAQIAal 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958805813 494 -------LPRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLG---REKDELEQELQKYKSLY 547
Cdd:COG3206 304 raqlqqeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPeleAELRRLEREVEVARELY 367
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
342-667 |
2.54e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRD-----SYLEEdgyQLQELRRELDRANK---NCRILQYRLRKAEQKSLKVAETGQVDGELIRSL 413
Cdd:pfam05557 202 LEKELERLREHNKHLNEnienkLLLKE---EVEDLKRKLEREEKyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 414 EQdlkvakdvsvrLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNEL------------ERLRESSLKRRgsre 481
Cdd:pfam05557 279 ED-----------LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELaqylkkiedlnkKLKRHKALVRR---- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 482 IYKEKKLVNQ-ITLPRAVLAWQDDsadlkcqlQFAKEEASlmrkkmAKLGREKDELEQELQKYKSLYGDVDSPLPTGE-- 558
Cdd:pfam05557 344 LQRRVLLLTKeRDGYRAILESYDK--------ELTMSNYS------PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEee 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 559 AGG---PPSTREAELKLRLK--------LVEEEASILGRKIVELEVENRGL---KAEMEDIRVQHEREGT---SRDHVPG 621
Cdd:pfam05557 410 LGGykqQAQTLERELQALRQqesladpsYSKEEVDSLRRKLETLELERQRLreqKNELEMELERRCLQGDydpKKTKVLH 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958805813 622 IPTSPFGDSMESSTELRRHLQfveEEAELLRRSISEIEDHNRQLTH 667
Cdd:pfam05557 490 LSMNPAAEAYQQRKNQLEKLQ---AEIERLKRLLKKLEDDLEQVLR 532
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
5-318 |
3.06e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.93 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 5 NGPAGGG-----APDPKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPflkdlhtrPATATPSAGRAPTPAAPRSPSLtg 79
Cdd:PHA03307 69 TGPPPGPgteapANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP--------PPPTPPPASPPPSPAPDLSEML-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 80 kappspGSPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAAPGTRRATRAGP---AEPLSRVGRPAGAEPPPALSK- 155
Cdd:PHA03307 139 ------RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSsppAEPPPSTPPAAASPRPPRRSSp 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 156 ------------GRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSVAGTRISHTDSSSdlsdcASEPLSDEQRLLPAAS 223
Cdd:PHA03307 213 isasasspapapGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWE-----ASGWNGPSSRPGPASS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 224 SDAESGTG-----SSDREPLRGAPTPSSGSRGPPPGSPEPPTLLAAPPVAGAclGGRSSPGGTPSGSPGPGSQEDVGG-- 296
Cdd:PHA03307 288 SSSPRERSpspspSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGA--AVSPGPSPSRSPSPSRPPPPADPSsp 365
|
330 340
....*....|....*....|...
gi 1958805813 297 -RAPPERTILGTPKEPSLGEQPR 318
Cdd:PHA03307 366 rKRPRPSRAPSSPAASAGRPTRR 388
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
342-554 |
3.75e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.25 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLEED-------------GYQLQELRRELDRANKNCRILQYRLRKAEQKS------LKVAE- 401
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEkraekaeaevaalNRRIQLLEEELERTEERLAEALEKLEEAEKAAdesergRKVLEn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 402 TGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELeRLRESSLKrrgSRE 481
Cdd:pfam00261 86 RALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEEL-KVVGNNLK---SLE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958805813 482 IYKEKKLVNQITlpravlaWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPL 554
Cdd:pfam00261 162 ASEEKASEREDK-------YEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
343-669 |
4.11e-04 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 45.49 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 343 KDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKD 422
Cdd:COG2770 264 KDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 423 VSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQITLPRAVLAWQ 502
Cdd:COG2770 344 LLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 503 DDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEAS 582
Cdd:COG2770 424 LAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 583 ILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHN 662
Cdd:COG2770 504 ELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELA 583
|
....*..
gi 1958805813 663 RQLTHEL 669
Cdd:COG2770 584 ALLLLLL 590
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
6-308 |
6.11e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 6 GPAGGGAPDPKPQPAGQHHRHHHLHP-LAERRRLHRAPSPAR----PFLKDLHTRPATATPSAGRA------PTPAAPRS 74
Cdd:PHA03307 107 TPPGPSSPDPPPPTPPPASPPPSPAPdLSEMLRPVGSPGPPPaaspPAAGASPAAVASDAASSRQAalplssPEETARAP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 75 PSLTGKAPPSPGSPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAAP----------------GTRRATRAGPAEPL 138
Cdd:PHA03307 187 SSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSsdssssessgcgwgpeNECPLPRPAPITLP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 139 SRVGRPAGAEPPPALSKGRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSVAGTRISHTDSSSDLSDcaseplSDEQRL 218
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE------SSRGAA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 219 LPAASSDAESGTGSSDREPLRGAPTPSSGSRGPPPGSPEPPTLLAAPPVAGACLGG----RSSPGGTPSGSPGP-GSQED 293
Cdd:PHA03307 341 VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGrarrRDATGRFPAGRPRPsPLDAG 420
|
330
....*....|....*
gi 1958805813 294 VGGRAPPERTILGTP 308
Cdd:PHA03307 421 AASGAFYARYPLLTP 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
494-769 |
6.23e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 494 LPRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLR 573
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------------ARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 574 LKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTELRRHLQFVEEEAELLRR 653
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 654 SISEIEDHNRQLTHELSKfkfephqesgwLGDGVSKGPGASAPLQEELKSARLQIDELSGKVLKLQCENRLLLSNAQRCD 733
Cdd:COG4942 158 DLAELAALRAELEAERAE-----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958805813 734 --LAAHLGLRAPSPRDSDAESDAGKKesdgeeGRLPQP 769
Cdd:COG4942 227 alIARLEAEAAAAAERTPAAGFAALK------GKLPWP 258
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
338-492 |
6.49e-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: 44.73 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 338 ENDYLKDELDELRAE--MEEMRDSYLEEDGYQLQELRRELDRANKN--CRILQYRLRKAEQKSLKVAETgQVDGELIRSL 413
Cdd:pfam17380 390 KNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQRevRRLEEERAREMERVRLEEQER-QQQVERLRQQ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 414 EQDLKVAKDVSVRLHHELETVEEKRAKA-EDDNETLRQHMIEVEISRQALQNELE----------RLRESSLKRRGSREI 482
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEerqkaiyeeeRRREAEEERRKQQEM 548
|
170
....*....|
gi 1958805813 483 YKEKKLVNQI 492
Cdd:pfam17380 549 EERRRIQEQM 558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
343-714 |
6.87e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 343 KDELDELR---AEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLkv 419
Cdd:TIGR00606 244 ENELDPLKnrlKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL-- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 420 akdvsVRLHHELETVEEKRakaeddnETLRQHMIEVEISRQALQNELERLRESSLKRRG--------------SREIYKE 485
Cdd:TIGR00606 322 -----VDCQRELEKLNKER-------RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSliqslatrleldgfERGPFSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 486 KKLVNQITLPR------AVLAWQDdSADLKCQLQFAKEEASLMRKKMAKLGR------EKDELEQELQKYKSLYG----- 548
Cdd:TIGR00606 390 RQIKNFHTLVIerqedeAKTAAQL-CADLQSKERLKQEQADEIRDEKKGLGRtielkkEILEKKQEELKFVIKELqqleg 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 549 ------DVDSPLPTGEAGGPPSTREAE---LKLRLKLVEEEASILGRKIVELEVENRGLKAEME---------------- 603
Cdd:TIGR00606 469 ssdrilELDQELRKAERELSKAEKNSLtetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTtrtqmemltkdkmdkd 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 604 ----DIRVQHEREGTSRdhVPGIPTSP-FGDSMESsteLRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQ 678
Cdd:TIGR00606 549 eqirKIKSRHSDELTSL--LGYFPNKKqLEDWLHS---KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958805813 679 ESGWLGDGVSKGPGAS--APLQEELKSARLQIDELSGK 714
Cdd:TIGR00606 624 YEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGA 661
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1-318 |
7.17e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 1 METLNGPAGGGAPDPKPqPAGQHHRHHHLHPLAERrrlhrAPSPARPFLKDLHTRP-ATATPSAGRAP-----TPAAPRS 74
Cdd:PHA03247 2540 LEELASDDAGDPPPPLP-PAAPPAAPDRSVPPPRP-----APRPSEPAVTSRARRPdAPPQSARPRAPvddrgDPRGPAP 2613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 75 PSLTGKAPPSPGSPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAAPgTRRATR----AGPAEPLSRVGRPAG---- 146
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR-PRRARRlgraAQASSPPQRPRRRAArptv 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 147 ------AEPPP----------ALSKGRKAKRGPGTPPARAVVPPAPAARVPAVTLSVTSVAGTRISH--TDSSSDLSDCA 208
Cdd:PHA03247 2693 gsltslADPPPppptpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPAPAPP 2772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 209 SEPLSDEQRLL--PAASSDAESGTGSSDREPLRGAPTPSSGSRGPPPGSPEPPTLLAAP----PVAGACLGGRSSPGGTP 282
Cdd:PHA03247 2773 AAPAAGPPRRLtrPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPtsaqPTAPPPPPGPPPPSLPL 2852
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958805813 283 SGSPGPGSqeDVGGRAPPERtilgTPKEPSLGEQPR 318
Cdd:PHA03247 2853 GGSVAPGG--DVRRRPPSRS----PAAKPAAPARPP 2882
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1167-1323 |
9.30e-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: 44.28 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 1167 GPLSKQVVENQQLFRALKALLEDFRSELREDEHARLRLQQQYASdkaawdvewavLKCRLEQLEEKTEKSLGELDSSAEG 1246
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-----------LEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 1247 KGALKKEREVHQKLLADSHGLVMDLRWQIHHREKNWNREKVEL------LERLDNERQEWGRQKEELLWRVEQLQKEKSP 1320
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
...
gi 1958805813 1321 RRS 1323
Cdd:TIGR02168 426 LLK 428
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
430-714 |
1.04e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 430 ELETVEEKRAKAEDDNEtlrqhMIEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQITLPRAVLAWQDDSADLK 509
Cdd:pfam07888 5 ELVTLEEESHGEEGGTD-----MLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 510 CQLQFAKEEaslmrkkmakLGREKDELEQELQKYKSLygdVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIV 589
Cdd:pfam07888 80 SRVAELKEE----------LRQSREKHEELEEKYKEL---SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 590 ELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFGDSMESSTE---LRRHLQFVEEEAELLRRSISEIED-----H 661
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEfqeLRNSLAQRDTQVLQLQDTITTLTQklttaH 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805813 662 NRQLTHELSKFKFEPHQE--------SGWLGDGVSKGPGASAPLQEELKSARLQIDELSGK 714
Cdd:pfam07888 227 RKEAENEALLEELRSLQErlnaserkVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
351-722 |
1.11e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 351 AEMEEMRDSYLEEDGYQLQE------LRRELDRANKNCRILQ--------YRLRKAEQKSL-------------KVAETG 403
Cdd:COG5022 734 AALEDMRDAKLDNIATRIQRairgryLRRRYLQALKRIKKIQviqhgfrlRRLVDYELKWRlfiklqpllsllgSRKEYR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 404 QVDgELIRSLEQDLKVAKDVSVRLHHELETVEE-------------KRAKAEDDNETLRQHMIEVEISRQALQNE-LERL 469
Cdd:COG5022 814 SYL-ACIIKLQKTIKREKKLRETEEVEFSLKAEvliqkfgrslkakKRFSLLKKETIYLQSAQRVELAERQLQELkIDVK 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 470 RESSLKRRGSREIYKEKKLVNQItlpravlawqddSADLKCQLQFaKEEASLMRKKMAKLGREKDELEQELQKYKSLygd 549
Cdd:COG5022 893 SISSLKLVNLELESEIIELKKSL------------SSDLIENLEF-KTELIARLKKLLNNIDLEEGPSIEYVKLPEL--- 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 550 vdsplptgeaggppstreaelklrLKLVEEEASiLGRKIVELEVENrglkaEMEDIrvqHEREG-TSRDHVPGIPTSPFG 628
Cdd:COG5022 957 ------------------------NKLHEVESK-LKETSEEYEDLL-----KKSTI---LVREGnKANSELKNFKKELAE 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 629 DSMEsstelRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK-FEPHQESgwlgdgVSKGPGASAPLQEELKSARLQ 707
Cdd:COG5022 1004 LSKQ-----YGALQESTKQLKELPVEVAELQSASKIISSESTELSiLKPLQKL------KGLLLLENNQLQARYKALKLR 1072
|
410
....*....|....*
gi 1958805813 708 IDelSGKVLKLQCEN 722
Cdd:COG5022 1073 RE--NSLLDDKQLYQ 1085
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-715 |
1.44e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRAnkncriLQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:COG1196 447 AAEEEAELEEEEEALLEL-LAELLEEAALLEAALAEL------LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 422 DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQAL-------QNELERLRESSLKRRGSREIYKEKKLVNQITL 494
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 495 PRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGgppstREAELKLRL 574
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG-----SRRELLAAL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 575 KLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDhvpgiptspfgdsmesstELRRHLQFVEEEAELLRRS 654
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL------------------EEELEEEALEEQLEAEREE 736
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805813 655 ISEIEDHNRQLTHELSKFKFEPhqesgwlgdgvskgPGASAPLQEELKSARLQIDELsGKV 715
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPE--------------PPDLEELERELERLEREIEAL-GPV 782
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
342-470 |
1.70e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYL--EEDGYQLQELRRELDRANKNCRILQYRLRKAEQ-------------KSLKVAETGQVD 406
Cdd:pfam06160 303 AEEQNKELKEELERVQQSYTlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayselqeeleeilEQLEEIEEEQEE 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 407 G-ELIRSLEQDLKVAKDVSVRLHHELETVeeKRaKAEDDN-----ETLRQHMIEVEISRQALQNELERLR 470
Cdd:pfam06160 383 FkESLQSLRKDELEAREKLDEFKLELREI--KR-LVEKSNlpglpESYLDYFFDVSDEIEDLADELNEVP 449
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
342-660 |
1.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMR-------------DSYLEEDgyqlQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGE 408
Cdd:PRK02224 211 LESELAELDEEIERYEeqreqaretrdeaDEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 409 LIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSLKRRGSREIYKEKkl 488
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 489 vnqitlpravlawqddSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPT-----GEAGGPP 563
Cdd:PRK02224 365 ----------------AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElreerDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 564 STREAELKLRLKLVEEEASIL-------------GRKIVELEVENRG----LKAEMEDIRVQHERegTSRDHvpgiptsp 626
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLeagkcpecgqpveGSPHVETIEEDRErveeLEAELEDLEEEVEE--VEERL-------- 498
|
330 340 350
....*....|....*....|....*....|....
gi 1958805813 627 fgDSMESSTELRRHLQFVEEEAELLRRSISEIED 660
Cdd:PRK02224 499 --ERAEDLVEAEDRIERLEERREDLEELIAERRE 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-501 |
2.58e-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: 42.74 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:TIGR02168 356 LEAELEELEAELEELESR-LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 422 dvSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELeRLRESSLKRRGSREIYKEKKLVNQITLPRAVLAW 501
Cdd:TIGR02168 435 --LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-673 |
2.92e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 332 MEELRSENDYLKDELDELRAEMEEMRD--SYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSlKVAETGQVDGEL 409
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK-ELKEIEEKERKL 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 410 IRSLEQDLKVAKDVSvRLHHELETVEEKRAKaeddNETLRQHMIEvEISRQAlqNELERLRESSLKRRG-----SREIYK 484
Cdd:PRK03918 479 RKELRELEKVLKKES-ELIKLKELAEQLKEL----EEKLKKYNLE-ELEKKA--EEYEKLKEKLIKLKGeikslKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 485 EKKLVNQitlpravlawqddSADLKCQLQFAKEEASLMRKKMAKLGREK-DELEQELQKYKSLYGDVDsplptgEAGGPP 563
Cdd:PRK03918 551 LEELKKK-------------LAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYL------ELKDAE 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 564 STREAELKlRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREgtsrdhvpgiptsPFGDSMESSTELRRHLQF 643
Cdd:PRK03918 612 KELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-------------EYEELREEYLELSRELAG 677
|
330 340 350
....*....|....*....|....*....|
gi 1958805813 644 VEEEAELLRRSISEIEDHNRQLTHELSKFK 673
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
342-673 |
3.66e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 42.14 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMrdsylEEDGYQLQELrrELDRankncRILQYrlrkaeQKSLKVAEtgqvdgELIRSLeqDLKVAK 421
Cdd:COG4477 227 LPDQLEELKSGYREM-----KEQGYVLEHL--NIEK-----EIEQL------EEQLKEAL------ELLEEL--DLDEAE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 422 DVSVRLHHELET---VEEKRAKA----EDDNETLRQHMIEVEISRQALQNELERLRES--------SLKRRGSREIYKEK 486
Cdd:COG4477 281 EELEEIEEEIDElydLLEKEVEAkkyvDKNQEELEEYLEHLKEQNRELKEEIDRVQQSyrlnenelEKVRNLEKQIEELE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 487 KLVNQITlpravlawqddsadlkcqLQFAKEEA--SLMRKKMAKLGREKDELEQELQKY----KSLygdvdsplptgeag 560
Cdd:COG4477 361 KRYDEID------------------ERIEEEKVaySELQEELEEIEEQLEEIEEEQEEFseklKSL-------------- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 561 gppstREAELKLRLKLVEeeasilgrkivelevenrgLKAEMEDIRVQHEREgtsrdHVPGIPTSpFGDSMESSTElrrH 640
Cdd:COG4477 409 -----RKDELEAREKLDE-------------------LKKKLREIKRRLEKS-----NLPGLPEE-YLEMFEEASD---E 455
|
330 340 350
....*....|....*....|....*....|...
gi 1958805813 641 LQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 673
Cdd:COG4477 456 IEELSEELNEVPLNMDEVNRLLEEAEEDIETLE 488
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
348-704 |
4.38e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 348 ELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKaeqkslKVAETgQVDGELIRSLEQDLKVAKDVSVRL 427
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRG-QVAELQEQVTSQSQEQAILQRALQD------KAAEV-EVERMSAKGLQMELSRAQEARRRQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 428 HHELETVEEKrakaeddnetLRQHMIEVEISRQALQNELERLRES-----SLKRRGSREIYKEKKLVNQITLPRAVLAWQ 502
Cdd:pfam07111 393 QQQTASAEEQ----------LKFVVNAMSSTQIWLETTMTRVEQAvaripSLSNRLSYAVRKVHTIKGLMARKVALAQLR 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 503 DDS-----------ADLKCQLQFAKEE-----------ASLMRKKMAKlGREKDE------------LEQELQKYKSLYG 548
Cdd:pfam07111 463 QEScpppppappvdADLSLELEQLREErnrldaelqlsAHLIQQEVGR-AREQGEaerqqlsevaqqLEQELQRAQESLA 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 549 DVDSPLPTGEAGGPPSTREAElKLRLKLVEEE---ASILGRKIVELEVENR----GLKAEMEDIRVQHEREGTSRDHVPG 621
Cdd:pfam07111 542 SVGQQLEVARQGQQESTEEAA-SLRQELTQQQeiyGQALQEKVAEVETRLReqlsDTKRRLNEARREQAKAVVSLRQIQH 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 622 IPTSpfgdSMESSTELRR-HLQFVEEEAELLRRSISEIE-DHN---RQLTHELSKFKFEPHQESGWLGDGVSKGPGASAP 696
Cdd:pfam07111 621 RATQ----EKERNQELRRlQDEARKEEGQRLARRVQELErDKNlmlATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSP 696
|
....*...
gi 1958805813 697 LQEELKSA 704
Cdd:pfam07111 697 RPECSASA 704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1169-1315 |
4.58e-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: 41.97 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 1169 LSKQVVENQQLFRALKALLEDFRSELRE--DEHARLRL--------QQQYASDKAAWDVEWAVLKCRLEQLEEKTEKSLG 1238
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDElrAELTLLNEeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 1239 ELDSSAEGKGALKKEREVHQKLLADSHGLVMDLRWQIH---HREKNWNREKVEL---LERLDNERQEWGRQKEELLWRVE 1312
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEelsEELRELESKRSELrreLEELREKLAQLELRLEGLEVRID 939
|
...
gi 1958805813 1313 QLQ 1315
Cdd:TIGR02168 940 NLQ 942
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
435-668 |
4.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 435 EEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRE-----SSLKRRGSREI---YKEKKLVNQITLPRAVLAWQDDSA 506
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 507 DLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTReAELKLRL------KLVEEE 580
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-ALLEERFaaalgdAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 581 ASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSrdhvpgiPTSPFGDSMESSTELRRHLQFVEEE---------AELL 651
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNREWPA-------ETADLDADLESLPEYLALLDRLEEDglpeyeerfKELL 840
|
250
....*....|....*...
gi 1958805813 652 RR-SISEIEDHNRQLTHE 668
Cdd:COG4913 841 NEnSIEFVADLLSKLRRA 858
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
460-657 |
4.75e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 460 QALQNELERLResslKRRGsreiykekklvnqiTLPRAVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQE 539
Cdd:COG1579 13 QELDSELDRLE----HRLK--------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 540 LQKYKSLYGDVDSPlptgeaggppstREAE--------LKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHER 611
Cdd:COG1579 75 IKKYEEQLGNVRNN------------KEYEalqkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958805813 612 EGTSRDhvpgiptspfgdsmESSTELRRHLQFVEEEAELLRRSISE 657
Cdd:COG1579 143 KKAELD--------------EELAELEAELEELEAEREELAAKIPP 174
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-508 |
5.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 340 DYLKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQkslkvaETGQVDGELIRsLEQDLKV 419
Cdd:COG4913 664 ASAEREIAELEAELER-----LDASSDDLAALEEQLEELEAELEELEEELDELKG------EIGRLEKELEQ-AEEELDE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 420 AKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVeisRQALQNELERLREsslkrrgsREIYKEKKLVNQITlpRAVL 499
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRA--------RLNRAEEELERAMR--AFNR 798
|
....*....
gi 1958805813 500 AWQDDSADL 508
Cdd:COG4913 799 EWPAETADL 807
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
330-665 |
6.63e-03 |
|
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: 41.26 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 330 REMEELRSendyLKDELDELRAEMEEMRDSYLEEDGYQLqELRRELDRankncriLQYRLRKAEQKSLKVAETGqVDGEL 409
Cdd:pfam17380 310 REVERRRK----LEEAEKARQAEMDRQAAIYAEQERMAM-ERERELER-------IRQEERKRELERIRQEEIA-MEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 410 IRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISR----QALQNELERLREsslKRRGSREIYKE 485
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRaeqeEARQREVRRLEE---ERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 486 KKLVNQITLPRavlawqddsadlkcqlqFAKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeaggppst 565
Cdd:pfam17380 454 EEQERQQQVER-----------------LRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL------------------- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 566 rEAELKLR-LKLVEEEASilgRKIVELEVENRGLKAEMEDIRVQHEREgtSRDHVPGIPTSPFGDSMESSTELRRHLQFV 644
Cdd:pfam17380 498 -EKELEERkQAMIEEERK---RKLLEKEMEERQKAIYEEERRREAEEE--RRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
330 340
....*....|....*....|.
gi 1958805813 645 EEEAELLRRsISEIEDHNRQL 665
Cdd:pfam17380 572 EREREMMRQ-IVESEKARAEY 591
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-659 |
6.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 390 RKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERL 469
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 470 RESslkrrgsreiykekklvnqitlpraVLAWQDDSADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKSLYGD 549
Cdd:COG4372 86 NEQ-------------------------LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 550 VDSPLptgeaggppSTREAELK-LRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRDHVPGIPTSPFG 628
Cdd:COG4372 141 LQSEI---------AEREEELKeLEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
250 260 270
....*....|....*....|....*....|.
gi 1958805813 629 DSMESSTELRRHLQFVEEEAELLRRSISEIE 659
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
345-610 |
7.13e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 345 ELDELRAEMEEMRDSYleedgyqlQELRRELDRANKNCRILQYRLRKA--EQKSLKVAETGQVDGELiRSLEQDLKVAKD 422
Cdd:pfam12128 633 ELEKASREETFARTAL--------KNARLDLRRLFDEKQSEKDKKNKAlaERKDSANERLNSLEAQL-KQLDKKHQAWLE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 423 VSVRLHHELET--------VEEKRAKAEDdneTLRQHMIEVEISRQALQNELERLRESSLKRRGSREIyKEKKLVNQI-T 493
Cdd:pfam12128 704 EQKEQKREARTekqaywqvVEGALDAQLA---LLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD-VIAKLKREIrT 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 494 LPRAVLAWQDDSADLKCQLQFAKEEASLMRKKMA----KLGREKDELEQELQKykslygdvdsplptgeaggppstREAE 569
Cdd:pfam12128 780 LERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAtqlsNIERAISELQQQLAR-----------------------LIAD 836
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958805813 570 LKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHE 610
Cdd:pfam12128 837 TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
440-601 |
7.74e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 440 KAEDDNETLRQHMIEVEISRQALQNELERL--RESSLKRRGSREIYKEKKLVNQIT---------LPRAVLA----WQDD 504
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSELVKARQALAQTiaRQKQLERRLEQQTEQAKKLEEKAQaaltkgneeLAREALAekksLEKQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 505 SADLKCQLQFAKEEASLMRKKMAKLGREKDELEQELQKYKS------LYGDVDSPLPTGEAGGPPS------TREAELKL 572
Cdd:pfam04012 99 AEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKArlkaakAQEAVQTSLGSLSTSSATDsferieEKIEEREA 178
|
170 180
....*....|....*....|....*....
gi 1958805813 573 RLKLVEEEASILGRkivELEVENRGLKAE 601
Cdd:pfam04012 179 RADAAAELASAVDL---DAKLEQAGIQME 204
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
340-545 |
7.94e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 340 DYLKDELDELRAEMEEMrdsylEEDGYQL--QELRRELDRankncrilqyrLRKAEQKSLKVAETGQVDG--ELIRSLEQ 415
Cdd:pfam06160 207 TELPDQLEELKEGYREM-----EEEGYALehLNVDKEIQQ-----------LEEQLEENLALLENLELDEaeEALEEIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 416 DLKvakdvsvRLHHELETveEKRAKAE-DDN-ETLRQHMIEVEISRQALQNELERLRES--------SLKRRGSREIYKE 485
Cdd:pfam06160 271 RID-------QLYDLLEK--EVDAKKYvEKNlPEIEDYLEHAEEQNKELKEELERVQQSytlnenelERVRGLEKQLEEL 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958805813 486 KKLVNQIT-------LPRAVLawQDDSADLKCQLQFAKEEASLMRKKMAKLgrEKDELE--QELQKYKS 545
Cdd:pfam06160 342 EKRYDEIVerleekeVAYSEL--QEELEEILEQLEEIEEEQEEFKESLQSL--RKDELEarEKLDEFKL 406
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-617 |
8.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAE--QKSL-----KVAETGQVDGELIRSLE 414
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLaelekKLDELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 415 Q-DLKVAKDVSVRLH----------------HELETVEEKRAKAEDDNEtlrqhMIEVEISRqaLQNELERLRE--SSLK 475
Cdd:PRK03918 581 ElGFESVEELEERLKelepfyneylelkdaeKELEREEKELKKLEEELD-----KAFEELAE--TEKRLEELRKelEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 476 RRGSREIYKEK-----KLVNQITLPRAVLAWQDDSAD-LKCQLQFAKEEASLM---RKKMAKLGREKDELEQELQKYKSL 546
Cdd:PRK03918 654 KKYSEEEYEELreeylELSRELAGLRAELEELEKRREeIKKTLEKLKEELEERekaKKELEKLEKALERVEELREKVKKY 733
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958805813 547 ygdvdsplptgeaggppstrEAELKLR-LKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTSRD 617
Cdd:PRK03918 734 --------------------KALLKERaLSKVGEIASEIFEELTEGKYSGVRVKAEENKVKLFVVYQGKERP 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
342-474 |
8.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 342 LKDELDELRAEMEEMRDSYLEEDGyQLQELRRELdrankncrilqyrlrkAEQKSLKVAETGQVdgelIRSLEQDLKVAK 421
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHP-DVIALRAQI----------------AALRAQLQQEAQRI----LASLEAELEALQ 326
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958805813 422 DVSVRLHHELETVEEKRAKAEDDNETLRQHMIEVEISRQALQNELERLRESSL 474
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
300-671 |
8.88e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 300 PERTILGTPKEPSLGEQPRLLVVAEEEELLREMEELRSENDylKDELDELRAEMEEmRDSYLEEDGYQLQELRRELDRAN 379
Cdd:pfam07888 27 PRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD--REQWERQRRELES-RVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 380 KNCRILQYRLRKAEQKSLKVAETGQVdgeLIRSLEQDLKVAKDVSVRLHHELETVEEKRAKA-------EDDNETLRQHM 452
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAAHEA---RIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 453 IEVEISRQALQNELERLRESSLKRRGSREIYKEKKLVNQITLPRAVLAWQDDSADLKcQLQFAKEEASLMRKKMAKLGRE 532
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE-ELRSLQERLNASERKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805813 533 -------KDELEQELQKYKSLYGDV-----DSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEVENRGLKA 600
Cdd:pfam07888 260 lssmaaqRDRTQAELHQARLQAAQLtlqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERM 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958805813 601 EMEDIRVQHEREGTSRdhvpgipTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSK 671
Cdd:pfam07888 340 EREKLEVELGREKDCN-------RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| |
