|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
1220-1341 |
4.75e-45 |
|
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: 159.47 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 1220 MDLRWQIHHREKNWNREKVELLERLDSERQEWGRQKEELLWRVEQLQKEKSPRRS------------GSFLCSRREDDTR 1287
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRKinmnerakvidgEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 166235133 1288 PYPHQGSLHSSR--PVSMWPCEDADSIPFEDRPLSKLKESDRCSASENLYLDALSL 1341
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSL 136
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
622-714 |
3.09e-41 |
|
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: 147.06 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 622 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQESGWLGD--GVSKGPAASVPLQEELKSARLQIDE 699
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDgeGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 166235133 700 LSGKVLKLQCENRLL 714
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
493-587 |
4.67e-38 |
|
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: 137.81 E-value: 4.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 493 DSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASI 572
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 166235133 573 LGRKIVELEVENRGL 587
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-648 |
5.94e-13 |
|
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: 74.71 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:TIGR02168 689 LEEKIAELEKALAELRKE-LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 422 DVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQL 501
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 502 QFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstreAELKLRLKLVEEEASILGRKIVELE 581
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-------------ALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166235133 582 VENRGLKAEMEDIRVQHEREGTGRDHVPSTPTSPFGDSMEsstELRRHLQFVEEEAELLRRSISEIE 648
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-595 |
2.38e-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: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 345 ELDELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDVS 424
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 425 VRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQLQFV 504
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 505 KEEASLMRKKMAKLgrEKDELEQELQKYKSLYGDVDSPLPTGEAggppstREAELKLRLKLVEEEASILGRKIVELEVEN 584
Cdd:TIGR02168 420 QQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEE------ALEELREELEEAEQALDAAERELAQLQARL 491
|
250
....*....|.
gi 166235133 585 RGLKAEMEDIR 595
Cdd:TIGR02168 492 DSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-700 |
4.66e-09 |
|
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: 61.62 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 343 KDELDELRAEMEEMrDSYLEEDGYQLQELRRELDRANKNcRILQYRLRKAEQKSL----------KVAETGQVDgELIRS 412
Cdd:TIGR02169 176 LEELEEVEENIERL-DLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGYELlkekealerqKEAIERQLA-SLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 413 LEQDLKVAKDVSVRLHH---ELETVEEK-RAKAEDDNETLRQQMIEVEVsrqalqnEVERLRES-SLKRRGSREMYKEkk 487
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEieqLLEELNKKiKDLGEEEQLRVKEKIGELEA-------EIASLERSiAEKERELEDAEER-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 488 lvnqddSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeagGPPSTREAELKLRLKLVE 567
Cdd:TIGR02169 324 ------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL------EEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 568 EEASILGRKIVELEVENRGLKAEMEdirvqhEREGTGRDHvpstptspfgdSMESSTELRRHLQFvEEEAELLRRSISEI 647
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQ------RLSEELADL-----------NAAIAGIEAKINEL-EEEKEDKALEIKKQ 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 166235133 648 EDHNRQLTHELSKFKFEPHQESGWLGDgvskgpaasvpLQEELKSARLQIDEL 700
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDR-----------VEKELSKLQRELAEA 495
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
340-660 |
7.89e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.92 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 340 DYLKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKV 419
Cdd:COG4372 41 DKLQEELEQLREELEQAREE-LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-------LESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 420 AKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDS--ADL 497
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 498 KCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPST---REAELKLRLKLVEEEASILG 574
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEellEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 575 RKIVELEVENRGLKAEMEDIRVQHEREGTGRDHVPSTPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQL 654
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
....*.
gi 166235133 655 THELSK 660
Cdd:COG4372 353 NDVLEL 358
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-601 |
8.32e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:COG1196 258 LEAELAELEAELEELRL--------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 422 DVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQL 501
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 502 QFVKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLRLKLVEEEASILGRKIVELE 581
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEE--------------------ALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260
....*....|....*....|
gi 166235133 582 VENRGLKAEMEDIRVQHERE 601
Cdd:COG1196 470 EEAALLEAALAELLEELAEA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
340-574 |
2.17e-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: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 340 DYLKDELDELRAEMEEM--RDSYLEEDGYQLQELRRELDRankncRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 747 SSLEQEIENVKSELKELeaRIEELEEDLHKLEEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 418 KvakdvsvRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLrESSLKRrgsremyKEKKLvnqddsADL 497
Cdd:TIGR02169 822 N-------RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEE-------LEAAL------RDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 498 KCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGD--------------VDSPLPTGEAGGPPSTREAELKLRL 563
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElkaklealeeelseIEDPKGEDEEIPEEELSLEDVQAEL 960
|
250
....*....|.
gi 166235133 564 KLVEEEASILG 574
Cdd:TIGR02169 961 QRVEEEIRALE 971
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
350-654 |
3.21e-08 |
|
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: 58.60 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 350 RAEMEEMRDSYLEEDGYQLqELRRELDRankncriLQYRLRKAEQKSLKVAETGqVDGELIRSLEQDLKVAKDVSVRLHH 429
Cdd:pfam17380 326 QAEMDRQAAIYAEQERMAM-ERERELER-------IRQEERKRELERIRQEEIA-MEISRMRELERLQMERQQKNERVRQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 430 ELETVEEKRAKAEDDNETLRQQMIEVEVSR----QALQNEVERLREsslKRRGSREMYKEKKLVNQDDSADLKcqlqfvK 505
Cdd:pfam17380 397 ELEAARKVKILEEERQRKIQQQKVEMEQIRaeqeEARQREVRRLEE---ERAREMERVRLEEQERQQQVERLR------Q 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 506 EEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeaggppstrEAELKLR-LKLVEEEASilgRKIVELEVEN 584
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKIL--------------------EKELEERkQAMIEEERK---RKLLEKEMEE 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 585 RGLKAEMEDIRVQHEREgtGRDHVPSTPTSPFGDSMESSTELRRHLQFVEEEAELLRRsISEIEDHNRQL 654
Cdd:pfam17380 525 RQKAIYEEERRREAEEE--RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-IVESEKARAEY 591
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
13-317 |
3.51e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 13 PDTKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKDLHTRPATATPSAG--RAPTPAAPRsPSLAGKAPPSPGPPAA 90
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSppQRPRRRAAR-PTVGSLTSLADPPPPP 2705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 91 PGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGTrRAARAGPAEPLS--RVGRPTGAEPPPAVAkgrkTKRGPGTPPA 168
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP-PAVPAGPATPGGpaRPARPPTTAGPPAPA----PPAAPAAGPP 2780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 169 RAVVPPARASRVPAVtlsvtsvagcriNHTDSSSDLSDcaseplsdeqrllPAASSDAESGTGSSDREPIRGAPTPSSGS 248
Cdd:PHA03247 2781 RRLTRPAVASLSESR------------ESLPSPWDPAD-------------PPAAVLAPAAALPPAASPAGPLPPPTSAQ 2835
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166235133 249 RGPPPGSpeppillAAPPVASACLGGRSSPGG--ASTGSPGPGSQEDVGGRAPPERTILGTSKEPSLGEQP 317
Cdd:PHA03247 2836 PTAPPPP-------PGPPPPSLPLGGSVAPGGdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
7-303 |
9.54e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 57.49 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 7 PAGGGAPDTKPqPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKdLHTRPATATPSAGRAPTPAAPRSPSLAGKAPPSPG 86
Cdd:PHA03307 152 PPAAGASPAAV-ASDAASSRQAALPLSSPEETARAPSSPPAEPP-PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 87 PPAAPGRLSRRSGVVPGAKD-------KPPPGAGARSAGGAKAVPGTRRAARAGPAEPlsrVGRPTGAEPPPAvakgrkt 159
Cdd:PHA03307 230 DDAGASSSDSSSSESSGCGWgpenecpLPRPAPITLPTRIWEASGWNGPSSRPGPASS---SSSPRERSPSPS------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 160 krgPGTPPARAVVPPARASRvpavtlsvtSVAGcrinhtDSSSDLSDCASEPLSDEQRLLPAASSDAESGTGSSDREPIR 239
Cdd:PHA03307 300 ---PSSPGSGPAPSSPRASS---------SSSS------SRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166235133 240 GAPTPSSGSrgpppgspeppilLAAPPVASACLGGRSSPGGASTGSPGPGSQEDVGGRAPPERT 303
Cdd:PHA03307 362 PSSPRKRPR-------------PSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-480 |
1.99e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKncrilqyRLRKAEQKSLKVAetgqvdgELIRSLEQDLKVAK 421
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLE-------ALLAALGLPLPASA 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166235133 422 DVSVRLHHEletVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRE--SSLKRRGSR 480
Cdd:COG4913 380 EEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiASLERRKSN 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-670 |
2.04e-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: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 346 LDELRAEMEEMRDsYLEEDGYQLQELRRELDRANKncrilqYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVAKDVSV 425
Cdd:TIGR02168 181 LERTRENLDRLED-ILNELERQLKSLERQAEKAER------YKELKAELRELELALLVLRLEELREELEE-LQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 426 RLHHELETveeKRAKAEDDNETLRQQMIEVEVSRQALQ-------NEVERLRESSLKRRGSREMYKEKKLVNQDDSADLK 498
Cdd:TIGR02168 253 EELEELTA---ELQELEEKLEELRLEVSELEEEIEELQkelyalaNEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 499 CQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYgdvdsplptgeaggppstreAELKLRLKLVEEEASILGRKIV 578
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------------------EELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 579 ELEVE---NRG----LKAEMEDIRVQHER-EGTGRDHVPSTPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDH 650
Cdd:TIGR02168 390 QLELQiasLNNeierLEARLERLEDRRERlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|
gi 166235133 651 NRQLTHELSKFKFEPHQESG 670
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQA 489
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-534 |
3.76e-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: 55.50 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDsyleedgyqlqELRRELDRANKNCRILQYRLRKAEqKSLKVAETG------QVD--GELIRSL 413
Cdd:pfam05483 546 LRDELESVREEFIQKGD-----------EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKcnnlkkQIEnkNKNIEEL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 414 EQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQAlQNEVERLRESSLKRRGSREMYKEKKLVNQDD 493
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 166235133 494 SADLKCQLQfVKEEASLMRKKMAKLGREKDELEQELQKYKS 534
Cdd:pfam05483 693 EIDKRCQHK-IAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-717 |
5.55e-07 |
|
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: 54.64 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRD------SYLEEDGYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKvaetGQVDGELIRSL 413
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTqlnqlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN----NQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 414 EQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEV-ERLRE-SSLKRRgsREMYKE--KKLV 489
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELeEKQNEiEKLKKE--NQSYKQeiKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 490 NQddSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEaggppsTREAELKLRLKLVEEE 569
Cdd:TIGR04523 391 SQ--INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT------NQDSVKELIIKNLDNT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 570 ASILGRKIVELEVENRGLKAEMEDIrvQHEREGTGRDHvpSTPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIED 649
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQK--QKELKSKEKEL--KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 650 HNRQLTHELSKFKFephqesgwlgdgvskgpaasvplqeELKSARL--QIDELSGKVLKLQCENRLLLSN 717
Cdd:TIGR04523 539 KISDLEDELNKDDF-------------------------ELKKENLekEIDEKNKEIEELKQTQKSLKKK 583
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-767 |
6.43e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 344 DELDELRAEMEEmrdsyleedgyQLQELRRELDRANKNcRILQYRLRKAEQKSLKVAetgqvdgelIRSLEQDLKVAKDV 423
Cdd:COG1196 189 ERLEDILGELER-----------QLEPLERQAEKAERY-RELKEELKELEAELLLLK---------LRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 424 SVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQLQF 503
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 504 VKEEASLMRKKMAKLGREKDELEQELQkykslygdvdsplptgeaggppsTREAELKLRLKLVEEEASILGRKIVELEVE 583
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELE-----------------------EAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 584 NRGLKAEMEDIRVQHEREgtgrdhvpstptspfgdsmessTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKF 663
Cdd:COG1196 385 AEELLEALRAAAELAAQL----------------------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 664 EPHQESGWLGDgvskgpaasvpLQEELKSARLQIDELSGKVLKLQCENRLLLSNAQRGDLAAHLGLRApsprdsdAESDA 743
Cdd:COG1196 443 ALEEAAEEEAE-----------LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-------EADYE 504
|
410 420
....*....|....*....|....
gi 166235133 744 GKKESDGEEGRLPQPKREGPVGGE 767
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
41-301 |
6.47e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 41 APSPARPFLKDLHTRP-ATATPSAGRAP-----TPAAPRSPSLAGKAPPSPGPPAAPGRLSRRSGVVPGAKDKPPPGAGA 114
Cdd:PHA03247 2574 APRPSEPAVTSRARRPdAPPQSARPRAPvddrgDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPR 2653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 115 RSAGGAKAVPGTRRAARAGPAEPLSRVGRPTGAEPPPAVAKGRKTKRGPGTPPARAVVPPARASRVPAVTLSVTSVAGCR 194
Cdd:PHA03247 2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP 2733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 195 INHTDSSSDLS-DCASEPLSDEQRLLPAASSDAESGTGSSDRE--PIRGAPTPSSGSRGPPPGSPEPPILLAAPPVA--- 268
Cdd:PHA03247 2734 ALPAAPAPPAVpAGPATPGGPARPARPPTTAGPPAPAPPAAPAagPPRRLTRPAVASLSESRESLPSPWDPADPPAAvla 2813
|
250 260 270
....*....|....*....|....*....|....
gi 166235133 269 -SACLGGRSSPggaSTGSPGPGSQEDVGGRAPPE 301
Cdd:PHA03247 2814 pAAALPPAASP---AGPLPPPTSAQPTAPPPPPG 2844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-662 |
8.75e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRILQYRLR---------KAEQKSL--KVAETGQVDG--- 407
Cdd:PRK03918 219 LREELEKLEKEVKE-----LEELKEEIEELEKELESLEGSKRKLEEKIReleerieelKKEIEELeeKVKELKELKEkae 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 408 ---ELIRSLEQDLKVAKDVSVRL---HHELETVEEKRAKAEDDNETLRqqmiEVEVSRQALQNEVERLRESSLK----RR 477
Cdd:PRK03918 294 eyiKLSEFYEEYLDELREIEKRLsrlEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELyeeaKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 478 GSREMYKEKKLVNQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREA 557
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 558 ELKLRLKLVEEEASILGRKIvELEVENRGLKAEMEDIRVQHEREgtgRDHVPSTPTSPFGDSMESSTEL--RRHLQFVEE 635
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKE---SELIKLKELAEQLKELEEKLKKynLEELEKKAE 525
|
330 340
....*....|....*....|....*..
gi 166235133 636 EAELLRRSISEIEDHNRQLTHELSKFK 662
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-533 |
2.58e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 350 RAEMEEMRDSYLEEDGYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHH 429
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 430 ELETVEEKRAKAED--DNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQLQFVKEE 507
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
170 180 190
....*....|....*....|....*....|..
gi 166235133 508 ASLMR------KKMAKLGREKDELEQELQKYK 533
Cdd:PTZ00121 1746 AEEAKkdeeekKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-534 |
2.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 344 DELDELRAEMEEMRDSY--LEedgyQLQELRRELDRANKNCRILQY-----RLRKAEQK-SLKVAETGQVDGELiRSLEQ 415
Cdd:COG4913 235 DDLERAHEALEDAREQIelLE----PIRELAERYAAARERLAELEYlraalRLWFAQRRlELLEAELEELRAEL-ARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 416 DLKVAKDVSVRLHHELETVEEKRAKAEDDN-ETLRQQMIEVEVSRQALQNEVERLRES----SLKRRGSREMYKEKKLVN 490
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 166235133 491 QDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKS 534
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
367-619 |
3.15e-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: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 367 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDvsvrlhhELETVEEKRAKAEDDNE 446
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALAR-------RIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 447 TLRQQMIEVEVSRQALQNEV-ERLRESSLKRRGSREMYkekkLVNQDDSAD-------LKCQLQFVKEEASLMRKKMAKL 518
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELaELLRALYRLGRQPPLAL----LLSPEDFLDavrrlqyLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 519 GREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQH 598
Cdd:COG4942 163 AALRAELEAERAELEALLAEL-------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250 260
....*....|....*....|..
gi 166235133 599 ER-EGTGRDHVPSTPTSPFGDS 619
Cdd:COG4942 230 ARlEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
430-710 |
3.96e-06 |
|
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: 51.99 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 430 ELETVEEKRAKAEDDNETLRQQMIEVEVSR------QALQNEVERlRESSLKRRGSREMYKEKKLVnQDDSADLKCQLQF 503
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKRE-YEGYELLKEKEALERQKEAI-ERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 504 VKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEVE 583
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE-----EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 584 NRGLKAEMEDIRVQHEREGTGRDHVpstpTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELskfkf 663
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI----- 401
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 166235133 664 EPHQ-ESGWLGDGVSKGPAASVPLQEELKSARLQIDELSGKVLKLQCE 710
Cdd:TIGR02169 402 NELKrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
337-653 |
5.02e-06 |
|
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: 51.61 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 337 SENDYLKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQD 416
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASR--------KIGEIEKEIEQLEQEEEKLKERLEELEED--------------LSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 417 LKVAKDVSVRLHHELETVEEKRAKAEDDNETL-----RQQMIEVEVSRQALQNEVERLR------ESSLKRRGSREMYKE 485
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEarlreiEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 486 KKLVN-QDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGppstREAE------ 558
Cdd:TIGR02169 833 KEIQElQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL----RELErkieel 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 559 ------LKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDI----RVQHEREGTGRD-----HVPSTPTSPFGDSMESS 623
Cdd:TIGR02169 909 eaqiekKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsleDVQAELQRVEEEiralePVNMLAIQEYEEVLKRL 988
|
330 340 350
....*....|....*....|....*....|
gi 166235133 624 TELRRHLQFVEEEAELLRRSISEIEDHNRQ 653
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
6-312 |
7.34e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.33 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 6 GPAGGGAPDTKPQPAGqhhrhhhlHPLAERRRLHRAPSPARPFLKDLHTRPATATPSAGRAPTPAAPRSPSLAgkappsp 85
Cdd:PHA03307 60 AACDRFEPPTGPPPGP--------GTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 86 gPPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGTRRAARAGPAEPLSRVGRPTGAEPPPAVAKGRKTKRGPGT 165
Cdd:PHA03307 125 -SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 166 PPARAVVPPARASRVPAVTLSVTSVAGCRINHTDSS--SDLSDCASEPLSDEQRLLPA-----ASSDAESGTGSSDREPI 238
Cdd:PHA03307 204 PRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSssSESSGCGWGPENECPLPRPApitlpTRIWEASGWNGPSSRPG 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166235133 239 RGAPTPSSGSRGPPPGSPEPPILLAAPPVASACLGGRSSPGGASTGSPGPGSQEDVGGRAPPERTILGTSKEPS 312
Cdd:PHA03307 284 PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPP 357
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
342-600 |
7.81e-06 |
|
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: 50.89 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRdsyleedgYQLQELRRELDRANKNCRILQYRLRKAEQkslkvaetgqvdgeLIRSLEQDLKVAK 421
Cdd:pfam05557 109 LKNELSELRRQIQRAE--------LELQSTNSELEELQERLDLLKAKASEAEQ--------------LRQNLEKQQSSLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 422 DVSVRlhheLETVEEKRAKAEDDNETLRQQMIEVEvSRQALQNEVERLRESSLKRRGSremyKEKKLVNQDDSADLKCQL 501
Cdd:pfam05557 167 EAEQR----IKELEFEIQSQEQDSEIVKNSKSELA-RIPELEKELERLREHNKHLNEN----IENKLLLKEEVEDLKRKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 502 QfvKEEAslMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPP----STREAELKLRLKLVEEEASILGRKI 577
Cdd:pfam05557 238 E--REEK--YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlQQREIVLKEENSSLTSSARQLEKAR 313
|
250 260
....*....|....*....|...
gi 166235133 578 VELEVENRGLKAEMEDIRVQHER 600
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKR 336
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-476 |
1.48e-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: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 338 ENDYLKDELDELRAEMEEMRdSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLR-AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166235133 418 KVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERL--RESSLKR 476
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVekELSKLQR 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-654 |
1.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSYLE--------EDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdGELIRSL 413
Cdd:COG4717 93 LQEELEELEEELEELEAELEElreeleklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 414 EQDLKVAKDVSVRLHHELETVEEKRAK-AEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQD 492
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 493 DS--------------------------ADLKCQLQFVKEEASLMRKKMAKLGREKDEL----------EQELQKYKSLY 536
Cdd:COG4717 249 RLllliaaallallglggsllsliltiaGVLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleeleEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 537 GdVDSPLPTGEAGGPPST-----------REAELKLRLKLVEEEASILG-----------RKIVELEVENRGLKAEMEDI 594
Cdd:COG4717 329 G-LPPDLSPEELLELLDRieelqellreaEELEEELQLEELEQEIAALLaeagvedeeelRAALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 595 RVQHEREGTGRDHVPSTPTspFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQL 654
Cdd:COG4717 408 EEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
342-543 |
2.50e-05 |
|
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: 47.72 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSYLEED-------------GYQLQELRRELDRANKNCRILQYRLRKAEQKS------LKVAE- 401
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEkraekaeaevaalNRRIQLLEEELERTEERLAEALEKLEEAEKAAdesergRKVLEn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 402 TGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSRE 481
Cdd:pfam00261 86 RALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166235133 482 MYKEKKLVNQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPL 543
Cdd:pfam00261 166 KASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
351-711 |
2.71e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 351 AEMEEMRDSYLEEDGYQLQE------LRRELDRANKNCRILQ--------YRLRKAEQKSL-------------KVAETG 403
Cdd:COG5022 734 AALEDMRDAKLDNIATRIQRairgryLRRRYLQALKRIKKIQviqhgfrlRRLVDYELKWRlfiklqpllsllgSRKEYR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 404 QVDgELIRSLEQDLKVAKDVSVRLHHELETVEE-------------KRAKAEDDNETLRQQMIEVEVSR---QALQNEVE 467
Cdd:COG5022 814 SYL-ACIIKLQKTIKREKKLRETEEVEFSLKAEvliqkfgrslkakKRFSLLKKETIYLQSAQRVELAErqlQELKIDVK 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 468 RLRESSLKRRGSREMYKEKKlvnQDDSADLKCQLQFvKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptge 547
Cdd:COG5022 893 SISSLKLVNLELESEIIELK---KSLSSDLIENLEF-KTELIARLKKLLNNIDLEEGPSIEYVKLPEL------------ 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 548 aggppstreaelklrLKLVEEEASiLGRKIVELEVENrglkaEMEDIrvqHEREGtgrdHVPSTPTSPFGDSMESSTELR 627
Cdd:COG5022 957 ---------------NKLHEVESK-LKETSEEYEDLL-----KKSTI---LVREG----NKANSELKNFKKELAELSKQY 1008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 628 RHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK-FEPHQESgwlgdgVSKGPAASVPLQEELKSARLQIDelSGKVLK 706
Cdd:COG5022 1009 GALQESTKQLKELPVEVAELQSASKIISSESTELSiLKPLQKL------KGLLLLENNQLQARYKALKLRRE--NSLLDD 1080
|
....*
gi 166235133 707 LQCEN 711
Cdd:COG5022 1081 KQLYQ 1085
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-477 |
2.97e-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: 47.61 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSYLEEDGyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDG---ElIRSLEQDLK 418
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqkE-IESLKRRIS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 166235133 419 VAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRR 477
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
423-823 |
4.70e-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: 48.53 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 423 VSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQLQ 502
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 503 FVKEEASLMRKKMAKLGREKDELEQELQKYkslygdvdsplptgeaggppstreaelklRLKLVEEEASILGRKIVELEV 582
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKL-----------------------------EEALNDLEARLSHSRIPEIQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 583 ENRGLKAEMEDIRvqheregtgrdhvpstptspfgdsmESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 662
Cdd:TIGR02169 799 ELSKLEEEVSRIE-------------------------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 663 FEPHQESGWLGDgvskgpaasvpLQEELKSARLQIDELSGKVLKLQcenrlllsnAQRGDLAAHLglrapsprdSDAESD 742
Cdd:TIGR02169 854 KEIENLNGKKEE-----------LEEELEELEAALRDLESRLGDLK---------KERDELEAQL---------RELERK 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 743 AGKKESDGEEGRLPQPKREGPVGGESDSEDMFEKTSGFGSGKPSEAS--EPCPAELLRVREDTECLVTIKLEA-QRLERT 819
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRALEPVNMLAiQEYEEV 984
|
....
gi 166235133 820 VERL 823
Cdd:TIGR02169 985 LKRL 988
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
342-600 |
6.18e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMR-------------DSYLEEDgyqlQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGE 408
Cdd:PRK02224 211 LESELAELDEEIERYEeqreqaretrdeaDEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 409 LIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRrgsREMYKEKkl 488
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL---EERAEEL-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 489 vnQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPT-----GEAGGPPSTREAELKLRL 563
Cdd:PRK02224 362 --REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElreerDELREREAELEATLRTAR 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 166235133 564 KLVEEEASIL-------------GRKIVELEVENRG----LKAEMEDIRVQHER 600
Cdd:PRK02224 440 ERVEEAEALLeagkcpecgqpveGSPHVETIEEDRErveeLEAELEDLEEEVEE 493
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
7-247 |
7.08e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 7 PAGGGAPDTKPQPAgqhHRHHHLHPLAERRRLHRAPSPARPFLKDLHTRPATATPSAG------RAPTPAAPRSP---SL 77
Cdd:PHA03247 2824 PAGPLPPPTSAQPT---APPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAParppvrRLARPAVSRSTesfAL 2900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 78 AGKAPPSPGPPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGTRRAARAGPAEPLSRVGRPTGAEPPpaVAKGR 157
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVA--VPRFR 2978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 158 KTKRGPGTPPARAVVPPARASRVPAVTLSVTSVAgcriNHTDSssdlsdcASEPLSDEQRLLPAASSDAESGTGSSDREP 237
Cdd:PHA03247 2979 VPQPAPSREAPASSTPPLTGHSLSRVSSWASSLA----LHEET-------DPPPVSLKQTLWPPDDTEDSDADSLFDSDS 3047
|
250
....*....|...
gi 166235133 238 IR---GAPTPSSG 247
Cdd:PHA03247 3048 ERsdlEALDPLPP 3060
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
330-660 |
1.20e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 330 REMEELRSENDYLKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRankncRILQYRLRKAEQKSLKVAETGQVDG-E 408
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE-----YLLYLDYLKLNEERIDLLQELLRDEqE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 409 LIRSLEQDLKVAKDVSVRLHHEL-------ETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKrrgsre 481
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENkeeekekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK------ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 482 myKEKKLVN-QDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDvdsplptgeaggppstREAELK 560
Cdd:pfam02463 326 --AEKELKKeKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL----------------ESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 561 LRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTGRDHVPStptspFGDSMESSTELRRHLQFVEEEAELL 640
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-----SIELKQGKLTEEKEELEKQELKLLK 462
|
330 340
....*....|....*....|
gi 166235133 641 RRSISEIEDHNRQLTHELSK 660
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKL 482
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
367-531 |
1.26e-04 |
|
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: 47.05 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 367 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAE 442
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 443 DDNETLRQQMI-EVEVSRQALQN---EVE-RLRE--SSLKRRGSREMYKEKKLV------------NQDDSADL-KCQLQ 502
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRLNEARREQAKAVvslrqiqhratqEKERNQELrRLQDE 638
|
170 180
....*....|....*....|....*....
gi 166235133 503 FVKEEASLMRKKMAKLGREKDELEQELQK 531
Cdd:pfam07111 639 ARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-648 |
1.32e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 390 RKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERL 469
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 470 RESSLKRRGSREMYKEkklvnqddsadlkcQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeag 549
Cdd:COG4372 86 NEQLQAAQAELAQAQE--------------ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 550 gppSTREAELK-LRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTGRDHVPSTPTSPFGDSMESSTELRR 628
Cdd:COG4372 146 ---AEREEELKeLEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260
....*....|....*....|
gi 166235133 629 HLQFVEEEAELLRRSISEIE 648
Cdd:COG4372 223 AKDSLEAKLGLALSALLDAL 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
410-590 |
1.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 410 IRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLREsSLKRRGsREMYKEKK-- 487
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-ELGERA-RALYRSGGsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 488 -----LVNQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLR 562
Cdd:COG3883 103 syldvLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA--------------------KLAELEAL 162
|
170 180
....*....|....*....|....*...
gi 166235133 563 LKLVEEEASILGRKIVELEVENRGLKAE 590
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
342-656 |
1.79e-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: 46.66 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRD-----SYLEEdgyQLQELRRELDRANK---NCRILQYRLRKAEQKSLKVAETGQVDGELIRSL 413
Cdd:pfam05557 202 LEKELERLREHNKHLNEnienkLLLKE---EVEDLKRKLEREEKyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 414 EQdlkvakdvsvrLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKlvnqdd 493
Cdd:pfam05557 279 ED-----------LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV------ 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 494 sADLKCQLQFVKEEASLMR-------KKMA------KLGREKDELEQELQKYKSLYGDVDSPLPTGE--AGG---PPSTR 555
Cdd:pfam05557 342 -RRLQRRVLLLTKERDGYRailesydKELTmsnyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEeeLGGykqQAQTL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 556 EAELKLRLK--------LVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTGRD---------HVPSTPTSpfgD 618
Cdd:pfam05557 421 ERELQALRQqesladpsYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDydpkktkvlHLSMNPAA---E 497
|
330 340 350
....*....|....*....|....*....|....*...
gi 166235133 619 SMESSTELRRHLQfveEEAELLRRSISEIEDHNRQLTH 656
Cdd:pfam05557 498 AYQQRKNQLEKLQ---AEIERLKRLLKKLEDDLEQVLR 532
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-662 |
1.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 332 MEELRSENDYLKDELDELRAEM-------------------------EEMRDSYLEEDGYQLQELRRELDRANKNCRILQ 386
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIkelkkaieelkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLR 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 387 YRLRKAEQKSLKVAETGQVD--GELIRSLEQDLKVakdvsvrlhHELETVEEKrakaEDDNETLRQQMIEVEVSRQALQN 464
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKelAEQLKELEEKLKK---------YNLEELEKK----AEEYEKLKEKLIKLKGEIKSLKK 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 465 EVERLREsslkrrgsremYKEKKlvnqddsADLKCQLQFVKEEASLMRKKMAKLGREK-DELEQELQKYKSLYGDVDspl 543
Cdd:PRK03918 547 ELEKLEE-----------LKKKL-------AELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYL--- 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 544 ptgEAGGPPSTREAELKlRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREgtgrdhvpstptsPFGDSMESS 623
Cdd:PRK03918 606 ---ELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-------------EYEELREEY 668
|
330 340 350
....*....|....*....|....*....|....*....
gi 166235133 624 TELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 662
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
8-311 |
2.09e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 8 AGGGAPDTKPQPAGQHHRHHHLHPLAERRrlhrapsPARPflkdlhtrPATATPSAGRAPT-PAAPRSPSLAGKAPPSPG 86
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPAR-------PARP--------PTTAGPPAPAPPAaPAAGPPRRLTRPAVASLS 2792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 87 PPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGT--RRAARAGPAEPLSRVGRPTGAEPPPAVAKGRKTKRGPG 164
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTsaQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPA 2872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 165 TPPARAVVPPARASRVPAVTLSVTSVAgcrinhtdsssdlsdcasEPlSDEQRLLPAASSDAESGTGSSDREPIRGAPTP 244
Cdd:PHA03247 2873 AKPAAPARPPVRRLARPAVSRSTESFA------------------LP-PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP 2933
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166235133 245 SSGSRgpppgspeppillaaPPVASACLGGRSSPGGASTGSPGPGSQEDVGGRAPPERTILGTSKEP 311
Cdd:PHA03247 2934 PPPPR---------------PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS 2985
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
342-601 |
2.22e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEM---RDSYLEedgyQLQELRRELDRANKncrilqyrLRKAEQKSLKvaetgqvdgELIRSLEQDLK 418
Cdd:COG1340 27 LKEKRDELNEELKELaekRDELNA----QVKELREEAQELRE--------KRDELNEKVK---------ELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 419 VAKDVSvrlhhelETVEEKRAKaeddnetlRQQMIEVEVSRQALQNEVERLRE----SSLKRRGSREMYK-----EKKLV 489
Cdd:COG1340 86 KLNELR-------EELDELRKE--------LAELNKAGGSIDKLRKEIERLEWrqqtEVLSPEEEKELVEkikelEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 490 NQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYK----SLYGDVDSplptgeaggppSTREA-------- 557
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHeemiELYKEADE-----------LRKEAdelhkeiv 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 166235133 558 ELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHERE 601
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
342-571 |
2.54e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEmRDSYLEEDGYQLQELRRE--------------LDRANKNCRILQyrlRKAE--QKSLKVAEtGQV 405
Cdd:pfam10174 343 LQTEVDALRLRLEE-KESFLNKKTKQLQDLTEEkstlageirdlkdmLDVKERKINVLQ---KKIEnlQEQLRDKD-KQL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 406 DG--ELIRSLEQDlkvakdvSVRLHHELETVEEKRAKAEDDNETLRQQMievEVSRQALQNEVERLRESSlkrrgsrEMY 483
Cdd:pfam10174 418 AGlkERVKSLQTD-------SSNTDTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKKEN-------KDL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 484 KEKKLVNQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRL 563
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI 560
|
....*...
gi 166235133 564 KLVEEEAS 571
Cdd:pfam10174 561 RLLEQEVA 568
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
6-303 |
2.55e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.06 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 6 GPAGGGAPDTKPQPAGQHHRHHHLHPLAERR---RLHRAPSPARPFLKDLHTRPATATPS-AGRAPTPAAPrSPSLAGKa 81
Cdd:pfam05109 465 GPTVSTADVTSPTPAGTTSGASPVTPSPSPRdngTESKAPDMTSPTSAVTTPTPNATSPTpAVTTPTPNAT-SPTLGKT- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 82 ppspgppaapgrlSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGT-RRAARAGPAEPLSRVGRPTGAEPPPAVAKGRKTK 160
Cdd:pfam05109 543 -------------SPTSAVTTPTPNATSPTPAVTTPTPNATIPTLgKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTL 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 161 RGPGTPPArAVVPPARASRvpAVTLSvtsvagcriNHTDSSSDLSDCASEPLSDEQRLLPAASSDaesgtgSSDREPIRG 240
Cdd:pfam05109 610 GGTSSTPV-VTSPPKNATS--AVTTG---------QHNITSSSTSSMSLRPSSISETLSPSTSDN------STSHMPLLT 671
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166235133 241 APTPSSG---SRGPPPGSPEPPILLAAPPVASACLGGRSSPGGASTgSPGPGSQEDVGGRAPPERT 303
Cdd:pfam05109 672 SAHPTGGeniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST-STKPGEVNVTKGTPPKNAT 736
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-531 |
2.57e-04 |
|
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: 45.87 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEmRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEqksLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:pfam05483 592 LENKCNNLKKQIEN-KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE---LELASAKQKFEEIIDNYQKEIEDKK 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 422 DVSVRLHHELEtveekRAKAEDDNETLRQQMIEVEVSRQ-----ALQNEVERLRESSLKRRGSR-EMYKEKKLVNQDDSA 495
Cdd:pfam05483 668 ISEEKLLEEVE-----KAKAIADEAVKLQKEIDKRCQHKiaemvALMEKHKHQYDKIIEERDSElGLYKNKEQEQSSAKA 742
|
170 180 190
....*....|....*....|....*....|....*.
gi 166235133 496 DLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQK 531
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-1266 |
2.63e-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: 46.20 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 367 QLQELRRELDRANKNcriLQYRLRKAEQ-KSLKVAETgqvdgelirslEQDLKVAKDVSVRLHHELETVEEKRAKAEDDN 445
Cdd:TIGR02168 190 RLEDILNELERQLKS---LERQAEKAERyKELKAELR-----------ELELALLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 446 ETLRQQMIEVEVSRQALQNEVERLRESSLKRRGsrEMYKEKKLVNqddsaDLKCQLQFVKEEASLMRKKMAKLGREKDEL 525
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQK--ELYALANEIS-----RLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 526 EQELQKYKslygdvdsplptgeaggppsTREAELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHERegtgr 605
Cdd:TIGR02168 329 ESKLDELA--------------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 606 dhvpstptspfgdsmessteLRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKfkfephqesgwlgdgvskgpaasvp 685
Cdd:TIGR02168 384 --------------------LRSKVAQLELQIASLNNEIERLEARLERLEDRRER------------------------- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 686 LQEELKSARLQIDELSGKVLKLQCENRlllsNAQRGDLAAHLGLRAPSPRDSDAESDAGKKESDGEEGRLPQpkregpVG 765
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELEEL----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ------LQ 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 766 GESDS-EDMFEKTSGFGSGKPSEASE--------PCPAELLRVREDTECLVTIKLEAQRLERTVERLISDTDGFIHDSGL 836
Cdd:TIGR02168 489 ARLDSlERLQENLEGFSEGVKALLKNqsglsgilGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQN 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 837 RGNGLASPGVQGGGGEGNSPSEPHLLETINVRMkAFRKELQAFLEQMSRIVDGLsplshltesssfLSTVTSVsrdspig 916
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL-GVAKDLVKFDPKLRKALSYL------------LGGVLVV------- 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 917 tlgkelgPDLQSKLReqlewqlnqDRGDEREGLRLrATRELHR-RADGDSGSHHGLGGQSCFNLEMEEDHLyalrWKELE 995
Cdd:TIGR02168 629 -------DDLDNALE---------LAKKLRPGYRI-VTLDGDLvRPGGVITGGSAKTNSSILERRREIEEL----EEKIE 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 996 MHSLALQNTLHKR-TWSDEKNLLQQELRSLKQNIFLFYVKLRWLLKHWRQGKQMEEGGEDLEESEHPEnvpgLAELGVQG 1074
Cdd:TIGR02168 688 ELEEKIAELEKALaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE----LTELEAEI 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 1075 VHQTDGIDQEDAdqgcslpmgehaphSLVQISEHGSRLQSSdggpLNKQVVENQQLFRALKALLEDFRsELREDEHARLR 1154
Cdd:TIGR02168 764 EELEERLEEAEE--------------ELAEAEAEIEELEAQ----IEQLKEELKALREALDELRAELT-LLNEEAANLRE 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 1155 LQQQYASDKAAWDVEWAVLKCRLEQLEEKTEKSLGELDSSAEGKGALKKEREVHQKLLADSHSLVMDLRWQIH---HREK 1231
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelsEELR 904
|
890 900 910
....*....|....*....|....*....|....*...
gi 166235133 1232 NWNREKVEL---LERLDSERQEWGRQKEELLWRVEQLQ 1266
Cdd:TIGR02168 905 ELESKRSELrreLEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
9-242 |
3.30e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.64 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 9 GGGAPDTKPQPAGQHhrhhhlhPLAERRRLHRAPSPARPflkdlhtRPATATPSAGRAPTPAAPRSPSLAGKAPPSPGPP 88
Cdd:PRK12323 366 GQSGGGAGPATAAAA-------PVAQPAPAAAAPAAAAP-------APAAPPAAPAAAPAAAAAARAVAAAPARRSPAPE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 89 ---AAPGRLSRRSGVVPGAKDKPPPgagarsaggaKAVPGTRRAArAGPAEPLsrvgrPTGAEPPPAVAKGRKTKRGPGT 165
Cdd:PRK12323 432 alaAARQASARGPGGAPAPAPAPAA----------APAAAARPAA-AGPRPVA-----AAAAAAPARAAPAAAPAPADDD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166235133 166 PPARAVVPPARASRVPAVTLSVTSVAGCRINHTDSSSDLSDcASEPLSDEQRLLPAASSDAESGTGSSDREPIRGAP 242
Cdd:PRK12323 496 PPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDD-AFETLAPAPAAAPAPRAAAATEPVVAPRPPRASAS 571
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
7-300 |
4.38e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.23 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 7 PAGGGAPdtkpqPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKdlhtrPATATPSAGRAPTPAAPRSPSLAGKAPPSPG 86
Cdd:PRK07003 362 VTGGGAP-----GGGVPARVAGAVPAPGARAAAAVGASAVPAVT-----AVTGAAGAALAPKAAAAAAATRAEAPPAAPA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 87 PPAAPGRLSR-RSGVVPGAKDKPPPGAGARSAGGAKAVPGTRRAARAGPAeplsrvgrptGAEPPPAvakgRKTKRGPGT 165
Cdd:PRK07003 432 PPATADRGDDaADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPA----------SDAPPDA----AFEPAPRAA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 166 PPARAVVPPARASRVPAVTlsvtsvagcrinhtdSSSDLSDCASEPLSDEQRLLPAASSDAESGTG-------------- 231
Cdd:PRK07003 498 APSAATPAAVPDARAPAAA---------------SREDAPAAAAPPAPEARPPTPAAAAPAARAGGaaaaldvlrnagmr 562
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 232 -SSDREPIRGAPTPSSGSrgpPPGSPEPPILLAAPPVASACLGGRSSPGGASTGSPGPGSQEDvgGRAPP 300
Cdd:PRK07003 563 vSSDRGARAAAAAKPAAA---PAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQAAES--RGAPP 627
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
342-533 |
5.48e-04 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 44.83 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMrdsylEEDGY---------QLQELRRELDRANKNcrILQYRLRKAEQKsLKVAETgQVDgELIRS 412
Cdd:COG4477 227 LPDQLEELKSGYREM-----KEQGYvlehlniekEIEQLEEQLKEALEL--LEELDLDEAEEE-LEEIEE-EID-ELYDL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 413 LEQDLKVAKDVsvrlHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRE-----SSLKRRG--SREMYKE 485
Cdd:COG4477 297 LEKEVEAKKYV----DKNQEELEEYLEHLKEQNRELKEEIDRVQQSYRLNENELEKVRNlekqiEELEKRYdeIDERIEE 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 166235133 486 KKLVN---QDDSADLKCQLQFVKEEASLMRKKMAKLgrEKDELE--QELQKYK 533
Cdd:COG4477 373 EKVAYselQEELEEIEEQLEEIEEEQEEFSEKLKSL--RKDELEarEKLDELK 423
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
6-181 |
6.55e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 6 GPAGGGAPDTKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPflkdlHTRPATATPSAGrAPTP--AAPRSPSLAGKAPP 83
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-----AALPPAASPAGP-LPPPtsAQPTAPPPPPGPPP 2847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 84 SPgppaapgrLSRRSGVVPGA--KDKPPPGAGARSAGGAKAVPGTRRAARAGPAEPLSRVGRPTGAEPPPAVAKGRKTKR 161
Cdd:PHA03247 2848 PS--------LPLGGSVAPGGdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP 2919
|
170 180
....*....|....*....|
gi 166235133 162 GPGTPPARAVVPPARASRVP 181
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRP 2939
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
426-657 |
1.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 426 RLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQnEVERLRESSLKRRGSREMYKEKK------LVNQDDSADLKC 499
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEaelerlDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 500 QLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTReAELKLRL------KLVEEEASIL 573
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-ALLEERFaaalgdAVERELRENL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 574 GRKIVELEVENRGLKAEMEDIRVQHEREGTGrdhvpstPTSPFGDSMESSTELRRHLQFVEEE---------AELLRR-S 643
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAFNREWPA-------ETADLDADLESLPEYLALLDRLEEDglpeyeerfKELLNEnS 844
|
250
....*....|....
gi 166235133 644 ISEIEDHNRQLTHE 657
Cdd:COG4913 845 IEFVADLLSKLRRA 858
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
342-535 |
1.10e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRD---------SYLEEDGYQLQELRRELDRankncriLQYR-----LRKAEQKSLkVAEtgqvdg 407
Cdd:COG1340 76 LKEERDELNEKLNELREeldelrkelAELNKAGGSIDKLRKEIER-------LEWRqqtevLSPEEEKEL-VEK------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 408 elIRSLEQDLKVAKDvSVRLHHELETVEEKRAKAEDDNETLRQQMievevsrQALQNEVERLRESSLKRRGSR-EMYKE- 485
Cdd:COG1340 142 --IKELEKELEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKI-------KELAEEAQELHEEMIELYKEAdELRKEa 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166235133 486 ----KKLVNQDDSAD--------LKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSL 535
Cdd:COG1340 212 delhKEIVEAQEKADelheeiieLQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
344-598 |
1.17e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 344 DELDELRAEMEEMRDSYLEEdgyqLQELRrELDRANKN----CRILQYRLRKaeqkslKVAETGQVDGELIRSLEQDLKV 419
Cdd:PRK04778 108 NEIESLLDLIEEDIEQILEE----LQELL-ESEEKNREeveqLKDLYRELRK------SLLANRFSFGPALDELEKQLEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 420 AKDvsvrlhhELETVEEKRA------------KAEDDNETLRQQMIEV-EVSRQaLQNEV-ERLREssLKRrGSREMYKE 485
Cdd:PRK04778 177 LEE-------EFSQFVELTEsgdyveareildQLEEELAALEQIMEEIpELLKE-LQTELpDQLQE--LKA-GYRELVEE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 486 K-KLvnqdDSADLKCQLQFVKEEASLMRKKMAKLgrEKDELEQELQ----KYKSLYgdvdsplptgeaggppSTREAELK 560
Cdd:PRK04778 246 GyHL----DHLDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEeiqeRIDQLY----------------DILEREVK 303
|
250 260 270
....*....|....*....|....*....|....*...
gi 166235133 561 LRlKLVEEEASILGRKIVELEVENRGLKAEMEdiRVQH 598
Cdd:PRK04778 304 AR-KYVEKNSDTLPDFLEHAKEQNKELKEEID--RVKQ 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-534 |
1.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 344 DELDELRAEMEEMRDSYleedgYQLQELRRELDRANKNCRILQYRLRKAEQK--SLKVAETGQVDGELIRSLEQDLKvak 421
Cdd:COG4717 71 KELKELEEELKEAEEKE-----EEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELA--- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 422 DVSVRLHhELETVEEKRAKAEDDNETLRQQmievevsRQALQNEVERLREsslkrrgsremykEKKLVNQDDSADLKCQL 501
Cdd:COG4717 143 ELPERLE-ELEERLEELRELEEELEELEAE-------LAELQEELEELLE-------------QLSLATEEELQDLAEEL 201
|
170 180 190
....*....|....*....|....*....|...
gi 166235133 502 QFVKEEASLMRKKMAKLGREKDELEQELQKYKS 534
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-780 |
1.57e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDsyleedgyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAK 421
Cdd:COG1196 342 LEEELEEAEEELEEAEA--------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 422 DVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQL 501
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 502 QFVKEEASLMRKKMAKLGREKDELEQELqkyksLYGDVDSpLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELE 581
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRG-----LAGAVAV-LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 582 VENRGlKAEMEDIRVQHEREGTGRDHVPSTPTSPFgDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKF 661
Cdd:COG1196 568 AAKAG-RATFLPLDKIRARAALAAALARGAIGAAV-DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 662 KFEPHQEsgwlGDGVSKGPAASVPLQEELKSARLQIDELSGKVLKLQCENRLLLSNAQRGDLAAHLGLRAPSPRDSDAES 741
Cdd:COG1196 646 LREVTLE----GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
410 420 430
....*....|....*....|....*....|....*....
gi 166235133 742 DAGKKESDGEEGRLPQPKREGPVGGESDSEDMFEKTSGF 780
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
343-703 |
1.66e-03 |
|
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: 43.50 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 343 KDELDELR---AEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLkv 419
Cdd:TIGR00606 244 ENELDPLKnrlKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL-- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 420 akdvsVRLHHELETVEEKRakaeddnETLRQQMIEVEVSRQALQNEVERLRESSLKR-----------------RGS--- 479
Cdd:TIGR00606 322 -----VDCQRELEKLNKER-------RLLNQEKTELLVEQGRLQLQADRHQEHIRARdsliqslatrleldgfeRGPfse 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 480 -----------REMYKEKKLVNQDdSADLKCQLQFVKEEASLMRKKMAKLGR------EKDELEQELQKYKSLYG----- 537
Cdd:TIGR00606 390 rqiknfhtlviERQEDEAKTAAQL-CADLQSKERLKQEQADEIRDEKKGLGRtielkkEILEKKQEELKFVIKELqqleg 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 538 ------DVDSPLPTGEAGGPPSTREAE---LKLRLKLVEEEASILGRKIVELEVENRGLKAEME---------------- 592
Cdd:TIGR00606 469 ssdrilELDQELRKAERELSKAEKNSLtetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTtrtqmemltkdkmdkd 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 593 ----DIRVQHEREGTGRdhVPSTPTSP-FGDSMESsteLRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQ 667
Cdd:TIGR00606 549 eqirKIKSRHSDELTSL--LGYFPNKKqLEDWLHS---KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
410 420 430
....*....|....*....|....*....|....*...
gi 166235133 668 ESGWLGDGVSKGPAASV--PLQEELKSARLQIDELSGK 703
Cdd:TIGR00606 624 YEDKLFDVCGSQDEESDleRLKEEIEKSSKQRAMLAGA 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-466 |
1.77e-03 |
|
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: 43.52 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 338 ENDYLKDELDELRAEMEEMRDsylEEDGYQLQELRRELDRANkncriLQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL 417
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKR---ELDRLQEELQRLSEELAD-----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 166235133 418 KVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEV 466
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-551 |
1.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSY--LEEDGYQLQELrRELDRANKNCRILQYRLRKAEQKsLKVAETGQVDgelIRSLEQDLKv 419
Cdd:COG4913 622 LEEELAEAEERLEALEAELdaLQERREALQRL-AEYSWDEIDVASAEREIAELEAE-LERLDASSDD---LAALEEQLE- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 420 akdvsvRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLreSSLKRRGSREMYKEK-KLVNQDDSADlk 498
Cdd:COG4913 696 ------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERfAAALGDAVER-- 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 166235133 499 cqlQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGP 551
Cdd:COG4913 766 ---ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1104-1274 |
2.03e-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: 43.12 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 1104 QISEHGSRLQSsdggpLNKQVVENQQLFRALKALLEDFRSELREDEHARLRLQQQYASdkaawdvewavLKCRLEQLEEK 1183
Cdd:TIGR02168 268 KLEELRLEVSE-----LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-----------LEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 1184 TEKSLGELDSSAEGKGALKKEREVHQKLLADSHSLVMDLRWQIHHREKNWNREKVEL------LERLDSERQEWGRQKEE 1257
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqIASLNNEIERLEARLER 411
|
170
....*....|....*..
gi 166235133 1258 LLWRVEQLQKEKSPRRS 1274
Cdd:TIGR02168 412 LEDRRERLQQEIEELLK 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-595 |
2.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAE--QKSLKVAEtgqvdgELIRSLEQDLKv 419
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELE------KKLDELEEELA- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 420 akdvsvRLHHELEtvEEKRAKAEDDNETLRQ------QMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDD 493
Cdd:PRK03918 574 ------ELLKELE--ELGFESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 494 SADLK-CQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLygdvdsplptgeaggppstREaELKLRLKLVEEEASI 572
Cdd:PRK03918 646 RKELEeLEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR-------------------RE-EIKKTLEKLKEELEE 705
|
250 260
....*....|....*....|...
gi 166235133 573 LGRKIVELEVENRGLkAEMEDIR 595
Cdd:PRK03918 706 REKAKKELEKLEKAL-ERVEELR 727
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
342-470 |
2.61e-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: 42.53 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSYL--EEDGYQLQELRRELDRANKNCRILQYRLRKAEQ-------------KSLKVAETGQVD 406
Cdd:pfam06160 303 AEEQNKELKEELERVQQSYTlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayselqeeleeilEQLEEIEEEQEE 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 407 G-ELIRSLEQDLKVAKDVSVRLHHELETVeeKRaKAEDDN-----ETLRQQMIEVEVSRQALQNEVERLR 470
Cdd:pfam06160 383 FkESLQSLRKDELEAREKLDEFKLELREI--KR-LVEKSNlpglpESYLDYFFDVSDEIEDLADELNEVP 449
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
340-534 |
2.70e-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: 42.53 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 340 DYLKDELDELRAEMEEMrdsylEEDGYQL--QELRRELDRankncrilqyrLRKAEQKSLKVAETGQVDG--ELIRSLEQ 415
Cdd:pfam06160 207 TELPDQLEELKEGYREM-----EEEGYALehLNVDKEIQQ-----------LEEQLEENLALLENLELDEaeEALEEIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 416 DLKvakdvsvRLHHELETveEKRAKAE-DDN-ETLRQQMIEVEVSRQALQNEVERLRES-------------------SL 474
Cdd:pfam06160 271 RID-------QLYDLLEK--EVDAKKYvEKNlPEIEDYLEHAEEQNKELKEELERVQQSytlnenelervrglekqleEL 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166235133 475 KRR--GSREMYKEKKLVN---QDDSADLKCQLQFVKEEASLMRKKMAKLgrEKDELE--QELQKYKS 534
Cdd:pfam06160 342 EKRydEIVERLEEKEVAYselQEELEEILEQLEEIEEEQEEFKESLQSL--RKDELEarEKLDEFKL 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
341-585 |
3.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 341 YLKDELDELRAEMEEMRDsYLEEdgyQLQELRRELDRANKncRILQYRlrkAEQKSLKVAETGQVDGELIRSLEQDLkva 420
Cdd:COG3206 161 YLEQNLELRREEARKALE-FLEE---QLPELRKELEEAEA--ALEEFR---QKNGLVDLSEEAKLLLQQLSELESQL--- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 421 kdvsVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSrQALQNEVERLRESSLKRRGSREMYkekklvnQDDSADLKcQ 500
Cdd:COG3206 229 ----AEARAELAEAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARY-------TPNHPDVI-A 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 501 LQfvKEEASLMRKKMAKLGREKDELEQELQKYKSlygdvdsplptgeaggppstREAELKLRLKLVEEEASILGRKIVEL 580
Cdd:COG3206 296 LR--AQIAALRAQLQQEAQRILASLEAELEALQA--------------------REASLQAQLAQLEARLAELPELEAEL 353
|
....*
gi 166235133 581 EVENR 585
Cdd:COG3206 354 RRLER 358
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
383-485 |
3.16e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 40.79 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 383 RILQYRLRKAEQKSLKVAETGQVD-GELIRSLEQDLKVAKDVSVRLHHELET----VEEKRAKAED---DNETLRQQMIE 454
Cdd:pfam15035 24 KVLQYKKRCSELEQQLLEKTSELEkTELLLRKLTLEPRLQRLEREHSADLEEalirLEEERQRSESlsqVNSLLREQLEQ 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 166235133 455 VEVSRQALQNEVERL-------------RESSLKRRgsREMYKE 485
Cdd:pfam15035 104 ASRANEALREDLQKLtndwerareeleqKESEWRKE--EEAFNE 145
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
368-531 |
4.25e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 40.28 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 368 LQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ----VD-----------GELIRSLEQDLKVAKDVSVRLHHELE 432
Cdd:pfam13870 1 MRAKRNELSKLRLELITLKHTLAKIQEKLEQKEELGEgltmIDflqlqienqalNEKIEERNKELKRLKLKVTNTVHALT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 433 TVEEKRAKAEDDNETLRQQMIEvevsrqaLQNEVERLREsslkrrgsrEMYKEKKLVNQ--DDSADLKCQLQFV------ 504
Cdd:pfam13870 81 HLKEKLHFLSAELSRLKKELRE-------RQELLAKLRK---------ELYRVKLERDKlrKQNKKLRQQGGLLhvpall 144
|
170 180 190
....*....|....*....|....*....|...
gi 166235133 505 ------KEEASLMRKKMAKLGREKDELEQELQK 531
Cdd:pfam13870 145 hdydktKAEVEEKRKSVKKLRRKVKILEMRIKE 177
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
430-703 |
4.82e-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: 41.80 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 430 ELETVEEKRAKAEDDNETL----RQQMIEVEVSR-QALQNEVERLRESSLKRR-GSREMYKEKKLVNQDDSADLKCQLQF 503
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDMLlvvpRAELLQNRLEEcLQERAELLQAQEAANRQReKEKERYKRDREQWERQRRELESRVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 504 VKEEaslmrkkmakLGREKDELEQELQKYKSLygdVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEVE 583
Cdd:pfam07888 85 LKEE----------LRQSREKHEELEEKYKEL---SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 584 NRGLKAEMEDIRVQHEREGTGRDHVPSTPTSPFGDSMESSTE---LRRHLQFVEEEAELLRRSISEIED-----HNRQLT 655
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEfqeLRNSLAQRDTQVLQLQDTITTLTQklttaHRKEAE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 166235133 656 HELSKFKFEPHQE--------SGWLGDGVSKGPAASVPLQEELKSARLQIDELSGK 703
Cdd:pfam07888 232 NEALLEELRSLQErlnaserkVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
342-530 |
5.21e-03 |
|
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: 41.98 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 342 LKDELDELRAEMEEMRDSyLEEDGYQLQELRRELDRANKNCRILQyrlRKAEQKSLKVAETGQVDGELIRSLEQ------ 415
Cdd:TIGR02169 327 LEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKlkrein 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 416 DLKVAKDvsvRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLrESSLKRrgsremykekklvNQDDSA 495
Cdd:TIGR02169 403 ELKRELD---RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKLEQ-------------LAADLS 465
|
170 180 190
....*....|....*....|....*....|....*
gi 166235133 496 DLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQ 530
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1120-1273 |
5.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 1120 LNKQVVENQQLFRALKALLEDFRSELREDEHARLRLQQQYA---SDKAAWDVEWAVLKCRLEQLEEKTEKSLGELDSSAE 1196
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166235133 1197 GKGALKKEREVHQKLLADSHSLVMDLRWQIHHREKNWNREKVELLERLDSERQEWGRQKEELLWRVEQLQKEKSPRR 1273
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
336-661 |
6.01e-03 |
|
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: 41.54 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 336 RSENDYLKDELDELRAEMEEmrdsyLEEDGYQLQELRRELDRANKNCRIlQYRLRKAEQKSLKVAETGQvdGELIRSLEQ 415
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQIND-----LESKIQNQEKLNQQKDEQIKKLQQ-EKELLEKEIERLKETIIKN--NSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 416 DlKVAKDVSVR--------LHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRE--SSLKRRGSREMYKE 485
Cdd:TIGR04523 448 Q-DSVKELIIKnldntresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkvKDLTKKISSLKEKI 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 486 KKL---VNQDDS--ADLKCQLQFVKEEaslmrKKMAKLGREKDELEQELQKYKSLYGDVDSplptgeaggppstREAELK 560
Cdd:TIGR04523 527 EKLeseKKEKESkiSDLEDELNKDDFE-----LKKENLEKEIDEKNKEIEELKQTQKSLKK-------------KQEEKQ 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 561 LRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTGRDHVPStptspfgdsmeSSTELRRHLQFVEEEAELL 640
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS-----------KKNKLKQEVKQIKETIKEI 657
|
330 340
....*....|....*....|.
gi 166235133 641 RRSISEIEDHNRQLTHELSKF 661
Cdd:TIGR04523 658 RNKWPEIIKKIKESKTKIDDI 678
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
300-660 |
6.17e-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: 41.42 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 300 PERTILGTSKEPSLGEQPRLLVVAEEEELLREMEELRSENDylKDELDELRAEMEEmRDSYLEEDGYQLQELRRELDRAN 379
Cdd:pfam07888 27 PRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD--REQWERQRRELES-RVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 380 KNCRILQYRLRKAEQKSLKVAETGQVdgeLIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEddnetlrQQMIEVEVSR 459
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAAHEA---RIRELEEDIKTLTQRVLERETELERMKERAKKAG-------AQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 460 QALQNEVERLRESSlkRRGSREMYKEKKLVNQDDSadlkcQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDV 539
Cdd:pfam07888 174 KQLQAKLQQTEEEL--RSLSKEFQELRNSLAQRDT-----QVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 540 DSPLPTGEA--------GGPPSTREAEL---------------KLRLKLVEEEASILG-----RKIVELEVEN-RGLKAE 590
Cdd:pfam07888 247 NASERKVEGlgeelssmAAQRDRTQAELhqarlqaaqltlqlaDASLALREGRARWAQeretlQQSAEADKDRiEKLSAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 591 MEDI--RVQHERE---------GTGRDhvpsTPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELS 659
Cdd:pfam07888 327 LQRLeeRLQEERMereklevelGREKD----CNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
.
gi 166235133 660 K 660
Cdd:pfam07888 403 T 403
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
343-524 |
6.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 343 KDELDELRAEmEEMRDSYLEEDGYQLQELRR--ELDRANKNCRIlqyrlRKAEQKslKVAETGQVDGELIRSLEQDLKVA 420
Cdd:PTZ00121 1619 KIKAEELKKA-EEEKKKVEQLKKKEAEEKKKaeELKKAEEENKI-----KAAEEA--KKAEEDKKKAEEAKKAEEDEKKA 1690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 421 KDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQ 500
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
170 180
....*....|....*....|....
gi 166235133 501 LQFVKEEASLMRKKMaklgREKDE 524
Cdd:PTZ00121 1771 EEIRKEKEAVIEEEL----DEEDE 1790
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
337-704 |
6.43e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 337 SENDYLKDELDELRAEMEE-----MRDSYLEEDGYQLQE--LRRELDRANkncrilqYRLRKAEQKSlKVAETGQVDGEL 409
Cdd:pfam05622 35 QENKKLQERLDQLESGDDSgtpggKKYLLLQKQLEQLQEenFRLETARDD-------YRIKCEELEK-EVLELQHRNEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 410 ------IRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERlrESSLKR----RGS 479
Cdd:pfam05622 107 tslaeeAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQL--EEELKKanalRGQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 480 REMYKEK--KLVNQDDSADLKC-QLQFvkeEASLMRKKMAKLGREKD----------ELEQELQKYKSLYGDVDSPLPTG 546
Cdd:pfam05622 185 LETYKRQvqELHGKLSEESKKAdKLEF---EYKKLEEKLEALQKEKErliierdtlrETNEELRCAQLQQAELSQADALL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 547 EAGGPPSTREAELKLRLKLVEeeasilgrKIVELEVENRGLKAEmedirvqheREGTGRDHVPSTpTSPFGDSMESSTEL 626
Cdd:pfam05622 262 SPSSDPGDNLAAEIMPAEIRE--------KLIRLQHENKMLRLG---------QEGSYRERLTEL-QQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 627 RrhlqfveEEAELLRRSISEIEDHNRQLTHELS------------KFKFEPHQESgwLGDgvskgpaasvpLQEELKSAR 694
Cdd:pfam05622 324 E-------TQNRLANQRILELQQQVEELQKALQeqgskaedssllKQKLEEHLEK--LHE-----------AQSELQKKK 383
|
410
....*....|
gi 166235133 695 LQIDELSGKV 704
Cdd:pfam05622 384 EQIEELEPKQ 393
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
55-318 |
7.12e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 55 RPATATPSAGRAPTPAAPRSPSLAGKAPPSPGPPAAPGRLS-RRSGVVPGAKDKPPPGAGARSAGGAKAVPGTRRAARAG 133
Cdd:PHA03307 21 FPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAAcDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 134 PAEPLSRVGRPTGAEPPPAVAKgrktkrgPGTPPARAvvPPARASRVPAVtlsvtsvagcrinhtdSSSDLSDCASEPLS 213
Cdd:PHA03307 101 AREGSPTPPGPSSPDPPPPTPP-------PASPPPSP--APDLSEMLRPV----------------GSPGPPPAASPPAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 214 DEQRllPAASSDAESGTGSSDREPIRGAPTPSSGSRGPPPGSPEPPILLAAPPvasaclGGRSSPGGASTGSPGPGSQED 293
Cdd:PHA03307 156 GASP--AAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRP------PRRSSPISASASSPAPAPGRS 227
|
250 260
....*....|....*....|....*
gi 166235133 294 VGGRAPPERTILGTSKEPSLGEQPR 318
Cdd:PHA03307 228 AADDAGASSSDSSSSESSGCGWGPE 252
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
7-175 |
8.51e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.21 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 7 PAGGGAPDTKPQPAGQHHRHHHLHPlaerRRLHRAPSPARP-FLKDLHTRPATATPSAgRAPTPAAP--------RSPSL 77
Cdd:PHA03378 645 VLVFPTPHQPPQVEITPYKPTWTQI----GHIPYQPSPTGAnTMLPIQWAPGTMQPPP-RAPTPMRPpaappgraQRPAA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 78 AGKAPPSPGPPAAPgrlSRRSGVVPGAKdkPPPGAGARSAGGAKAVPGTRRAARAGPaeplsrvGRPTGAEPPPAVAKGR 157
Cdd:PHA03378 720 ATGRARPPAAAPGR---ARPPAAAPGRA--RPPAAAPGRARPPAAAPGRARPPAAAP-------GAPTPQPPPQAPPAPQ 787
|
170
....*....|....*...
gi 166235133 158 KTKRGPGTPPARAVVPPA 175
Cdd:PHA03378 788 QRPRGAPTPQPPPQAGPT 805
|
|
| PTZ00436 |
PTZ00436 |
60S ribosomal protein L19-like protein; Provisional |
57-181 |
9.04e-03 |
|
60S ribosomal protein L19-like protein; Provisional
Pssm-ID: 185616 [Multi-domain] Cd Length: 357 Bit Score: 40.70 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 57 ATATPSAGRAPTPAAPRSPSLAGKAPPSPGPPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGTRRAARAGPAE 136
Cdd:PTZ00436 225 AAAAPAKAAAPPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAA 304
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 166235133 137 PLSRVGR-PTGAEPPPAVAKGRKTKrgPGTPPARAVVPPARASRVP 181
Cdd:PTZ00436 305 APAKAAAaPAKAAAPPAKAAAPPAK--AATPPAKAAAPPAKAAAAP 348
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
49-182 |
9.21e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.01 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166235133 49 LKDLHTRPATATPSAGRAPTPAAPRSpslAGKAPPSPGPPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGTRR 128
Cdd:PRK12323 358 LRMLAFRPGQSGGGAGPATAAAAPVA---QPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALA 434
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 166235133 129 AARAGPAEPLSRVGRPTGAEPPPAVAKGRKTKRGPGTPPARAVVPPARASRVPA 182
Cdd:PRK12323 435 AARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAA 488
|
|
| |
