|
Name |
Accession |
Description |
Interval |
E-value |
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
596-636 |
1.26e-13 |
|
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.
Pssm-ID: 462805 [Multi-domain] Cd Length: 41 Bit Score: 65.05 E-value: 1.26e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 28195388 596 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 636
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-621 |
6.43e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 338 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHRE----------- 406
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 407 --AYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 481
Cdd:TIGR02168 767 eeRLEEAEEELAEaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 482 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 558
Cdd:TIGR02168 847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28195388 559 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 621
Cdd:TIGR02168 923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-616 |
1.51e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 339 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 418
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 419 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 498
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 499 LIEDLRKELEHLQMykldcerpgrgrsassglGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLyEAKNL 578
Cdd:COG1196 380 ELEELAEELLEALR------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEE 440
|
250 260 270
....*....|....*....|....*....|....*...
gi 28195388 579 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 616
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
369-511 |
2.39e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 369 KQENTQLVHRVHELEEMVKD-----QETTAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTRL 443
Cdd:COG4717 87 EEEYAELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEEL 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28195388 444 KSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 511
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-511 |
3.44e-08 |
|
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: 56.99 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 338 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQET--TAEQALEEEARRHREAYGKLEREK 415
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEEL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 416 ATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD-EMDLYKRMMDKLRQNRLEFQKERE 494
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457
|
170
....*....|....*..
gi 28195388 495 ATQELIEDLRKELEHLQ 511
Cdd:TIGR02168 458 RLEEALEELREELEEAE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-615 |
8.88e-08 |
|
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: 55.45 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 342 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREAYGKLEREK 415
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 416 atevELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 495
Cdd:TIGR02168 319 ----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 496 TQELIEDLRKELEhlqmykldcerpgrgrsassglgefNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE- 574
Cdd:TIGR02168 391 LELQIASLNNEIE-------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEl 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 28195388 575 -------AKNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 615
Cdd:TIGR02168 446 eeeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-610 |
1.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 363 DLKSKLKQENTQLVHRVHELEEMVKDqettAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTR 442
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 443 LKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNRLEFQKE-REATQEL------IEDLRKELEHLQMYK 514
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARlREIEQKLnrltleKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 515 LDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSlyeaKNLFAAQTKAQSLAAEIDT 594
Cdd:TIGR02169 843 IDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE----AQLRELERKIEELEAQIEK 914
|
250
....*....|....*.
gi 28195388 595 AsrDELMEALKEQEEI 610
Cdd:TIGR02169 915 K--RKRLSELKAKLEA 928
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
339-612 |
1.49e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 339 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 417
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 418 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 495
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 496 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 575
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 28195388 576 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 612
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
331-506 |
2.23e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 331 DSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ------ALEEEARRH 404
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgDLKKERDEL 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 405 REAYGKLEREK---ATEVEL-------LNARVQQLEEENTELRTTVTRLKSQT------EKLDEERQRMSDR---LEDTS 465
Cdd:TIGR02169 895 EAQLRELERKIeelEAQIEKkrkrlseLKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEiraLEPVN 974
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 28195388 466 LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 506
Cdd:TIGR02169 975 MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
341-508 |
5.09e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 341 TEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAE-QALEEEARRHREAYGKLEREKAT-- 417
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 418 ----EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEM--DLYKR----MMDKLRQN-R 486
Cdd:COG4913 689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERElR 768
|
170 180
....*....|....*....|..
gi 28195388 487 LEFQKEREATQELIEDLRKELE 508
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELE 790
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
382-516 |
7.26e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 382 LEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRl 461
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28195388 462 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRKELEHL-QMYKLD 516
Cdd:COG2433 457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-621 |
7.38e-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: 52.75 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 381 ELEEMVKDQETTAEQalEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 460
Cdd:TIGR02168 233 RLEELREELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 461 ---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCER----------PGRGRSAS 527
Cdd:TIGR02168 311 lanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqleTLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 528 SGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQ 607
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250
....*....|....
gi 28195388 608 EEINFRLRQYMDKI 621
Cdd:TIGR02168 471 EEAEQALDAAEREL 484
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
350-512 |
1.01e-06 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 50.79 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 350 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 424
Cdd:pfam04849 97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 425 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 499
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239
|
170
....*....|...
gi 28195388 500 IEDLRKELEHLQM 512
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-616 |
1.05e-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: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 367 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRL 443
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 444 KSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRG 523
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRD----KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK------REINEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 524 RSASSGLGEFNARARE--VELEHEVKRLKQENYKLRDQNDDLngqilslslyeAKNLFAAQTKAQSLAAEIDTAsRDELM 601
Cdd:TIGR02169 405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDK-----------ALEIKKQEWKLEQLAADLSKY-EQELY 472
|
250
....*....|....*
gi 28195388 602 EALKEQEEINFRLRQ 616
Cdd:TIGR02169 473 DLKEEYDRVEKELSK 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-511 |
1.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 380 HELEEmVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD 459
Cdd:COG4913 302 AELAR-LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 28195388 460 RLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 511
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
347-591 |
1.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 347 LEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARV 426
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 427 QQLEEENTELRTTVTRLKSQTEKLDEERQRmsDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 506
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQL--EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 507 LEHLQmykldcerpgrgrsassgLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSL-SLYEAKNLFAAQTKA 585
Cdd:COG1196 451 EAELE------------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLlEAEADYEGFLEGVKA 512
|
....*.
gi 28195388 586 QSLAAE 591
Cdd:COG1196 513 ALLLAG 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-511 |
2.34e-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: 50.15 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 330 RDSIDSCDNDITEKVSFLEKKVTELEND-SLTNGDLKS---KLKQENTQLVHRVHELEEMVKDQETTAEQALEE------ 399
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQElAALEAELAElekEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 400 ---EARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 476
Cdd:COG4942 130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 28195388 477 RMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 511
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
393-609 |
4.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 393 AEQAL------EEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTS- 465
Cdd:COG1196 209 AEKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 466 ---------LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgrgrsASSGLGEFNAR 536
Cdd:COG1196 289 eeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--------------EELEEAEEELE 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28195388 537 AREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEE 609
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
342-511 |
7.24e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 342 EKVSfLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ-----------ALEEEARRHREAYGK 410
Cdd:pfam01576 125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknkheamISDLEERLKKEEKGR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 411 LEREKATevellnarvQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR------- 483
Cdd:pfam01576 204 QELEKAK---------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIReleaqis 274
|
170 180 190
....*....|....*....|....*....|.
gi 28195388 484 --QNRLEFQK-EREATQELIEDLRKELEHLQ 511
Cdd:pfam01576 275 elQEDLESERaARNKAEKQRRDLGEELEALK 305
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
365-559 |
1.32e-05 |
|
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: 48.20 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 365 KSKLKQENTQ--LVHRVHELEEMVKDQETTAE---QALEEEARRHREAYGKLEREKATEVEllnaRVQQLEEENTELRTT 439
Cdd:pfam17380 403 KVKILEEERQrkIQQQKVEMEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 440 VTRLKSQTEKLDEERQRMsdrledtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQELI--EDLRKELEHLQMYKLDC 517
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKI----------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEM 548
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 28195388 518 ERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQ 559
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-574 |
1.62e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 394 EQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD-------------- 459
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreeleklekllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 460 -----RLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRKELEHLQMyKLDCERPGRGRSASSGLGEfn 534
Cdd:COG4717 128 lplyqELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEELEE-- 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 28195388 535 ARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE 574
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
369-634 |
1.84e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 369 KQENTQLVHRVHELEEMVKDQET-TAEQALEEEARRHR-----EAYGKLEREKATEVELLNARVQQLEEENTELRTTVTR 442
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKkKAEEAKKAEEDKNMalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 443 LKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLyKRMMDKLRQNRLEFQKEREATQELIEDLRKELEH----LQMYKLDCE 518
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 519 RPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRD 598
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
250 260 270
....*....|....*....|....*....|....*.
gi 28195388 599 ELMEALKEQEEinfRLRQYMDKIILAILDHNPSILE 634
Cdd:PTZ00121 1780 VIEEELDEEDE---KRRMEVDKKIKDIFDNFANIIE 1812
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
287-621 |
2.69e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 287 LEARLKNLKANSPNRKISSTAFGRQLMHSSNFSSSNGSTEDLFRDSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKS 366
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 367 KLKQENTQL-VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKS 445
Cdd:pfam02463 768 ELSLKEKELaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 446 QtEKLDEERQRMSDRlEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpgrgrs 525
Cdd:pfam02463 848 L-EKLAEEELERLEE-EITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK----------------- 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 526 assglgEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEAL- 604
Cdd:pfam02463 909 ------LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEe 982
|
330
....*....|....*....
gi 28195388 605 --KEQEEINFRLRQYMDKI 621
Cdd:pfam02463 983 feEKEERYNKDELEKERLE 1001
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
347-508 |
3.38e-05 |
|
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: 46.94 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 347 LEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEqALEEEARRHREAYGKLERE---KATEVELLN 423
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKIKQNLEQKQKElksKEKELKKLN 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 424 ARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLED------------TSLRLKDEMDLYKRMMDKLRQNRLEFQK 491
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
170 180
....*....|....*....|....
gi 28195388 492 EREATQELIE-------DLRKELE 508
Cdd:TIGR04523 583 KQEEKQELIDqkekekkDLIKEIE 606
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
395-611 |
3.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 395 QALEEEARRHREAYGKLEREKATEVELLNA--RVQQLEEENTELRTTVTRLksqtEKLDEERQRM---SDRLEdtslRLK 469
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREI----AELEAELERLdasSDDLA----ALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 470 DEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASsglgEFNARAREVELEHEVKRL 549
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28195388 550 KQEnykLRDQNDDLNGQILSLS--LYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEIN 611
Cdd:COG4913 768 REN---LEERIDALRARLNRAEeeLERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-590 |
3.66e-05 |
|
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: 46.30 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 363 DLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEArrhreaygKLEREKATEVELLNARVQQLEEENTELRTTVTR 442
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 443 LKSQTEKLDEERQRMSDRL---------------------EDTSLRL----------KDEMDLYKRMMDKLRQNRLEFQK 491
Cdd:COG4942 92 IAELRAELEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLqylkylaparREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 492 EREATQELIEDLRKELEHLQMYKldcerpgrgrsassglgefNARAREV-ELEHEVKRLKQENYKLRDQNDDLNGQILSL 570
Cdd:COG4942 172 ERAELEALLAELEEERAALEALK-------------------AERQKLLaRLEKELAELAAELAELQQEAEELEALIARL 232
|
250 260
....*....|....*....|
gi 28195388 571 SLYEAKNlfAAQTKAQSLAA 590
Cdd:COG4942 233 EAEAAAA--AERTPAAGFAA 250
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
353-612 |
4.37e-05 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 46.60 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 353 ELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKA------------TEVE 420
Cdd:COG5244 394 EDNKDVTLILKILHPILETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQdnrlflypscdiTLSS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 421 LLNARVQ-------QLEEENTELRTTVTRLKSQTEKLDE---ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRL--E 488
Cdd:COG5244 474 ILTILFSdklevffQGIESLLENITIFPEQPSQQTSDSEnikENSLLSDRLNEENIRLKEVLVQKENMLTEETKIKIiiG 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 489 FQKEREATQELIEDLRKELEHLQMyKLDCERPgrgrsassglgefnararevELEHEVKRLKQENYKLRDQNdDLNGQIL 568
Cdd:COG5244 554 RDLERKTLEENIKTLKVELNNKNN-KLKEENF--------------------NLVNRLKNMELKLYQIKDNN-TLNKIYL 611
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 28195388 569 SL--SLYEAKNLFAAQTKAQsLAAEIDTASRDELMEALKE--QEEINF 612
Cdd:COG5244 612 DLvsEIMELRETIRRQIKEQ-KRVSIDFSWLDELKQPFKEhiIEMFNF 658
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
399-615 |
5.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 399 EEARRHREAYGKLEREKATEVELLNARVQQLEEEN-----TELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL----- 468
Cdd:PRK02224 169 ERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeehee 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 469 -KDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLqmykldcERPGRGRSASSGLGEFNARA---REVELEH 544
Cdd:PRK02224 249 rREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAveaRREELED 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28195388 545 EVKRLKQENYKLRDQNDDLNGQILSLsLYEAKNLFAAQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 615
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
369-508 |
6.19e-05 |
|
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: 46.27 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 369 KQENTQLVHRVHELEEMVKDQETTAEQALEE-EARRHreaYGKLEREKATEVELLNARVQQLEEENTELRttvtrlKSQT 447
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQElEAARK---VKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREV 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28195388 448 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELE 508
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
379-607 |
6.29e-05 |
|
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: 46.27 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 379 VHELEEMVKDQETTAEQALEEEARRHREAYGKLERE-KATEVEllnaRVQQLEEENTELRTTVTR---LKSQTEKLDEER 454
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEeKAREVE----RRRKLEEAEKARQAEMDRqaaIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 455 QRMSDRLedtslRLKDEmdlyKRMMDKLRQNRL--EFQKERE------ATQELIEDLRKELEHLQMYKLDCERPGRGRSA 526
Cdd:pfam17380 347 ERELERI-----RQEER----KRELERIRQEEIamEISRMRElerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 527 SSGLGEF------NARAREV-----ELEHEVKRLKQENY-------KLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSL 588
Cdd:pfam17380 418 QKVEMEQiraeqeEARQREVrrleeERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
250
....*....|....*....
gi 28195388 589 AAEIDTASRDELMEALKEQ 607
Cdd:pfam17380 498 EKELEERKQAMIEEERKRK 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
378-552 |
8.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 378 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEReKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 457
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 458 SDRLEDTSLRLKDEMdlyKRMMDKLRQNRLEFQKEREATQELIEDL-------RKELEHLQmyKLDCERPGRGRSASSGL 530
Cdd:COG4913 329 EAQIRGNGGDRLEQL---EREIERLERELEERERRRARLEALLAALglplpasAEEFAALR--AEAAALLEALEEELEAL 403
|
170 180
....*....|....*....|....
gi 28195388 531 GE--FNARAREVELEHEVKRLKQE 552
Cdd:COG4913 404 EEalAEAEAALRDLRRELRELEAE 427
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-481 |
1.22e-04 |
|
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: 44.15 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 339 DITEKVSFLEKKVTELENDSltnGDLKSKLKQENTQL--VHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 414
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRriSDLEDEILELMERIEELEEE 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28195388 415 KATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEdtslrlKDEMDLYKRMMDK 481
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP------PELLALYERIRKR 186
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
368-519 |
1.56e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 368 LKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQT 447
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28195388 448 EKLDEERQRMSDRLEdtslrlkdemdlykrmmdklrqnRLEFQKEREATQELIEDLRKELEH--LQMYKLDCER 519
Cdd:PRK12705 119 LELEELEKQLDNELY-----------------------RVAGLTPEQARKLLLKLLDAELEEekAQRVKKIEEE 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
340-557 |
1.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 340 ITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQA-----LEEEARRHREAYGKLERE 414
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyikLSEFYEEYLDELREIEKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 415 KAT-------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMsDRLEDTSLRLKD-EMDLYKRMMD 480
Cdd:PRK03918 316 LSRleeeingieerikELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLTGlTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 481 KLRQNRLEFQKE-REATQEL------IEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVE-LEHEVKRLKQE 552
Cdd:PRK03918 395 ELEKAKEEIEEEiSKITARIgelkkeIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKrIEKELKEIEEK 474
|
....*
gi 28195388 553 NYKLR 557
Cdd:PRK03918 475 ERKLR 479
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
341-578 |
1.70e-04 |
|
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: 44.63 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 341 TEKVSFLEKKVTELENdslTNGDLKSKLKQENTQLVHRVHELEEmVKDQETTAEQALEEEARrhreaygKLErEKATEVE 420
Cdd:TIGR04523 210 IQKNKSLESQISELKK---QNNQLKDNIEKKQQEINEKTTEISN-TQTQLNQLKDEQNKIKK-------QLS-EKQKELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 421 LLNARVQQLEEENTELRTTVTRLKSQTE-----KLDEERQRMSDRLEDTSL----------RLKDEMDLYKRMMDKLRQN 485
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNqisqnnkiisQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 486 RLEFQKEREATQELIEDLRKE-------LEHLQMYKLDCERPGRGRSASSGLGEFNARAREVE---LEHEVKRLKQENYK 555
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEkelLEKEIERLKETIIK 437
|
250 260
....*....|....*....|...
gi 28195388 556 LRDQNDDLNGQILSLSLyEAKNL 578
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKEL-IIKNL 459
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
342-473 |
2.18e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 41.91 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 342 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALeeearrhreaygklerEKATEVEL 421
Cdd:pfam12718 14 ERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESE----------------KLKTNNEN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28195388 422 LNARVQQLEEE----NTELRTTVTRLKsQTEKLDEERQRMSDRLEDTSLRLKDEMD 473
Cdd:pfam12718 78 LTRKIQLLEEEleesDKRLKETTEKLR-ETDVKAEHLERKVQALEQERDEWEKKYE 132
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
20-78 |
2.27e-04 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 39.54 E-value: 2.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28195388 20 RLREVFEVCGRDPDGFLRVERVAALGLRFGQG-----EEVEKLVKYLDPNDLGRINFKDFCRGV 78
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGeplsdEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
394-621 |
2.30e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 394 EQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSdRLEDTSLRLKDEMD 473
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK-ELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 474 LYKRMMDKLRQNRLEFQKEREAtqelIEDLRKELEHL----QMYKLDCERPGRGRSASSGLGE-FNARAREVELEHEVKR 548
Cdd:COG1340 89 ELREELDELRKELAELNKAGGS----IDKLRKEIERLewrqQTEVLSPEEEKELVEKIKELEKeLEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 549 LKQENYKLRDQNDDLNGQILSLS--LYEAKNLFAAQ-TKAQSLAAEIDTASR--DELMEALKEQE----EINFRLRQYMD 619
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAeeAQELHEEMIELyKEADELRKEADELHKeiVEAQEKADELHeeiiELQKELRELRK 244
|
..
gi 28195388 620 KI 621
Cdd:COG1340 245 EL 246
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
345-509 |
2.59e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 345 SFLEKKVTELENDSltngdlKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNA 424
Cdd:PRK12704 27 KIAEAKIKEAEEEA------KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 425 RVQQLEEENTELRTTVTRLKSQTEKLDEERQRmsdrledtslrlkdemdlYKRMMDKLRQnRLE----FQKErEATQELI 500
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEE------------------LEELIEEQLQ-ELErisgLTAE-EAKEILL 160
|
....*....
gi 28195388 501 EDLRKELEH 509
Cdd:PRK12704 161 EKVEEEARH 169
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
370-624 |
3.09e-04 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 43.82 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 370 QENTQLVHRVHELEEMVKDQETTAEQALEEEARRhreaygklerekaTEVELLNARVQQLEEENT----ELRTTVTRLKS 445
Cdd:PRK10361 26 QHAQQKAEQLAEREEMVAELSAAKQQITQSEHWR-------------AECELLNNEVRSLQSINTsleaDLREVTTRMEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 446 -QTEKLDEERQRMSdrledTSLRLKDEMD-LYKRMMDKlrQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpGRG 523
Cdd:PRK10361 93 aQQHADDKIRQMIN-----SEQRLSEQFEnLANRIFEH--SNRRVDEQNRQSLNSLLSPLREQLD------------GFR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 524 RSASSGLGEfNARAREVeLEHEVKRLKQENYKLRDQNDDLN-------------GQILSLSLYEAKNLFAAQTKAQSLAA 590
Cdd:PRK10361 154 RQVQDSFGK-EAQERHT-LAHEIRNLQQLNAQMAQEAINLTralkgdnktqgnwGEVVLTRVLEASGLREGYEYETQVSI 231
|
250 260 270
....*....|....*....|....*....|....
gi 28195388 591 EIDTASRdelmealkEQEEINFRLRQYMDKIILA 624
Cdd:PRK10361 232 ENDARSR--------MQPDVIVRLPQGKDVVIDA 257
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
376-487 |
3.13e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 376 VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLERE---KATEVELLnarvQQLEEENTELRTTVTRLKSQTEKLDE 452
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlHAEDIKAL----QALREELNELKAEIAELKAEAESAKA 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 28195388 453 ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR-QNRL 487
Cdd:pfam07926 86 ELEESEESWEEQKKELEKELSELEKRIEDLNeQNKL 121
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
412-612 |
3.37e-04 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 43.06 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 412 EREKATEVELLNARVQQLEEENTElrtTVTRLKSQTEKLDEERQRMSDRLE-----------DTSLRLKDEMDLYKRMMD 480
Cdd:NF033928 100 KRGDLTEEELSELPPIPLSSDDKE---IVKELKEILEDLKNDIKDYQQKADdvkkelddfenDLREELLPQLKLKKKLYD 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 481 KLRQNrlefqKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEF-----------NARAREVELEHEVKRL 549
Cdd:NF033928 177 DNLGS-----DSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTGLAGGPIGLAitggifgskaeKIRKEKNALIQEIDEL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28195388 550 KQenyKLRDQN------DDLNGQILSLSLYEAKNLFAAQTKA---QSLAAEIDtASRDELMEALKEQEEINF 612
Cdd:NF033928 252 QE---QLKKKNallgslERLQTSLDDILTRMEDALPALKKLKgvwQSLLTDID-SSINALKEIDDADSLRLF 319
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
331-567 |
5.16e-04 |
|
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: 43.09 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 331 DSIDSCDNDITEKVSFLEKKVTELENDSL----TNGDLKSKL-------------KQENTQLVHRVHELEEMVKDQETTA 393
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLniqkNIDKIKNKLlklelllsnlkkkIQKNKSLESQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 394 EQ------ALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENT---ELRTTVTRLKSQTEKLDEERQrmsdrlEDT 464
Cdd:TIGR04523 235 EKkqqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLNNQKE------QDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 465 SLRLKDEMdlyKRMMDKLRQNRLEFQKEREATQEL---IEDLRKELEHLQMYKLDCERpgrgrsassglgEFNARAREVE 541
Cdd:TIGR04523 309 NKELKSEL---KNQEKKLEEIQNQISQNNKIISQLneqISQLKKELTNSESENSEKQR------------ELEEKQNEIE 373
|
250 260
....*....|....*....|....*..
gi 28195388 542 -LEHEVKRLKQENYKLRDQNDDLNGQI 567
Cdd:TIGR04523 374 kLKKENQSYKQEIKNLESQINDLESKI 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
413-616 |
7.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 413 REKATEVelLNARVQQLEEENTELRTTVTRlkSQTEKLDEERQRMSDRLEDTSLRLKD------------EMDLYKRMMD 480
Cdd:COG3206 147 PELAAAV--ANALAEAYLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 481 KLRQNRLEFQKEREATQELIEDLRKELehlqmykldcerpGRGRSASSGLGE----FNARAREVELEHEVKRLKQ---EN 553
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQL-------------GSGPDALPELLQspviQQLRAQLAELEAELAELSArytPN 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28195388 554 Y----KLRDQNDDLNGQILSLSlyeAKNLFAAQTKAQSLAAEIDT--ASRDELMEALKEQEEINFRLRQ 616
Cdd:COG3206 290 HpdviALRAQIAALRAQLQQEA---QRILASLEAELEALQAREASlqAQLAQLEARLAELPELEAELRR 355
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-609 |
7.53e-04 |
|
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: 42.70 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 275 SQCCKKINLLNDLEARLKNLKANSPNRKISStafgrqlmhssnfsssngstedlfrdsidscDNDITEKVSFLEKkvTEL 354
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSESENSEK-------------------------------QRELEEKQNEIEK--LKK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 355 ENDSltngdlkskLKQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREK---ATEVELLNARVQQLEE 431
Cdd:TIGR04523 378 ENQS---------YKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEIerlKETIIKNNSEIKDLTN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 432 ENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD---EMDLYKRMMDKL-RQNRLEFQKEREATQElIEDLRKEL 507
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLnEEKKELEEKVKDLTKK-ISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 508 EHLQMYKLDCERpgrgrsassglgefnaraREVELEHEVKRLKQENYK--LRDQNDDLNGQILSLSLyEAKNLFAAQTKA 585
Cdd:TIGR04523 527 EKLESEKKEKES------------------KISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQ-TQKSLKKKQEEK 587
|
330 340
....*....|....*....|....
gi 28195388 586 QSLAAEIDtasrDELMEALKEQEE 609
Cdd:TIGR04523 588 QELIDQKE----KEKKDLIKEIEE 607
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
374-506 |
7.69e-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: 42.82 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 374 QLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLerekATEVELLNARVQQLEEENTELRTTVTRLK-----SQTE 448
Cdd:pfam07111 506 QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASV----GQQLEVARQGQQESTEEAASLRQELTQQQeiygqALQE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28195388 449 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQE---LIEDLRKE 506
Cdd:pfam07111 582 KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQElrrLQDEARKE 642
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
369-572 |
8.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 369 KQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYgkLEREKATEVELLNARVQQLEEENtELRTTVTRLKSQTE 448
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 449 KLDEERQRMSDRLEDTSLRLKDEmdlykrmmdklrqnrlEFQKEREATQELIEDLRKElehlqmykldcerpgrgrsass 528
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELE----------------ELEEELEELEEELEELREE---------------------- 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 28195388 529 gLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSL 572
Cdd:COG4717 455 -LAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
395-511 |
9.12e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 395 QALEEEARRHREAYGKLEREKATE-----VELLNARVQQLEEENTELRTTVTRLKSQTEK----LDEERQRMSDRLEDTS 465
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKdqtaLETLEKALKDLLTDEG 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 28195388 466 LRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRKELEHLQ 511
Cdd:cd22656 174 GAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
395-511 |
9.27e-04 |
|
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: 41.45 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 395 QALEEEARRHREAYGKLEREkatevellnarVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD---- 470
Cdd:COG1579 13 QELDSELDRLEHRLKELPAE-----------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeq 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28195388 471 ---------------EMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 511
Cdd:COG1579 82 lgnvrnnkeyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-460 |
1.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 347 LEKKVTELENDSLTN-GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNAR 425
Cdd:COG4913 321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAA-LGLPLPASAEEFAALRAEAAALLEALEEE 399
|
90 100 110
....*....|....*....|....*....|....*
gi 28195388 426 VQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 460
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
337-510 |
1.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 337 DNDITEKVSFLEKKVTELENDSltngdlkSKLKQENTQLVHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 414
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLEEHEERREelETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 415 KAT---EVELLNARVQQLEEENTELRTTV-------TRLKSQTEKLDEERQRMSDRLEDTSL----------RLKDEMDL 474
Cdd:PRK02224 274 REElaeEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVaaqahneeaeSLREDADD 353
|
170 180 190
....*....|....*....|....*....|....*.
gi 28195388 475 YKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHL 510
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
338-628 |
1.19e-03 |
|
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: 42.02 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 338 NDITEKVSFLEKKVTELENDSLTNGDlKSKLKQENTQLVHRVHELEEmvKDQETTAE-QALEEEARR---HREAYGKLER 413
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIAEELKG--KEQELIFLlQAREKEIHDleiQLTAIKTSEE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 414 EKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRL----EDTSLRLKDEMDLYKRmMDKLRQNRLEF 489
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELkkhqEDIINCKKQEERMLKQ-IENLEEKEMNL 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 490 QKEREATQELIEDLRKELE------HLQMYKLDCERPGRGRSASSGLGEFNARAREVELEHE-VKRLKQENYKLRDQNDD 562
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKckldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnIEELHQENKALKKKGSA 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 563 LNGQI---------LSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELM-----------EALKEQEEINFRLRQYMDKII 622
Cdd:pfam05483 627 ENKQLnayeikvnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakaiadEAVKLQKEIDKRCQHKIAEMV 706
|
....*.
gi 28195388 623 LAILDH 628
Cdd:pfam05483 707 ALMEKH 712
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
377-473 |
1.53e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 39.52 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 377 HRVHELEEMVKDQETTAEQALEEEA--RRHREAYGKLEREKATEVELLNARVQQLEEENTELRTT-VTRLKSQTEKLDEE 453
Cdd:pfam09744 47 EHNVELEELREDNEQLETQYEREKAlrKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADhVSRLEEKEAELKKE 126
|
90 100
....*....|....*....|
gi 28195388 454 RQRMSDRLEDTSLRLKDEMD 473
Cdd:pfam09744 127 YSKLHERETEVLRKLKEVVD 146
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-571 |
1.78e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 383 EEMVKDQETTAEQAL---EEEARRHREAY-------GKLEREKA--TEVELLN---------ARVQQLEEENTELRTTVT 441
Cdd:COG3096 450 EQQATEEVLELEQKLsvaDAARRQFEKAYelvckiaGEVERSQAwqTARELLRryrsqqalaQRLQQLRAQLAELEQRLR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 442 RLKSQTEKLDEERQRMS------DRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE--------- 506
Cdd:COG3096 530 QQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqd 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28195388 507 -LEHLqmykldCERPGRGRSASSGLGEFnaRAREVELEHEVKRLKQEnykLRDQNDDLNGQILSLS 571
Cdd:COG3096 610 aLERL------REQSGEALADSQEVTAA--MQQLLEREREATVERDE---LAARKQALESQIERLS 664
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
340-557 |
1.84e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 340 ITEKVSFLEKKVTELendSLTNGDLKSKLKQENTQLVHRVHELEEM-------VKDQETTAEQALEEearrhreayGKLE 412
Cdd:pfam15905 120 LSASVASLEKQLLEL---TRVNELLKAKFSEDGTQKKMSSLSMELMklrnkleAKMKEVMAKQEGME---------GKLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 413 rEKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMS---DRLEDTSLRLKDEMDLYKRMMDKLRQNRLEF 489
Cdd:pfam15905 188 -VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELScvsEQVEKYKLDIAQLEELLKEKNDEIESLKQSL 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28195388 490 QKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASsglgefnaRAREVE-LEHEVKRLKQENYKLR 557
Cdd:pfam15905 267 EEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQT--------LNAELEeLKEKLTLEEQEHQKLQ 327
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
333-499 |
1.95e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 333 IDSCDNDITEKVSFLEKKVTELENDSLTngdLKSKLKQENTQLVHRVHELEEmvkdQETTAEQALEEEARRHREA----- 407
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASSS---LGSDLAAREDALNQSLKELMH----QARTVLKARTEAHFNNNEEvtaal 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 408 -----YGKLEREKATEVELLNARVQQLEEENTELRTTVTR----LKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRM 478
Cdd:TIGR00618 775 qtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY 854
|
170 180
....*....|....*....|.
gi 28195388 479 MDKLRQNRLEFQKEREATQEL 499
Cdd:TIGR00618 855 EECSKQLAQLTQEQAKIIQLS 875
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
382-564 |
1.99e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 382 LEEMVKDQETTAEQAlEEEARRHREAYG--KLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD 459
Cdd:COG3206 180 LEEQLPELRKELEEA-EAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 460 RLEDTSL-RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcERPGRGRSASSGLGEfNARAR 538
Cdd:COG3206 259 LLQSPVIqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------QEAQRILASLEAELE-ALQAR 328
|
170 180
....*....|....*....|....*.
gi 28195388 539 EVELEHEVKRLKQENYKLRDQNDDLN 564
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELR 354
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-611 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 378 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 457
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 458 SDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgRGRSAssgLGEFNARA 537
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE----------REIEA---LGPVNLLA 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28195388 538 REvELEHEVKRLKqenyKLRDQNDDLNGQILSLslyeaknlfaaqtkaQSLAAEIDTASRDELMEALkeqEEIN 611
Cdd:COG1196 787 IE-EYEELEERYD----FLSEQREDLEEARETL---------------EEAIEEIDRETRERFLETF---DAVN 837
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
366-551 |
2.26e-03 |
|
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: 41.26 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 366 SKLKQENT--QLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRL 443
Cdd:pfam05557 367 KELTMSNYspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 444 KSQTEKLDEERQRMSDRLEDTSLR-----LKDEMDLYKRMMDKLRQNRLefQKEREATQELIEDLRKELEHL----QMYK 514
Cdd:pfam05557 447 RRKLETLELERQRLREQKNELEMElerrcLQGDYDPKKTKVLHLSMNPA--AEAYQQRKNQLEKLQAEIERLkrllKKLE 524
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 28195388 515 LDCERPGRGRSASSGLG--EFNARAREVE-LEHEVKRLKQ 551
Cdd:pfam05557 525 DDLEQVLRLPETTSTMNfkEVLDLRKELEsAELKNQRLKE 564
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
413-616 |
2.45e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 413 REKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYkrmmdklrqNRLEFQKE 492
Cdd:PRK10246 415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL---------ADVKTICE 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 493 REATQELIEDLRKELEHLQMYKL--DCERPGRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQIL-- 568
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQALEPGV--NQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQrd 563
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28195388 569 ---SLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 616
Cdd:PRK10246 564 eseAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRL 614
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
367-507 |
2.50e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 39.66 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 367 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQ 446
Cdd:pfam04012 54 QLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28195388 447 TEKL--DEERQRMSDRLEDT--SLRLKDEMDLYKRMMDKlrqnrlefQKEREATQELIEDLRKEL 507
Cdd:pfam04012 134 KNLLkaRLKAAKAQEAVQTSlgSLSTSSATDSFERIEEK--------IEEREARADAAAELASAV 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
417-609 |
2.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 417 TEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTslrlkdemdlykrmmdklrqnrlefQKEREAT 496
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-------------------------QAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 497 QELIEDLRKELEHLQ---------MYKldcerpgRGRSA--------SSGLGEFNARA--------REVELEHEVKRLKQ 551
Cdd:COG3883 71 QAEIAEAEAEIEERReelgeraraLYR-------SGGSVsyldvllgSESFSDFLDRLsalskiadADADLLEELKADKA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 552 ENYKLRDQNDDlngqilslslyEAKNLFAAQTKAQSLAAEIDT--ASRDELMEALKEQEE 609
Cdd:COG3883 144 ELEAKKAELEA-----------KLAELEALKAELEAAKAELEAqqAEQEALLAQLSAEEA 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-550 |
3.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 383 EEMVKDQETTAEQALEEEARRHREaYGKLEREKATEVELLNARVQQLE---EENTELRTTVTRLKSQTEKLDEERQRMSD 459
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 460 RLEDTSLRLKD---------EMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRGRSASSGL 530
Cdd:PRK03918 267 RIEELKKEIEEleekvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE------ERIKELEEKEERL 340
|
170 180
....*....|....*....|
gi 28195388 531 GEFnaRAREVELEHEVKRLK 550
Cdd:PRK03918 341 EEL--KKKLKELEKRLEELE 358
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-611 |
3.55e-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: 40.44 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 395 QALEEEARRHREaygKLEREKA--------------TEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 460
Cdd:TIGR02169 190 DLIIDEKRQQLE---RLRREREkaeryqallkekreYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 461 LEDTSLRLKdemDLYKRMMDKLRQNRLEFQKEreatqelIEDLRKELEHLQMYKLDCERPGRgrsassglgefNARAREV 540
Cdd:TIGR02169 267 LEEIEQLLE---ELNKKIKDLGEEEQLRVKEK-------IGELEAEIASLERSIAEKERELE-----------DAEERLA 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28195388 541 ELEHEVKRLKQENYKLRDQNDDLNGQILSLSlYEAKNLFAAQTKAQSLAAEIDT---ASRDELMEALKEQEEIN 611
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLT-EEYAELKEELEDLRAELEEVDKefaETRDELKDYREKLEKLK 398
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
347-608 |
3.70e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 347 LEKKVTELEndsLTNGDLKSKLKQE---NTQLVHRVHELEEMVKDQEttaEQALEEEARRHreaygKLEREKATevelLN 423
Cdd:pfam01576 66 LAARKQELE---EILHELESRLEEEeerSQQLQNEKKKMQQHIQDLE---EQLDEEEAARQ-----KLQLEKVT----TE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 424 ARVQQLEEEntelrttVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKrMMDKLRqnrlefQKEREATQELIEDL 503
Cdd:pfam01576 131 AKIKKLEED-------ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAK-SLSKLK------NKHEAMISDLEERL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 504 RKELEHLQmykldcerpgrgrsassglgefnararevELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKN---LFA 580
Cdd:pfam01576 197 KKEEKGRQ-----------------------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKeeeLQA 247
|
250 260
....*....|....*....|....*...
gi 28195388 581 AQTKaqslaAEIDTASRDELMEALKEQE 608
Cdd:pfam01576 248 ALAR-----LEEETAQKNNALKKIRELE 270
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
347-628 |
4.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 347 LEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEmvkdQETTAEQALEEEARRHREAYGKLEREKATevelLNARV 426
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSE----LEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 427 QQLEEENTELRTTVTRLKSQTEKLdEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 506
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEEL-ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 507 LEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQ----NDDLNGQILSLSLYEAKNLFAAQ 582
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESlpreLAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 28195388 583 TKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKIILAILDH 628
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
342-558 |
5.35e-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: 40.03 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 342 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVhrvhelEEMVKDQETTAEQALEEEARRHREAYGKlEREKA---TE 418
Cdd:TIGR00606 255 KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE------LKMEKVFQGTDEQLNDLYHNHQRTVREK-ERELVdcqRE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 419 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEE-RQRMSDRLEdtsLRLKDEMDLYKRMMDKLRQ--NRLEFQKEREA 495
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHiRARDSLIQS---LATRLELDGFERGPFSERQikNFHTLVIERQE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 496 TQ-----ELIEDL--RKELEHLQMYKLDCERPGRGRSASSglgefnaraREVELEHEVKRLKQENYKLRD 558
Cdd:TIGR00606 405 DEaktaaQLCADLqsKERLKQEQADEIRDEKKGLGRTIEL---------KKEILEKKQEELKFVIKELQQ 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-505 |
5.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 342 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATevel 421
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 422 LNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTslrlkdemdlykrmMDKLRQNRLEFQKEREATQELIE 501
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIA 429
|
....
gi 28195388 502 DLRK 505
Cdd:COG4913 430 SLER 433
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
386-552 |
6.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 386 VKDQETTAEQALEEeARRHREAYGKLEREKATEvELLNARvQQLEEENTELRttvtrlksqtekldEERQRMSDRLEDTS 465
Cdd:PRK12704 33 IKEAEEEAKRILEE-AKKEAEAIKKEALLEAKE-EIHKLR-NEFEKELRERR--------------NELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 466 LRLKDEMDLYKRmmdklRQNRLEFQKER-EATQELIEDLRKELEHLQMYKLD-CERpgrgrsaSSGLGEFNARAR----- 538
Cdd:PRK12704 96 ENLDRKLELLEK-----REEELEKKEKElEQKQQELEKKEEELEELIEEQLQeLER-------ISGLTAEEAKEIllekv 163
|
170
....*....|....*...
gi 28195388 539 EVELEHE----VKRLKQE 552
Cdd:PRK12704 164 EEEARHEaavlIKEIEEE 181
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
327-565 |
6.24e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 327 DLFRDSIDSCDNDITEKVSFLEKKVTELEND---------------SLTNGDLKSKLKQENTQLVHRVHELEEMVKDQET 391
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKKSRLEEKIREIEIEvkdidekivdlkkrkEYLESEEINKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 392 TAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDE 471
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD----DKSY 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 472 MDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRGRSASSGLGEFNARAREVElehevKRLKQ 551
Cdd:PRK01156 617 IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYK------KQIAEIDSIIPDLKEITSRINDIE-----DNLKK 685
|
250
....*....|....
gi 28195388 552 ENYKLRDQNDDLNG 565
Cdd:PRK01156 686 SRKALDDAKANRAR 699
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
356-499 |
6.25e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 356 NDSLTNGDLKSKLKQENTQLVHRVHELEEmvkdqettaEQaleEEARRHREAYGKLEREKATEVELLN---ARVQQL--- 429
Cdd:PRK10929 99 PPNMSTDALEQEILQVSSQLLEKSRQAQQ---------EQ---DRAREISDSLSQLPQQQTEARRQLNeieRRLQTLgtp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 430 -----EEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLkdemDLYKRMMDKLR------QNRLEFQKEREATQE 498
Cdd:PRK10929 167 ntplaQAQLTALQAESAALKALVDELELAQLSANNRQELARLRS----ELAKKRSQQLDaylqalRNQLNSQRQREAERA 242
|
.
gi 28195388 499 L 499
Cdd:PRK10929 243 L 243
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
378-616 |
6.38e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 378 RVHELEEMV---KDQETTAEQALEEEARR---HREAYGKLEREKATeVELLNARVQQLEEENTELRTtvtRLKSQTEKLD 451
Cdd:COG3096 383 RLEAAEEEVdslKSQLADYQQALDVQQTRaiqYQQAVQALEKARAL-CGLPDLTPENAEDYLAAFRA---KEQQATEEVL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 452 EERQRMSDRlEDTSLRLKDEMDLYKRMMDK-------------LRQNR-LEFQKEREAT--QELiEDLRKELEHLQ---- 511
Cdd:COG3096 459 ELEQKLSVA-DAARRQFEKAYELVCKIAGEversqawqtarelLRRYRsQQALAQRLQQlrAQL-AELEQRLRQQQnaer 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 512 MYKLDCERPGRGRSASSGLGEFNARAREV--ELEHEVKRLKQENYKLRDQNDDLNGQILSLSLyEAKNLFAAQTKAQSLA 589
Cdd:COG3096 537 LLEEFCQRIGQQLDAAEELEELLAELEAQleELEEQAAEAVEQRSELRQQLEQLRARIKELAA-RAPAWLAAQDALERLR 615
|
250 260
....*....|....*....|....*....
gi 28195388 590 AEIDT--ASRDELMEALKEQEEinfRLRQ 616
Cdd:COG3096 616 EQSGEalADSQEVTAAMQQLLE---RERE 641
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
339-567 |
6.66e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 339 DITEKVSFLEKKVTELEndsltngDLKSKLKQENTqLVHRVHELEEMVKDQETTAEQAlEEEARRHREAYGKLErekaTE 418
Cdd:PRK02224 486 DLEEEVEEVEERLERAE-------DLVEAEDRIER-LEERREDLEELIAERRETIEEK-RERAEELRERAAELE----AE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 419 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMsDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 498
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRT----LLAAIADAEDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28195388 499 LIEDLR---KELEHlqmyKLDCERPGrgrsassglgefNARAREVELEHEVKRLKQENYKLRDQNDDLNGQI 567
Cdd:PRK02224 628 RLAEKRerkRELEA----EFDEARIE------------EAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
347-628 |
6.81e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 347 LEKKVTELENdsltngdLKSKLKQENTQLVHRVHELEEmvKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARV 426
Cdd:COG4372 54 LEQAREELEQ-------LEEELEQARSELEQLEEELEE--LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 427 QQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 506
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 507 LEHLQMYKLDCERpgRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQ 586
Cdd:COG4372 205 AEKLIESLPRELA--EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 28195388 587 SLAAEIDTASRDELMEALKEQEEINFRLRQYMDKIILAILDH 628
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-456 |
7.64e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 367 KLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQ 446
Cdd:COG4717 150 ELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90
....*....|
gi 28195388 447 TEKLDEERQR 456
Cdd:COG4717 229 LEQLENELEA 238
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
419-507 |
8.57e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 38.53 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 419 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDL------YKRMMDKLRQNRLEFQKE 492
Cdd:pfam15294 128 SALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVksnlkeISDLEEKMAALKSDLEKT 207
|
90
....*....|....*
gi 28195388 493 REATQELIEDLRKEL 507
Cdd:pfam15294 208 LNASTALQKSLEEDL 222
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
340-563 |
9.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 340 ITEKVSFLEKKVTELENdSLTNGDLKSKLKQENTQL--------VHRVHELEEMVKDQETTAEQALEEEARRhREAYGKL 411
Cdd:PRK03918 471 IEEKERKLRKELRELEK-VLKKESELIKLKELAEQLkeleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28195388 412 EREKATEVEL--LNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEF 489
Cdd:PRK03918 549 EKLEELKKKLaeLEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28195388 490 QKEREATQEL---IEDLRKELEHLQMyKLDCErpgrgrsassglgEF-NARAREVELEHEVKRLKQENYKLRDQNDDL 563
Cdd:PRK03918 629 DKAFEELAETekrLEELRKELEELEK-KYSEE-------------EYeELREEYLELSRELAGLRAELEELEKRREEI 692
|
|
| |
