|
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 ... |
494-534 |
5.97e-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: 63.13 E-value: 5.97e-13
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 756140942 494 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 534
Cdd:pfam09457 1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
236-519 |
2.37e-10 |
|
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: 63.54 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 236 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHRE----------- 304
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 305 --AYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 379
Cdd:TIGR02168 767 eeRLEEAEEELAEaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 380 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 456
Cdd:TIGR02168 847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756140942 457 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 519
Cdd:TIGR02168 923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-514 |
2.84e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 237 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 316
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 317 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 396
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 397 LIEDLRKELEHLQMykldcerpgrgrsassglGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLyEAKNL 476
Cdd:COG1196 380 ELEELAEELLEALR------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEE 440
|
250 260 270
....*....|....*....|....*....|....*...
gi 756140942 477 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 514
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-409 |
6.85e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 267 KQENTQLVHRVHELEEMVKD-----QETTAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTRL 341
Cdd:COG4717 87 EEEYAELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEEL 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756140942 342 KSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 409
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
236-409 |
7.35e-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: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 236 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQET--TAEQALEEEARRHREAYGKLEREK 313
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEEL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 314 ATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD-EMDLYKRMMDKLRQNRLEFQKERE 392
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457
|
170
....*....|....*..
gi 756140942 393 ATQELIEDLRKELEHLQ 409
Cdd:TIGR02168 458 RLEEALEELREELEEAE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
240-513 |
3.22e-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: 53.52 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 240 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREAYGKLEREK 313
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 314 atevELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 393
Cdd:TIGR02168 319 ----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 394 TQELIEDLRKELEhlqmykldcerpgrgrsassglgefNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE- 472
Cdd:TIGR02168 391 LELQIASLNNEIE-------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEl 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 756140942 473 -------AKNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 513
Cdd:TIGR02168 446 eeeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
261-508 |
3.88e-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: 53.15 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 261 DLKSKLKQENTQLVHRVHELEEMVKDqettAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTR 340
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 341 LKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNRLEFQKE-REATQEL------IEDLRKELEHLQMYK 412
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARlREIEQKLnrltleKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 413 LDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSlyeaKNLFAAQTKAQSLAAEIDT 492
Cdd:TIGR02169 843 IDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE----AQLRELERKIEELEAQIEK 914
|
250
....*....|....*.
gi 756140942 493 AsrDELMEALKEQEEI 508
Cdd:TIGR02169 915 K--RKRLSELKAKLEA 928
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
280-414 |
5.85e-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: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 280 LEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRl 359
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 756140942 360 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRKELEHL-QMYKLD 414
Cdd:COG2433 457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-404 |
6.07e-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: 52.38 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 229 DSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ------ALEEEARRH 302
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgDLKKERDEL 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 303 REAYGKLER----------EKATEVELLNARVQQLEEENTELRTTVTRLKSQT------EKLDEERQRMSDR---LEDTS 363
Cdd:TIGR02169 895 EAQLRELERkieeleaqieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEiraLEPVN 974
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 756140942 364 LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 404
Cdd:TIGR02169 975 MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-510 |
6.40e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 237 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 315
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 316 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 393
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 394 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 473
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 756140942 474 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 510
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-406 |
7.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 239 TEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAE-QALEEEARRHREAYGKLEREKAT-- 315
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 316 ----EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEM--DLYKR----MMDKLRQN-R 384
Cdd:COG4913 689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERElR 768
|
170 180
....*....|....*....|..
gi 756140942 385 LEFQKEREATQELIEDLRKELE 406
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
285-409 |
1.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 285 KDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSL 364
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 756140942 365 RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 409
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-519 |
1.73e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 279 ELEEMVKDQETTAEQalEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 358
Cdd:TIGR02168 233 RLEELREELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 359 ---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCER----------PGRGRSAS 425
Cdd:TIGR02168 311 lanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqleTLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 426 SGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQ 505
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250
....*....|....
gi 756140942 506 EEINFRLRQYMDKI 519
Cdd:TIGR02168 471 EEAEQALDAAEREL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-409 |
2.68e-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: 50.45 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 267 KQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTE 346
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 756140942 347 KLD------EERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 409
Cdd:TIGR02169 393 KLEklkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
265-514 |
3.49e-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: 50.07 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 265 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRL 341
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 342 KSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRG 421
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRD----KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK------REINEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 422 RSASSGLGEFNARARE--VELEHEVKRLKQENYKLRDQNDDLngqilslslyeAKNLFAAQTKAQSLAAEIDTAsRDELM 499
Cdd:TIGR02169 405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDK-----------ALEIKKQEWKLEQLAADLSKY-EQELY 472
|
250
....*....|....*
gi 756140942 500 EALKEQEEINFRLRQ 514
Cdd:TIGR02169 473 DLKEEYDRVEKELSK 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-409 |
4.43e-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: 48.99 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 228 RDSIDSCDNDITEKVSFLEKKVTELENDSLTN----GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEE------ 297
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 298 ---EARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 374
Cdd:COG4942 130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 756140942 375 RMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 409
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
291-507 |
7.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 291 AEQAL------EEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTS- 363
Cdd:COG1196 209 AEKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 364 ---------LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgrgrsASSGLGEFNAR 434
Cdd:COG1196 289 eeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--------------EELEEAEEELE 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756140942 435 AREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEE 507
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
248-410 |
8.04e-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: 47.71 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 248 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 322
Cdd:pfam04849 97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 323 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 397
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239
|
170
....*....|...
gi 756140942 398 IEDLRKELEHLQM 410
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
293-509 |
5.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 293 QALEEEARRHREAYGKLEREKATEVELLNA--RVQQLEEENTELRTTVTRLksqtEKLDEERQRM---SDRLEdtslRLK 367
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREI----AELEAELERLdasSDDLA----ALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 368 DEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASsglgEFNARAREVELEHEVKRL 447
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756140942 448 KQEnykLRDQNDDLNGQILSLS--LYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEIN 509
Cdd:COG4913 768 REN---LEERIDALRARLNRAEeeLERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
292-472 |
5.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 292 EQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD-------------- 357
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreeleklekllql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 358 -----RLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRKELEHLQMyKLDCERPGRGRSASSGLGEfn 432
Cdd:COG4717 128 lplyqELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEELEE-- 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 756140942 433 ARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE 472
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
240-409 |
6.21e-05 |
|
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: 45.94 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 240 EKVSfLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ-----------ALEEEARRHREAYGK 308
Cdd:pfam01576 125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknkheamISDLEERLKKEEKGR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 309 LEREKATevellnarvQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR------- 381
Cdd:pfam01576 204 QELEKAK---------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIReleaqis 274
|
170 180 190
....*....|....*....|....*....|.
gi 756140942 382 --QNRLEFQK-EREATQELIEDLRKELEHLQ 409
Cdd:pfam01576 275 elQEDLESERaARNKAEKQRRDLGEELEALK 305
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
263-457 |
7.23e-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: 45.50 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 263 KSKLKQENTQ--LVHRVHELEEMVKDQETTAE---QALEEEARRHREAYGKLEREKATEVEllnaRVQQLEEENTELRTT 337
Cdd:pfam17380 403 KVKILEEERQrkIQQQKVEMEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 338 VTRLKSQTEKLDEERQRMsdrledtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQELI--EDLRKELEHLQMYKLDC 415
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKI----------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEM 548
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 756140942 416 ERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQ 457
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
267-532 |
7.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 267 KQENTQLVHRVHELEEMVKDQET-TAEQALEEEARRHR-----EAYGKLEREKATEVELLNARVQQLEEENTELRTTVTR 340
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKkKAEEAKKAEEDKNMalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 341 LKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLyKRMMDKLRQNRLEFQKEREATQELIEDLRKELEH----LQMYKLDCE 416
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 417 RPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRD 496
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
250 260 270
....*....|....*....|....*....|....*.
gi 756140942 497 ELMEALKEQEEinfRLRQYMDKIILAILDHNPSILE 532
Cdd:PTZ00121 1780 VIEEELDEEDE---KRRMEVDKKIKDIFDNFANIIE 1812
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-488 |
8.31e-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: 45.14 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 261 DLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEArrhreaygKLEREKATEVELLNARVQQLEEENTELRTTVTR 340
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 341 LKSQTEKLDEERQRMSDRL-----------------EDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRK 403
Cdd:COG4942 92 IAELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 404 ELEHLQMYKLDCERpgRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNlfAAQTKA 483
Cdd:COG4942 172 ERAELEALLAELEE--ERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPA 245
|
....*
gi 756140942 484 QSLAA 488
Cdd:COG4942 246 AGFAA 250
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
297-513 |
1.16e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 297 EEARRHREAYGKLEREKATEVELLNARVQQLEEEN-----TELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL----- 366
Cdd:PRK02224 169 ERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeehee 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 367 -KDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLqmykldcERPGRGRSASSGLGEFNARA---REVELEH 442
Cdd:PRK02224 249 rREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAveaRREELED 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756140942 443 EVKRLKQENYKLRDQNDDLNGQILSLsLYEAKNLFAAQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 513
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-450 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 276 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREkATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 355
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 356 SDRLEDTSLRLKDEMdlyKRMMDKLRQNRLEFQKEREATQELIEDL-------RKELEHLQmyKLDCERPGRGRSASSGL 428
Cdd:COG4913 329 EAQIRGNGGDRLEQL---EREIERLERELEERERRRARLEALLAALglplpasAEEFAALR--AEAAALLEALEEELEAL 403
|
170 180
....*....|....*....|....
gi 756140942 429 GE--FNARAREVELEHEVKRLKQE 450
Cdd:COG4913 404 EEalAEAEAALRDLRRELRELEAE 427
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
266-417 |
2.00e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 266 LKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQT 345
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756140942 346 EKLDEERQRMSDRLEdtslrlkdemdlykrmmdklrqnRLEFQKEREATQELIEDLRKELEH--LQMYKLDCER 417
Cdd:PRK12705 119 LELEELEKQLDNELY-----------------------RVAGLTPEQARKLLLKLLDAELEEekAQRVKKIEEE 169
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
267-406 |
2.29e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 267 KQENTQLVHRVHELEEMVKDQETTAEQALEE-EARRHreaYGKLEREKATEVELLNARVQQLEEENTELRttvtrlKSQT 345
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQElEAARK---VKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREV 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756140942 346 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELE 406
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
185-519 |
2.59e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 185 LEARLKNLKANSPNRKISSTAFGRQLMHSSNFSSSNGSTEDLFRDSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKS 264
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 265 KLKQENTQL-VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKS 343
Cdd:pfam02463 768 ELSLKEKELaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 344 QTEKLDEERQRmsDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpgrgrs 423
Cdd:pfam02463 848 LEKLAEEELER--LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK----------------- 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 424 assglgEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEAL- 502
Cdd:pfam02463 909 ------LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEe 982
|
330
....*....|....*....
gi 756140942 503 --KEQEEINFRLRQYMDKI 519
Cdd:pfam02463 983 feEKEERYNKDELEKERLE 1001
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-366 |
2.87e-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: 42.60 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 237 DITEKVSFLEKKVTELENDSltnGDLKSKLKQENTQL--VHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 312
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRriSDLEDEILELMERIEELEEE 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 756140942 313 KATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL 366
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
243-407 |
3.24e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 243 SFLEKKVTELENDSltngdlKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNA 322
Cdd:PRK12704 27 KIAEAKIKEAEEEA------KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 323 RVQQLEEENTELRTTVTRLKSQTEKLDEERQRmsdrledtslrlkdemdlYKRMMDKLRQnRLE----FQKErEATQELI 398
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEE------------------LEELIEEQLQ-ELErisgLTAE-EAKEILL 160
|
....*....
gi 756140942 399 EDLRKELEH 407
Cdd:PRK12704 161 EKVEEEARH 169
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
251-510 |
6.15e-04 |
|
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: 42.75 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 251 ELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKA------------TEVE 318
Cdd:COG5244 394 EDNKDVTLILKILHPILETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQdnrlflypscdiTLSS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 319 LLNARVQ-------QLEEENTELRTTVTRLKSQTEKLDE---ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRL--E 386
Cdd:COG5244 474 ILTILFSdklevffQGIESLLENITIFPEQPSQQTSDSEnikENSLLSDRLNEENIRLKEVLVQKENMLTEETKIKIiiG 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 387 FQKEREATQELIEDLRKELEHLQMyKLDCERPgrgrsassglgefnararevELEHEVKRLKQENYKLRDQNDDlnGQIL 466
Cdd:COG5244 554 RDLERKTLEENIKTLKVELNNKNN-KLKEENF--------------------NLVNRLKNMELKLYQIKDNNTL--NKIY 610
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 756140942 467 SLSLYEAKNL--FAAQTKAQSLAAEIDTASRDELMEALKE--QEEINF 510
Cdd:COG5244 611 LDLVSEIMELreTIRRQIKEQKRVSIDFSWLDELKQPFKEhiIEMFNF 658
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-408 |
6.19e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 238 ITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQA-----LEEEARRHREAYGKLERE 312
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyikLSEFYEEYLDELREIEKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 313 KAT-------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMsDRLEDTSLRLKD-EMDLYKRMMD 378
Cdd:PRK03918 316 LSRleeeingieerikELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLTGlTPEKLEKELE 394
|
170 180 190
....*....|....*....|....*....|
gi 756140942 379 KLRQNRLEFQKEREATQELIEDLRKELEHL 408
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
245-404 |
6.51e-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: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 245 LEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEqALEEEARRHREAYGKLERE---KATEVELLN 321
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKIKQNLEQKQKElksKEKELKKLN 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 322 ARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLED------------TSLRLKDEMDLYKRMMDKLRQNRLEFQK 389
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
170
....*....|....*
gi 756140942 390 EREATQELIEDLRKE 404
Cdd:TIGR04523 583 KQEEKQELIDQKEKE 597
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
277-505 |
7.51e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 277 VHELEEMVKDQETTAEQALEEEARRHREAYGKLERE-KATEVEllnaRVQQLEEENTELRTTVTR---LKSQTEKLDEER 352
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEeKAREVE----RRRKLEEAEKARQAEMDRqaaIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 353 QRMSDRLedtslRLKDEmdlyKRMMDKLRQNRL--EFQKERE------ATQELIEDLRKELEHLQMYKLDCERPGRGRSA 424
Cdd:pfam17380 347 ERELERI-----RQEER----KRELERIRQEEIamEISRMRElerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 425 SSGLGEF------NARAREV-----ELEHEVKRLKQENY-------KLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSL 486
Cdd:pfam17380 418 QKVEMEQiraeqeEARQREVrrleeERAREMERVRLEEQerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
250
....*....|....*....
gi 756140942 487 AAEIDTASRDELMEALKEQ 505
Cdd:pfam17380 498 EKELEERKQAMIEEERKRK 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-358 |
1.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 245 LEKKVTELENDSLTN-GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNAR 323
Cdd:COG4913 321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAA-LGLPLPASAEEFAALRAEAAALLEALEEE 399
|
90 100 110
....*....|....*....|....*....|....*
gi 756140942 324 VQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 358
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
310-510 |
1.32e-03 |
|
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: 41.13 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 310 EREKATEVELLNARVQQLEEENTElrtTVTRLKSQTEKLDEERQRMSDRLE-----------DTSLRLKDEMDLYKRMMD 378
Cdd:NF033928 100 KRGDLTEEELSELPPIPLSSDDKE---IVKELKEILEDLKNDIKDYQQKADdvkkelddfenDLREELLPQLKLKKKLYD 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 379 KLRQNrlefqKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEF-----------NARAREVELEHEVKRL 447
Cdd:NF033928 177 DNLGS-----DSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTGLAGGPIGLAitggifgskaeKIRKEKNALIQEIDEL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756140942 448 KQenyKLRDQN------DDLNGQILSLSLYEAKNLFAAQTKA---QSLAAEIDtASRDELMEALKEQEEINF 510
Cdd:NF033928 252 QE---QLKKKNallgslERLQTSLDDILTRMEDALPALKKLKgvwQSLLTDID-SSINALKEIDDADSLRLF 319
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
311-514 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 311 REKATEVelLNARVQQLEEENTELRTTVTRlkSQTEKLDEERQRMSDRLEDTSLRLKD------------EMDLYKRMMD 378
Cdd:COG3206 147 PELAAAV--ANALAEAYLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 379 KLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcERPGRGRSASSGLGEFNARAREVELEHEVKRLKQ---ENY--- 452
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLG---------SGPDALPELLQSPVIQQLRAQLAELEAELAELSArytPNHpdv 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756140942 453 -KLRDQNDDLNGQILSLSlyeAKNLFAAQTKAQSLAAEIDT--ASRDELMEALKEQEEINFRLRQ 514
Cdd:COG3206 294 iALRAQIAALRAQLQQEA---QRILASLEAELEALQAREASlqAQLAQLEARLAELPELEAELRR 355
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
268-522 |
1.77e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 41.12 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 268 QENTQLVHRVHELEEMVKDQETTAEQALEEEARRhreaygklerekaTEVELLNARVQQLEEENT----ELRTTVTRLKS 343
Cdd:PRK10361 26 QHAQQKAEQLAEREEMVAELSAAKQQITQSEHWR-------------AECELLNNEVRSLQSINTsleaDLREVTTRMEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 344 -QTEKLDEERQRMSdrledTSLRLKDEMD-LYKRMMDKlrQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpGRG 421
Cdd:PRK10361 93 aQQHADDKIRQMIN-----SEQRLSEQFEnLANRIFEH--SNRRVDEQNRQSLNSLLSPLREQLD------------GFR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 422 RSASSGLGEfNARAREVeLEHEVKRLKQENYKLRDQNDDLN-------------GQILSLSLYEAKNLFAAQTKAQSLAA 488
Cdd:PRK10361 154 RQVQDSFGK-EAQERHT-LAHEIRNLQQLNAQMAQEAINLTralkgdnktqgnwGEVVLTRVLEASGLREGYEYETQVSI 231
|
250 260 270
....*....|....*....|....*....|....
gi 756140942 489 EIDTASRdelmealkEQEEINFRLRQYMDKIILA 522
Cdd:PRK10361 232 ENDARSR--------MQPDVIVRLPQGKDVVIDA 257
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
240-371 |
2.09e-03 |
|
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: 38.82 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 240 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALeeearrhreaygklerEKATEVEL 319
Cdd:pfam12718 14 ERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESE----------------KLKTNNEN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 756140942 320 LNARVQQLEEE----NTELRTTVTRLKsQTEKLDEERQRMSDRLEDTSLRLKDEMD 371
Cdd:pfam12718 78 LTRKIQLLEEEleesDKRLKETTEKLR-ETDVKAEHLERKVQALEQERDEWEKKYE 132
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
293-409 |
2.13e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 293 QALEEEARRHREAYGKLEREkatevellnarVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD---- 368
Cdd:COG1579 13 QELDSELDRLEHRLKELPAE-----------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeq 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 756140942 369 ---------------EMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 409
Cdd:COG1579 82 lgnvrnnkeyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
235-408 |
2.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 235 DNDITEKVSFLEKKVTELENDSltngdlkSKLKQENTQLVHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 312
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLEEHEERREelETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 313 KAT---EVELLNARVQQLEEENTELRTTV-------TRLKSQTEKLDEERQRMSDRLEDTSL----------RLKDEMDL 372
Cdd:PRK02224 274 REElaeEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVaaqahneeaeSLREDADD 353
|
170 180 190
....*....|....*....|....*....|....*.
gi 756140942 373 YKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHL 408
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
272-404 |
2.52e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.51 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 272 QLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLerekATEVELLNARVQQLEEENTELRTTVTRLK-----SQTE 346
Cdd:pfam07111 506 QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASV----GQQLEVARQGQQESTEEAASLRQELTQQQeiygqALQE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 756140942 347 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQE---LIEDLRKE 404
Cdd:pfam07111 582 KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQElrrLQDEARKE 642
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
292-519 |
2.57e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 292 EQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSdRLEDTSLRLKDEMD 371
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK-ELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 372 LYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGE-FNARAREVELEHEVKRLKQE 450
Cdd:COG1340 89 ELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKeLEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 756140942 451 NYKLRDQNDDLNGQILSLS--LYEAKNLFAAQ-TKAQSLAAEIDTASR--DELMEALKEQE----EINFRLRQYMDKI 519
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAeeAQELHEEMIELyKEADELRKEADELHKeiVEAQEKADELHeeiiELQKELRELRKEL 246
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
293-409 |
2.81e-03 |
|
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: 40.05 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 293 QALEEEARRHREAYGKLEREKATE-----VELLNARVQQLEEENTELRTTVTRLKSQTEK----LDEERQRMSDRLEDTS 363
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKdqtaLETLEKALKDLLTDEG 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 756140942 364 LRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRKELEHLQ 409
Cdd:cd22656 174 GAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-470 |
2.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 267 KQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYgkLEREKATEVELLNARVQQLEEENtELRTTVTRLKSQTE 346
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 347 KLDEERQRMSDRLEDTSLRLKDEmdlykrmmdklrqnrlEFQKEREATQELIEDLRKElehlqmykldcerpgrgrsass 426
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELE----------------ELEEELEELEEELEELREE---------------------- 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 756140942 427 gLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSL 470
Cdd:COG4717 455 -LAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
274-385 |
2.92e-03 |
|
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: 38.00 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 274 VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLERE---KATEVELLnarvQQLEEENTELRTTVTRLKSQTEKLDE 350
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlHAEDIKAL----QALREELNELKAEIAELKAEAESAKA 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 756140942 351 ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR-QNRL 385
Cdd:pfam07926 86 ELEESEESWEEQKKELEKELSELEKRIEDLNeQNKL 121
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
281-469 |
3.41e-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: 40.32 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 281 EEMVKDQETTAEQAL---EEEARRHREAY-------GKLEREKA--TEVELLN---------ARVQQLEEENTELRTTVT 339
Cdd:COG3096 450 EQQATEEVLELEQKLsvaDAARRQFEKAYelvckiaGEVERSQAwqTARELLRryrsqqalaQRLQQLRAQLAELEQRLR 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 340 RLKSQTEKLDEERQRMS------DRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE--------- 404
Cdd:COG3096 530 QQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqd 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 756140942 405 -LEHLqmykldCERPGRGRSASSGLGEFnaRAREVELEHEVKRLKQEnykLRDQNDDLNGQILSLS 469
Cdd:COG3096 610 aLERL------REQSGEALADSQEVTAA--MQQLLEREREATVERDE---LAARKQALESQIERLS 664
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-509 |
3.43e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 276 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 355
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 356 SDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgRGRSAssgLGEFNARA 435
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE----------REIEA---LGPVNLLA 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756140942 436 REvELEHEVKRLKqenyKLRDQNDDLNGQILSLslyeaknlfaaqtkaQSLAAEIDTASRDELMEALkeqEEIN 509
Cdd:COG1196 787 IE-EYEELEERYD----FLSEQREDLEEARETL---------------EEAIEEIDRETRERFLETF---DAVN 837
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
275-371 |
3.63e-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: 37.98 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 275 HRVHELEEMVKDQETTAEQALEEEA--RRHREAYGKLEREKATEVELLNARVQQLEEENTELRTT-VTRLKSQTEKLDEE 351
Cdd:pfam09744 47 EHNVELEELREDNEQLETQYEREKAlrKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADhVSRLEEKEAELKKE 126
|
90 100
....*....|....*....|
gi 756140942 352 RQRMSDRLEDTSLRLKDEMD 371
Cdd:pfam09744 127 YSKLHERETEVLRKLKEVVD 146
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
280-462 |
4.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 280 LEEMVKDQETTAEQAlEEEARRHREAYG--KLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD 357
Cdd:COG3206 180 LEEQLPELRKELEEA-EAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 358 RLEDTSL-RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcERPGRGRSASSGLGEfNARAR 436
Cdd:COG3206 259 LLQSPVIqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------QEAQRILASLEAELE-ALQAR 328
|
170 180
....*....|....*....|....*.
gi 756140942 437 EVELEHEVKRLKQENYKLRDQNDDLN 462
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELR 354
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
311-514 |
6.04e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.40 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 311 REKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYkrmmdklrqNRLEFQKE 390
Cdd:PRK10246 415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL---------ADVKTICE 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 391 REATQELIEDLRKELEHLQMYKL--DCERPGRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQIL-- 466
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQALEPGV--NQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQrd 563
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 756140942 467 ---SLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 514
Cdd:PRK10246 564 eseAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRL 614
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
240-403 |
6.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 240 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATevel 319
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 320 LNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTslrlkdemdlykrmMDKLRQNRLEFQKEREATQELIE 399
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIA 429
|
....
gi 756140942 400 DLRK 403
Cdd:COG4913 430 SLER 433
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
265-405 |
7.08e-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: 38.12 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 265 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQ 344
Cdd:pfam04012 54 QLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756140942 345 TEKL--DEERQRMSDRLEDT--SLRLKDEMDLYKRMMDKlrqnrlefQKEREATQELIEDLRKEL 405
Cdd:pfam04012 134 KNLLkaRLKAAKAQEAVQTSlgSLSTSSATDSFERIEEK--------IEEREARADAAAELASAV 190
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
254-397 |
8.47e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.88 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 254 NDSLTNGDLKSKLKQENTQLVHRVHELEEmvkdqettaEQaleEEARRHREAYGKLEREKATEVELLN---ARVQQL--- 327
Cdd:PRK10929 99 PPNMSTDALEQEILQVSSQLLEKSRQAQQ---------EQ---DRAREISDSLSQLPQQQTEARRQLNeieRRLQTLgtp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 328 -----EEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLkdemDLYKRMMDKLR------QNRLEFQKEREATQE 396
Cdd:PRK10929 167 ntplaQAQLTALQAESAALKALVDELELAQLSANNRQELARLRS----ELAKKRSQQLDaylqalRNQLNSQRQREAERA 242
|
.
gi 756140942 397 L 397
Cdd:PRK10929 243 L 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
284-450 |
8.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 284 VKDQETTAEQALEEeARRHREAYGKLEREKATEvELLNARvQQLEEENTELRttvtrlksqtekldEERQRMSDRLEDTS 363
Cdd:PRK12704 33 IKEAEEEAKRILEE-AKKEAEAIKKEALLEAKE-EIHKLR-NEFEKELRERR--------------NELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 364 LRLKDEMDLYKRmmdklRQNRLEFQKER-EATQELIEDLRKELEHLQMYKLD-CERpgrgrsaSSGLGEFNARAR----- 436
Cdd:PRK12704 96 ENLDRKLELLEK-----REEELEKKEKElEQKQQELEKKEEELEELIEEQLQeLER-------ISGLTAEEAKEIllekv 163
|
170
....*....|....*...
gi 756140942 437 EVELEHE----VKRLKQE 450
Cdd:PRK12704 164 EEEARHEaavlIKEIEEE 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
281-448 |
9.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 281 EEMVKDQETTAEQALEEEARRHREaYGKLEREKATEVELLNARVQQLE---EENTELRTTVTRLKSQTEKLDEERQRMSD 357
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756140942 358 RLEDTSLRLKD---------EMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRGRSASSGL 428
Cdd:PRK03918 267 RIEELKKEIEEleekvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE------ERIKELEEKEERL 340
|
170 180
....*....|....*....|
gi 756140942 429 GEFnaRAREVELEHEVKRLK 448
Cdd:PRK03918 341 EEL--KKKLKELEKRLEELE 358
|
|
| |
